{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,27]],"date-time":"2026-07-27T07:59:29Z","timestamp":1785139169994,"version":"3.55.0"},"reference-count":160,"publisher":"Springer Science and Business Media LLC","issue":"7","license":[{"start":{"date-parts":[[2026,6,13]],"date-time":"2026-06-13T00:00:00Z","timestamp":1781308800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"},{"start":{"date-parts":[[2026,6,13]],"date-time":"2026-06-13T00:00:00Z","timestamp":1781308800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"}],"funder":[{"DOI":"10.13039\/501100006087","name":"Direcci\u00f3n General de Asuntos del Personal Acad\u00e9mico, Universidad Nacional Aut\u00f3noma de M\u00e9xico","doi-asserted-by":"publisher","award":["DGAPA IN203225"],"award-info":[{"award-number":["DGAPA IN203225"]}],"id":[{"id":"10.13039\/501100006087","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Arch Virol"],"published-print":{"date-parts":[[2026,7]]},"DOI":"10.1007\/s00705-026-06669-3","type":"journal-article","created":{"date-parts":[[2026,6,13]],"date-time":"2026-06-13T06:14:27Z","timestamp":1781331267000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["The role of DPP4 in viral infections: from receptor biology to antiviral target"],"prefix":"10.1007","volume":"171","author":[{"ORCID":"https:\/\/orcid.org\/0009-0002-6490-5506","authenticated-orcid":false,"given":"Catalina","family":"Aguilera-Flores","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-3130-4501","authenticated-orcid":false,"given":"Carlos F.","family":"Arias","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2026,6,13]]},"reference":[{"issue":"3","key":"6669_CR1","doi-asserted-by":"publisher","first-page":"333","DOI":"10.1016\/0167-4781(92)90036-Y","volume":"1131","author":"Y Misumi","year":"1992","unstructured":"Misumi Y, Hayashi Y, Arakawa F, Ikehara Y (1992) Molecular cloning and sequence analysis of human dipeptidyl peptidase IV, a serine proteinase on the cell surface. Biochim Biophys Acta 1131(3):333\u2013336. https:\/\/doi.org\/10.1016\/0167-4781(92)90036-Y","journal-title":"Biochim Biophys Acta"},{"issue":"5","key":"6669_CR2","doi-asserted-by":"publisher","first-page":"G763","DOI":"10.1152\/ajpgi.1991.261.5.G763","volume":"261","author":"D Darmoul","year":"1991","unstructured":"Darmoul D, Rouyer-Fessard C, Blais A et al (1991) Dipeptidyl peptidase IV expression in rat jejunal crypt-villus axis is controlled at mRNA level. Am J Physiol 261(5):G763\u2013G769. https:\/\/doi.org\/10.1152\/ajpgi.1991.261.5.G763","journal-title":"Am J Physiol"},{"issue":"2","key":"6669_CR3","doi-asserted-by":"publisher","first-page":"481","DOI":"10.4049\/jimmunol.149.2.481","volume":"149","author":"T Tanaka","year":"1992","unstructured":"Tanaka T, Camerini D, Seed B et al (1992) Cloning and functional expression of the T cell activation antigen CD26. J Immunol 149(2):481\u2013486. https:\/\/doi.org\/10.4049\/jimmunol.149.2.481","journal-title":"J Immunol"},{"issue":"1","key":"6669_CR4","doi-asserted-by":"publisher","first-page":"205","DOI":"10.1016\/0008-8749(91)90343-A","volume":"134","author":"MD Gorrell","year":"1991","unstructured":"Gorrell MD, Wickson J, McCaughan GW (1991) Expression of the rat CD26 Antigen (dipeptidyl peptidase IV) on subpopulations of rat lymphocytes. Cell Immunol 134(1):205\u2013215. https:\/\/doi.org\/10.1016\/0008-8749(91)90343-A","journal-title":"Cell Immunol"},{"issue":"1\u20132","key":"6669_CR5","doi-asserted-by":"publisher","first-page":"47","DOI":"10.1016\/0165-2478(94)00230-O","volume":"45","author":"F B\u00fchling","year":"1995","unstructured":"B\u00fchling F, Junker U, Reinhold D et al (1995) Functional role of CD26 on human B lymphocytes. Immunol Lett 45(1\u20132):47\u201351. https:\/\/doi.org\/10.1016\/0165-2478(94)00230-O","journal-title":"Immunol Lett"},{"issue":"1","key":"6669_CR6","doi-asserted-by":"publisher","first-page":"256","DOI":"10.1016\/0014-4827(89)90296-6","volume":"182","author":"W Hong","year":"1989","unstructured":"Hong W, Petell JK, Swank D et al (1989) Expression of dipeptidyl peptidase IV in rat tissues is mainly regulated at the mRNA levels. Exp Cell Res 182(1):256\u2013266. https:\/\/doi.org\/10.1016\/0014-4827(89)90296-6","journal-title":"Exp Cell Res"},{"issue":"9","key":"6669_CR7","doi-asserted-by":"publisher","first-page":"546","DOI":"10.1007\/s00262-003-0392-9","volume":"52","author":"K Shingu","year":"2003","unstructured":"Shingu K, Helfritz A, Zielinska-Skowronek M et al (2003) CD26 expression determines lung metastasis in mutant F344 rats: involvement of NK cell function and soluble CD26. Cancer Immunol Immunother 52(9):546\u2013554. https:\/\/doi.org\/10.1007\/s00262-003-0392-9","journal-title":"Cancer Immunol Immunother"},{"issue":"5","key":"6669_CR8","doi-asserted-by":"publisher","first-page":"331","DOI":"10.1007\/BF01246674","volume":"40","author":"CA Abbott","year":"1994","unstructured":"Abbott CA, McCaughan GW, Baker E, Sutherland GR (1994) Genomic organization, exact localization, and tissue expression of the human CD26 (dipeptidyl peptidase IV) gene. Immunogenetics 40(5):331\u2013338. https:\/\/doi.org\/10.1007\/BF01246674","journal-title":"Immunogenetics"},{"issue":"1","key":"6669_CR9","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1111\/cei.12781","volume":"185","author":"C Klemann","year":"2016","unstructured":"Klemann C, Wagner L, Stephan M, von H\u00f6rsten S (2016) Cut to the chase: a review of CD26\/dipeptidyl peptidase-4\u2019s (DPP4) entanglement in the immune system. Clin Exp Immunol 185(1):1\u201321. https:\/\/doi.org\/10.1111\/cei.12781","journal-title":"Clin Exp Immunol"},{"key":"6669_CR10","doi-asserted-by":"publisher","first-page":"D227","DOI":"10.1093\/nar\/gkp971","volume":"38","author":"ND Rawlings","year":"2010","unstructured":"Rawlings ND, Barrett AJ, Bateman A (2010) MEROPS: the peptidase database. Nucleic Acids Res 38:D227\u2013D233. https:\/\/doi.org\/10.1093\/nar\/gkp971","journal-title":"Nucleic Acids Res"},{"issue":"1","key":"6669_CR11","doi-asserted-by":"publisher","first-page":"9","DOI":"10.1016\/S0167-0115(99)00089-0","volume":"85","author":"R Mentlein","year":"1999","unstructured":"Mentlein R (1999) Dipeptidyl-peptidase IV (CD26)-role in the inactivation of regulatory peptides. Regul Pept 85(1):9\u201324. https:\/\/doi.org\/10.1016\/S0167-0115(99)00089-0","journal-title":"Regul Pept"},{"issue":"1","key":"6669_CR12","doi-asserted-by":"publisher","first-page":"19","DOI":"10.1038\/nsb882","volume":"10","author":"HB Rasmussen","year":"2003","unstructured":"Rasmussen HB, Branner S, Wiberg FC, Wagtmann N (2003) Crystal structure of human dipeptidyl peptidase IV\/CD26 in complex with a substrate analog. Nat Struct Biol 10(1):19\u201325. https:\/\/doi.org\/10.1038\/nsb882","journal-title":"Nat Struct Biol"},{"issue":"4","key":"6669_CR13","doi-asserted-by":"publisher","first-page":"849","DOI":"10.1016\/S0006-291X(03)00258-4","volume":"302","author":"H Hiramatsu","year":"2003","unstructured":"Hiramatsu H, Kyono K, Higashiyama Y et al (2003) The structure and function of human dipeptidyl peptidase IV, possessing a unique eight-bladed \u03b2-propeller fold. Biochem Biophys Res Commun 302(4):849\u2013854. https:\/\/doi.org\/10.1016\/S0006-291X(03)00258-4","journal-title":"Biochem Biophys Res Commun"},{"issue":"2","key":"6669_CR14","doi-asserted-by":"publisher","first-page":"412","DOI":"10.1110\/ps.03460604","volume":"13","author":"K Aertgeerts","year":"2004","unstructured":"Aertgeerts K, Ye S, Tennant MG et al (2004) Crystal structure of human dipeptidyl peptidase IV in complex with a decapeptide reveals details on substrate specificity and tetrahedral intermediate formation. Protein Sci 13(2):412\u2013421. https:\/\/doi.org\/10.1110\/ps.03460604","journal-title":"Protein Sci"},{"issue":"2","key":"6669_CR15","doi-asserted-by":"publisher","first-page":"215","DOI":"10.1016\/S0167-4838(97)00045-9","volume":"1340","author":"A-M Lambeir","year":"1997","unstructured":"Lambeir A-M, D\u0131\u0301az Pereira JF, Chac\u00f3n P et al (1997) A prediction of DPP IV\/CD26 domain structure from a physico-chemical investigation of dipeptidyl peptidase IV (CD26) from human seminal plasma. Biochim Biophys Acta 1340(2):215\u2013226. https:\/\/doi.org\/10.1016\/S0167-4838(97)00045-9","journal-title":"Biochim Biophys Acta"},{"issue":"9","key":"6669_CR16","doi-asserted-by":"publisher","first-page":"5063","DOI":"10.1073\/pnas.0230620100","volume":"100","author":"M Engel","year":"2003","unstructured":"Engel M, Hoffmann T, Wagner L et al (2003) The crystal structure of dipeptidyl peptidase IV (CD26) reveals its functional regulation and enzymatic mechanism. Proc Natl Acad Sci U S A 100(9):5063\u20135068. https:\/\/doi.org\/10.1073\/pnas.0230620100","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"21","key":"6669_CR17","doi-asserted-by":"publisher","first-page":"3870","DOI":"10.1016\/j.febslet.2014.08.029","volume":"588","author":"D R\u00f6hrborn","year":"2014","unstructured":"R\u00f6hrborn D, Eckel J, Sell H (2014) Shedding of dipeptidyl peptidase 4 is mediated by metalloproteases and up-regulated by hypoxia in human adipocytes and smooth muscle cells. FEBS Lett 588(21):3870\u20133877. https:\/\/doi.org\/10.1016\/j.febslet.2014.08.029","journal-title":"FEBS Lett"},{"issue":"21","key":"6669_CR18","doi-asserted-by":"publisher","first-page":"8110","DOI":"10.3390\/ijms21218110","volume":"21","author":"LR Moffitt","year":"2020","unstructured":"Moffitt LR, Bilandzic M, Wilson AL et al (2020) Hypoxia Regulates DPP4 Expression, Proteolytic Inactivation, and Shedding from Ovarian Cancer Cells. Int J Mol Sci 21(21):8110. https:\/\/doi.org\/10.3390\/ijms21218110","journal-title":"Int J Mol Sci"},{"issue":"11","key":"6669_CR19","doi-asserted-by":"publisher","first-page":"1529","DOI":"10.1016\/j.molmet.2017.09.004","volume":"6","author":"T Nargis","year":"2017","unstructured":"Nargis T, Kumar K, Ghosh AR et al (2017) KLK5 induces shedding of DPP4 from circulatory Th17 cells in type 2 diabetes. Mol Metab 6(11):1529\u20131539. https:\/\/doi.org\/10.1016\/j.molmet.2017.09.004","journal-title":"Mol Metab"},{"issue":"2","key":"6669_CR20","doi-asserted-by":"publisher","first-page":"112","DOI":"10.1002\/iub.1709","volume":"70","author":"T Nargis","year":"2018","unstructured":"Nargis T, Chakrabarti P (2018) Significance of circulatory DPP4 activity in metabolic diseases. IUBMB Life 70(2):112\u2013119. https:\/\/doi.org\/10.1002\/iub.1709","journal-title":"IUBMB Life"},{"key":"6669_CR21","doi-asserted-by":"publisher","unstructured":"Wagner L (2018) Dipeptidyl Peptidase 4. In: Choi S (ed) Encyclopedia of Signaling Molecules. Springer. https:\/\/doi.org\/10.1007\/978-3-319-67199-4_101580Cham.1383\u20131396","DOI":"10.1007\/978-3-319-67199-4_101580"},{"issue":"8","key":"6669_CR22","doi-asserted-by":"publisher","first-page":"2026","DOI":"10.3390\/biomedicines10082026","volume":"10","author":"A Sebasti\u00e1n-Mart\u00edn","year":"2022","unstructured":"Sebasti\u00e1n-Mart\u00edn A, S\u00e1nchez BG, Mora-Rodr\u00edguez JM, Bort A, D\u00edaz-Laviada I (2022) Role of Dipeptidyl Peptidase-4 (DPP4) on COVID-19 Physiopathology. Biomedicines 10(8):2026. https:\/\/doi.org\/10.3390\/biomedicines10082026","journal-title":"Biomedicines"},{"issue":"6","key":"6669_CR23","doi-asserted-by":"publisher","first-page":"992","DOI":"10.1210\/er.2014-1035","volume":"35","author":"EE Mulvihill","year":"2014","unstructured":"Mulvihill EE, Drucker DJ (2014) Pharmacology, Physiology, and Mechanisms of Action of Dipeptidyl Peptidase-4 Inhibitors. Endocr Rev 35(6):992\u20131019. https:\/\/doi.org\/10.1210\/er.2014-1035","journal-title":"Endocr Rev"},{"issue":"2","key":"6669_CR24","doi-asserted-by":"publisher","first-page":"257","DOI":"10.1016\/j.peptides.2006.09.027","volume":"28","author":"N Frerker","year":"2007","unstructured":"Frerker N, Wagner L, Wolf R et al (2007) Neuropeptide Y (NPY) cleaving enzymes: Structural and functional homologues of dipeptidyl peptidase 4. Peptides (NY) 28(2):257\u2013268. https:\/\/doi.org\/10.1016\/j.peptides.2006.09.027","journal-title":"Peptides (NY)"},{"issue":"2","key":"6669_CR25","doi-asserted-by":"publisher","first-page":"133","DOI":"10.1016\/0167-0115(93)90435-B","volume":"49","author":"R Mentlein","year":"1993","unstructured":"Mentlein R, Dahms P, Grandt D, Kr\u00fcger R (1993) Proteolytic processing of neuropeptide Y and peptide YY by dipeptidyl peptidase IV. Regul Pept 49(2):133\u2013144. https:\/\/doi.org\/10.1016\/0167-0115(93)90435-B","journal-title":"Regul Pept"},{"issue":"2","key":"6669_CR26","doi-asserted-by":"publisher","first-page":"417","DOI":"10.1016\/0005-2744(78)90237-1","volume":"525","author":"T Kato","year":"1978","unstructured":"Kato T, Nagatsu T, Fukasawa K et al (1978) Successive cleavage of N-terminal Arg1-Pro2 and Lys3-Pro4 from substance P but no release of Arg1-Pro2 from bradykinin, by X-Pro dipeptidyl-aminopeptidase. Biochim Biophys Acta 525(2):417\u2013422. https:\/\/doi.org\/10.1016\/0005-2744(78)90237-1","journal-title":"Biochim Biophys Acta"},{"issue":"2","key":"6669_CR27","doi-asserted-by":"publisher","first-page":"360","DOI":"10.1016\/0014-5793(78)81210-1","volume":"91","author":"E Heymann","year":"1978","unstructured":"Heymann E, Mentlein R (1978) Liver dipeptidyl aminopeptidase IV hydrolyzes substance P. FEBS Lett 91(2):360\u2013364. https:\/\/doi.org\/10.1016\/0014-5793(78)81210-1","journal-title":"FEBS Lett"},{"key":"6669_CR28","doi-asserted-by":"publisher","first-page":"21","DOI":"10.1016\/j.npep.2016.02.007","volume":"57","author":"L Wagner","year":"2016","unstructured":"Wagner L, Kaestner F, Wolf R et al (2016) Identifying neuropeptide Y (NPY) as the main stress-related substrate of dipeptidyl peptidase 4 (DPP4) in blood circulation. Neuropeptides 57:21\u201334. https:\/\/doi.org\/10.1016\/j.npep.2016.02.007","journal-title":"Neuropeptides"},{"issue":"7","key":"6669_CR29","doi-asserted-by":"publisher","first-page":"673","DOI":"10.1038\/nbt0797-673","volume":"15","author":"DJ Drucker","year":"1997","unstructured":"Drucker DJ, Shi Q, Crivici A et al (1997) Regulation of the biological activity of glucagon-like peptide 2 in vivo by dipeptidyl peptidase IV. Nat Biotechnol 15(7):673\u2013677. https:\/\/doi.org\/10.1038\/nbt0797-673","journal-title":"Nat Biotechnol"},{"issue":"8","key":"6669_CR30","doi-asserted-by":"publisher","first-page":"3585","DOI":"10.1210\/endo.136.8.7628397","volume":"136","author":"TJ Kieffer","year":"1995","unstructured":"Kieffer TJ, McIntosh CH, Pederson RA (1995) Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV. Endocrinology 136(8):3585\u20133596. https:\/\/doi.org\/10.1210\/endo.136.8.7628397","journal-title":"Endocrinology"},{"issue":"3","key":"6669_CR31","doi-asserted-by":"publisher","first-page":"829","DOI":"10.1111\/j.1432-1033.1993.tb17986.x","volume":"214","author":"R Mentlein","year":"1993","unstructured":"Mentlein R, Gallwitz B, Schmidt WE (1993) Dipeptidyl-peptidase IV hydrolyses gastric inhibitory polypeptide, glucagon\u2010like peptide\u20101(7\u201336)amide, peptide histidine methionine and is responsible for their degradation in human serum. Eur J Biochem 214(3):829\u2013835. https:\/\/doi.org\/10.1111\/j.1432-1033.1993.tb17986.x","journal-title":"Eur J Biochem"},{"issue":"25","key":"6669_CR32","doi-asserted-by":"publisher","first-page":"22418","DOI":"10.1074\/jbc.M212355200","volume":"278","author":"L Zhu","year":"2003","unstructured":"Zhu L, Tamvakopoulos C, Xie D et al (2003) The Role of Dipeptidyl Peptidase IV in the Cleavage of Glucagon Family Peptides. J Biol Chem 278(25):22418\u201322423. https:\/\/doi.org\/10.1074\/jbc.M212355200","journal-title":"J Biol Chem"},{"issue":"5","key":"6669_CR33","doi-asserted-by":"publisher","first-page":"1533","DOI":"10.1172\/JCI114049","volume":"83","author":"LA Frohman","year":"1989","unstructured":"Frohman LA, Downs TR, Heimer EP, Felix AM (1989) Dipeptidylpeptidase IV and trypsin-like enzymatic degradation of human growth hormone-releasing hormone in plasma. J Clin Invest 83(5):1533\u20131540. https:\/\/doi.org\/10.1172\/JCI114049","journal-title":"J Clin Invest"},{"issue":"4","key":"6669_CR34","doi-asserted-by":"publisher","first-page":"906","DOI":"10.1172\/JCI112679","volume":"78","author":"LA Frohman","year":"1986","unstructured":"Frohman LA, Downs TR, Williams TC et al (1986) Rapid enzymatic degradation of growth hormone-releasing hormone by plasma in vitro and in vivo to a biologically inactive product cleaved at the NH2 terminus. J Clin Invest 78(4):906\u2013913. https:\/\/doi.org\/10.1172\/JCI112679","journal-title":"J Clin Invest"},{"issue":"4","key":"6669_CR35","doi-asserted-by":"publisher","first-page":"301","DOI":"10.59566\/IJBS.2010.6301","volume":"6","author":"CT Lin","year":"2010","unstructured":"Lin CT, Tang HY, Han YS et al (2010) Downregulation of Signaling-active IGF-1 by Dipeptidyl Peptidase IV (DPP-IV). Int J Biomed Sci 6(4):301","journal-title":"Int J Biomed Sci"},{"issue":"3","key":"6669_CR36","doi-asserted-by":"publisher","first-page":"327","DOI":"10.1016\/S0014-5793(01)02982-9","volume":"507","author":"A-M Lambeir","year":"2001","unstructured":"Lambeir A-M, Durinx C, Proost P et al (2001) Kinetic study of the processing by dipeptidyl-peptidase IV\/CD26 of neuropeptides involved in pancreatic insulin secretion. FEBS Lett 507(3):327\u2013330. https:\/\/doi.org\/10.1016\/S0014-5793(01)02982-9","journal-title":"FEBS Lett"},{"issue":"13","key":"6669_CR37","doi-asserted-by":"publisher","first-page":"7222","DOI":"10.1074\/jbc.273.13.7222","volume":"273","author":"P Proost","year":"1998","unstructured":"Proost P, De Meester I, Schols D et al (1998) Amino-terminal Truncation of Chemokines by CD26\/Dipeptidyl-peptidase IV. J Biol Chem 273(13):7222\u20137227. https:\/\/doi.org\/10.1074\/jbc.273.13.7222","journal-title":"J Biol Chem"},{"issue":"13","key":"6669_CR38","doi-asserted-by":"publisher","first-page":"3554","DOI":"10.1182\/blood.V98.13.3554","volume":"98","author":"P Proost","year":"2001","unstructured":"Proost P, Schutyser E, Menten P et al (2001) Amino-terminal truncation of CXCR3 agonists impairs receptor signaling and lymphocyte chemotaxis, while preserving antiangiogenic properties. Blood 98(13):3554\u20133561. https:\/\/doi.org\/10.1182\/blood.V98.13.3554","journal-title":"Blood"},{"issue":"1","key":"6669_CR39","doi-asserted-by":"publisher","first-page":"183","DOI":"10.1189\/jlb.72.1.183","volume":"72","author":"A Ludwig","year":"2002","unstructured":"Ludwig A, Schiemann F, Mentlein R, Lindner B, Brandt E (2002) Dipeptidyl peptidase IV (CD26) on T cells cleaves the CXC chemokine CXCL11 (I-TAC) and abolishes the stimulating but not the desensitizing potential of the chemokine. J Leukoc Biol 72(1):183\u2013191. https:\/\/doi.org\/10.1189\/jlb.72.1.183","journal-title":"J Leukoc Biol"},{"issue":"11","key":"6669_CR40","doi-asserted-by":"publisher","first-page":"6331","DOI":"10.1073\/pnas.95.11.6331","volume":"95","author":"T Shioda","year":"1998","unstructured":"Shioda T, Kato H, Ohnishi Y et al (1998) Anti-HIV-1 and chemotactic activities of human stromal cell-derived factor 1\u03b1 (SDF-1\u03b1) and SDF-1\u03b2 are abolished by CD26\/dipeptidyl peptidase IV-mediated cleavage. Proc Natl Acad Sci U S A 95(11):6331\u20136336. https:\/\/doi.org\/10.1073\/pnas.95.11.6331","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"1\u20132","key":"6669_CR41","doi-asserted-by":"publisher","first-page":"73","DOI":"10.1016\/S0014-5793(98)00830-8","volume":"432","author":"P Proost","year":"1998","unstructured":"Proost P, Struyf S, Schols D et al (1998) Processing by CD26\/dipeptidyl-peptidase IV reduces the chemotactic and anti\u2010HIV\u20101 activity of stromal\u2010cell\u2010derived factor\u20101\u03b1. FEBS Lett 432(1\u20132):73\u201376. https:\/\/doi.org\/10.1016\/S0014-5793(98)00830-8","journal-title":"FEBS Lett"},{"issue":"2","key":"6669_CR42","doi-asserted-by":"publisher","first-page":"236","DOI":"10.1016\/S0014-5793(98)00763-7","volume":"431","author":"T Ohtsuki","year":"1998","unstructured":"Ohtsuki T, Hosono O, Kobayashi H et al (1998) Negative regulation of the anti-human immunodeficiency virus and chemotactic activity of human stromal cell\u2010derived factor 1\u03b1 by CD26\/dipeptidyl peptidase IV. FEBS Lett 431(2):236\u2013240. https:\/\/doi.org\/10.1016\/S0014-5793(98)00763-7","journal-title":"FEBS Lett"},{"issue":"5","key":"6669_CR43","doi-asserted-by":"publisher","first-page":"1674","DOI":"10.1182\/blood.V96.5.1674","volume":"96","author":"P Proost","year":"2000","unstructured":"Proost P, Menten P, Struyf S et al (2000) Cleavage by CD26\/dipeptidyl peptidase IV converts the chemokine LD78\u03b2 into a most efficient monocyte attractant and CCR1 agonist. Blood 96(5):1674\u20131680. https:\/\/doi.org\/10.1182\/blood.V96.5.1674","journal-title":"Blood"},{"issue":"7","key":"6669_CR44","doi-asserted-by":"publisher","first-page":"2170","DOI":"10.1002\/1521-4141(200107)31:7<2170::AID-IMMU2170>3.0.CO;2-D","volume":"31","author":"S Struyf","year":"2001","unstructured":"Struyf S, Menten P, Lenaerts J-P et al (2001) Diverging binding capacities of natural LD78\u03b2 isoforms of macrophage inflammatory protein-1\u03b1 to the CC chemokine receptors 1, 3 and 5 affect their anti-HIV-1 activity and chemotactic potencies for neutrophils and eosinophils. Eur J Immunol 31(7):2170\u20132178. https:\/\/doi.org\/10.1002\/1521-4141(200107)31:7%3C2170::AID-IMMU2170%3E3.0.CO;2-D","journal-title":"Eur J Immunol"},{"issue":"1","key":"6669_CR45","doi-asserted-by":"publisher","first-page":"53","DOI":"10.1002\/jcb.20041","volume":"92","author":"E Guan","year":"2004","unstructured":"Guan E, Wang J, Norcross MA (2004) Amino-terminal processing of MIP\u20101\u03b2\/CCL4 by CD26\/dipeptidyl\u2010peptidase IV. J Cell Biochem 92(1):53\u201364. https:\/\/doi.org\/10.1002\/jcb.20041","journal-title":"J Cell Biochem"},{"issue":"3","key":"6669_CR46","doi-asserted-by":"publisher","first-page":"417","DOI":"10.1093\/intimm\/11.3.417","volume":"11","author":"S Iwata","year":"1999","unstructured":"Iwata S, Yamaguchi N, Munakata Y et al (1999) CD26\/dipeptidyl peptidase IV differentially regulates the chemotaxis of T cells and monocytes toward RANTES: possible mechanism for the switch from innate to acquired immune response. Int Immunol 11(3):417\u2013426. https:\/\/doi.org\/10.1093\/intimm\/11.3.417","journal-title":"Int Immunol"},{"issue":"3","key":"6669_CR47","doi-asserted-by":"publisher","first-page":"175","DOI":"10.1016\/S0166-3542(98)00039-4","volume":"39","author":"D Schols","year":"1998","unstructured":"Schols D, Proost P, Struyf S et al (1998) CD26-processed RANTES(3\u201368), but not intact RANTES, has potent anti-HIV-1 activity. Antiviral Res 39(3):175\u2013187. https:\/\/doi.org\/10.1016\/S0166-3542(98)00039-4","journal-title":"Antiviral Res"},{"issue":"3","key":"6669_CR48","doi-asserted-by":"publisher","first-page":"291","DOI":"10.1165\/ajrcmb.21.3.f160","volume":"21","author":"ME Rothenberg","year":"1999","unstructured":"Rothenberg ME (1999) Eotaxin: An Essential Mediator of Eosinophil Trafficking into Mucosal Tissues. Am J Respir Cell Mol Biol 21(3):291\u2013295. https:\/\/doi.org\/10.1165\/ajrcmb.21.3.f160","journal-title":"Am J Respir Cell Mol Biol"},{"issue":"2","key":"6669_CR49","doi-asserted-by":"publisher","first-page":"1229","DOI":"10.4049\/jimmunol.0802145","volume":"183","author":"R Richter","year":"2009","unstructured":"Richter R, Casarosa P, St\u00e4ndker L et al (2009) Significance of N-Terminal Proteolysis of CCL14a to Activity on the Chemokine Receptors CCR1 and CCR5 and the Human Cytomegalovirus-Encoded Chemokine Receptor US28. J Immunol 183(2):1229\u20131237. https:\/\/doi.org\/10.4049\/jimmunol.0802145","journal-title":"J Immunol"},{"issue":"7","key":"6669_CR50","doi-asserted-by":"publisher","first-page":"3988","DOI":"10.1074\/jbc.274.7.3988","volume":"274","author":"P Proost","year":"1999","unstructured":"Proost P, Struyf S, Schols D et al (1999) Truncation of Macrophage-derived Chemokine by CD26\/ Dipeptidyl-Peptidase IV beyond Its Predicted Cleavage Site Affects Chemotactic Activity and CC Chemokine Receptor 4 Interaction. J Biol Chem 274(7):3988\u20133993. https:\/\/doi.org\/10.1074\/jbc.274.7.3988","journal-title":"J Biol Chem"},{"issue":"4","key":"6669_CR51","doi-asserted-by":"publisher","first-page":"265","DOI":"10.1016\/j.ejcb.2011.06.001","volume":"91","author":"H Fan","year":"2012","unstructured":"Fan H, Tansi FL, Weihofen WA et al (2012) Molecular mechanism and structural basis of interactions of dipeptidyl peptidase IV with adenosine deaminase and human immunodeficiency virus type-1 transcription transactivator. Eur J Cell Biol 91(4):265\u2013273. https:\/\/doi.org\/10.1016\/j.ejcb.2011.06.001","journal-title":"Eur J Cell Biol"},{"issue":"5120","key":"6669_CR52","doi-asserted-by":"publisher","first-page":"466","DOI":"10.1126\/science.8101391","volume":"261","author":"J Kameoka","year":"1993","unstructured":"Kameoka J, Tanaka T, Nojima Y, Schlossman SF, Morimoto C (1993) Direct Association of Adenosine Deaminase with a T Cell Activation Antigen, CD26. Sci (1979) 261(5120):466\u2013469. https:\/\/doi.org\/10.1126\/science.8101391","journal-title":"Sci (1979)"},{"issue":"41","key":"6669_CR53","doi-asserted-by":"publisher","first-page":"43330","DOI":"10.1074\/jbc.M405001200","volume":"279","author":"WA Weihofen","year":"2004","unstructured":"Weihofen WA, Liu J, Reutter W, Saenger W, Fan H (2004) Crystal Structure of CD26\/Dipeptidyl-peptidase IV in Complex with Adenosine Deaminase Reveals a Highly Amphiphilic Interface. J Biol Chem 279(41):43330\u201343335. https:\/\/doi.org\/10.1074\/jbc.M405001200","journal-title":"J Biol Chem"},{"issue":"13","key":"6669_CR54","doi-asserted-by":"publisher","first-page":"10117","DOI":"10.1074\/jbc.M609157200","volume":"282","author":"K Ohnuma","year":"2007","unstructured":"Ohnuma K, Uchiyama M, Yamochi T et al (2007) Caveolin-1 Triggers T-cell Activation via CD26 in Association with CARMA1. J Biol Chem 282(13):10117\u201310131. https:\/\/doi.org\/10.1074\/jbc.M609157200","journal-title":"J Biol Chem"},{"issue":"2","key":"6669_CR55","doi-asserted-by":"publisher","first-page":"327","DOI":"10.1016\/j.bbrc.2009.06.027","volume":"386","author":"K Ohnuma","year":"2009","unstructured":"Ohnuma K, Uchiyama M, Hatano R et al (2009) Blockade of CD26-mediated T cell costimulation with soluble caveolin-1-Ig fusion protein induces anergy in CD4\u2009+\u2009T cells. Biochem Biophys Res Commun 386(2):327\u2013332. https:\/\/doi.org\/10.1016\/j.bbrc.2009.06.027","journal-title":"Biochem Biophys Res Commun"},{"issue":"1","key":"6669_CR56","doi-asserted-by":"publisher","first-page":"13","DOI":"10.1111\/j.1365-2249.2005.02683.x","volume":"139","author":"K Ohnuma","year":"2004","unstructured":"Ohnuma K, Yamochi T, Hosono O, Morimoto C (2004) CD26\u2009+\u2009T cells in the pathogenesis of asthma. Clin Exp Immunol 139(1):13\u201316. https:\/\/doi.org\/10.1111\/j.1365-2249.2005.02683.x","journal-title":"Clin Exp Immunol"},{"issue":"1","key":"6669_CR57","doi-asserted-by":"publisher","first-page":"341","DOI":"10.1006\/bbrc.1995.2782","volume":"217","author":"K Loster","year":"1995","unstructured":"Loster K, Zeilinger K, Schuppan D, Reutter W (1995) The Cysteine-Rich Region of Dipeptidyl Peptidase IV (CD 26) Is the Collagen Binding Site. Biochem Biophys Res Commun 217(1):341\u2013348. https:\/\/doi.org\/10.1006\/bbrc.1995.2782","journal-title":"Biochem Biophys Res Commun"},{"issue":"27","key":"6669_CR58","doi-asserted-by":"publisher","first-page":"24600","DOI":"10.1074\/jbc.M303424200","volume":"278","author":"H-C Cheng","year":"2003","unstructured":"Cheng H-C, Abdel-Ghany M, Pauli BU (2003) A Novel Consensus Motif in Fibronectin Mediates Dipeptidyl Peptidase IV Adhesion and Metastasis. J Biol Chem 278(27):24600\u201324607. https:\/\/doi.org\/10.1074\/jbc.M303424200","journal-title":"J Biol Chem"},{"issue":"2","key":"6669_CR59","doi-asserted-by":"publisher","first-page":"397","DOI":"10.1042\/0264-6021:3550397","volume":"355","author":"M Gonzalez-Gronow","year":"2001","unstructured":"Gonzalez-Gronow M, Grenett HE, Weber MR, Gawdi G, Pizzo SV (2001) Interaction of plasminogen with dipeptidyl peptidase IV initiates a signal transduction mechanism which regulates expression of matrix metalloproteinase-9 by prostate cancer cells. Biochem J 355(2):397. https:\/\/doi.org\/10.1042\/0264-6021:3550397","journal-title":"Biochem J"},{"issue":"6","key":"6669_CR60","doi-asserted-by":"publisher","first-page":"366","DOI":"10.1016\/S0268-9499(98)80395-0","volume":"12","author":"M Gonzalez-Gronow","year":"1998","unstructured":"Gonzalez-Gronow M, Weber MR, Shearin TV et al (1998) Plasmin(ogen) carbohydrate chains mediate binding to dipeptidyl peptidase IV (CD 26) in rheumatoid arthritis human synovial fibroblasts. Fibrinolysis Proteol 12(6):366\u2013374. https:\/\/doi.org\/10.1016\/S0268-9499(98)80395-0","journal-title":"Fibrinolysis Proteol"},{"issue":"3","key":"6669_CR61","doi-asserted-by":"publisher","first-page":"129","DOI":"10.1016\/S0268-9499(98)80294-4","volume":"12","author":"M Gonzalez-Gronow","year":"1998","unstructured":"Gonzalez-Gronow M, Weber MR, Gawdi G, Pizzo SV (1998) Dipeptidyl peptidase IV (CD26) is a receptor for streptokinase on rheumatoid synovial fibroblasts. Fibrinolysis Proteol 12(3):129\u2013135. https:\/\/doi.org\/10.1016\/S0268-9499(98)80294-4","journal-title":"Fibrinolysis Proteol"},{"issue":"6","key":"6669_CR62","doi-asserted-by":"publisher","first-page":"1253","DOI":"10.1128\/CDLI.9.6.1253-1259.2002","volume":"9","author":"M Cuchacovich","year":"2002","unstructured":"Cuchacovich M, Gatica H, Vial P et al (2002) Streptokinase Promotes Development of Dipeptidyl Peptidase IV (CD26) Autoantibodies after Fibrinolytic Therapy in Myocardial Infarction Patients. Clin Diagn Lab Immunol 9(6):1253\u20131259. https:\/\/doi.org\/10.1128\/CDLI.9.6.1253-1259.2002","journal-title":"Clin Diagn Lab Immunol"},{"issue":"2","key":"6669_CR63","doi-asserted-by":"publisher","first-page":"53","DOI":"10.1078\/0171-9335-00302","volume":"82","author":"E Boonacker","year":"2003","unstructured":"Boonacker E, Van Noorden CJF (2003) The multifunctional or moonlighting protein CD26\/DPPIV. Eur J Cell Biol 82(2):53\u201373. https:\/\/doi.org\/10.1078\/0171-9335-00302","journal-title":"Eur J Cell Biol"},{"key":"6669_CR64","doi-asserted-by":"publisher","first-page":"105757","DOI":"10.1016\/j.intimp.2019.105757","volume":"75","author":"Y Zhao","year":"2019","unstructured":"Zhao Y (2019) CD26 in autoimmune diseases: The other side of moonlight protein. Int Immunopharmacol 75:105757. https:\/\/doi.org\/10.1016\/j.intimp.2019.105757","journal-title":"Int Immunopharmacol"},{"key":"6669_CR65","doi-asserted-by":"publisher","first-page":"108947","DOI":"10.1016\/j.bioorg.2025.108947","volume":"165","author":"R Dutta","year":"2025","unstructured":"Dutta R, Khatun S, Ghosh P et al (2025) Exploring DPP-4: Implications in diverse diseases and structural insights for novel inhibitor design. Bioorg Chem 165:108947. https:\/\/doi.org\/10.1016\/j.bioorg.2025.108947","journal-title":"Bioorg Chem"},{"issue":"12","key":"6669_CR66","doi-asserted-by":"publisher","first-page":"2250302","DOI":"10.1002\/eji.202250302","volume":"53","author":"M Drakul","year":"2023","unstructured":"Drakul M, \u010coli\u0107 M (2023) Immunomodulatory activity of dipeptidyl peptidase-4 inhibitors in immune\u2010related diseases. Eur J Immunol 53(12):2250302. https:\/\/doi.org\/10.1002\/eji.202250302","journal-title":"Eur J Immunol"},{"key":"6669_CR67","doi-asserted-by":"publisher","first-page":"830863","DOI":"10.3389\/fimmu.2022.830863","volume":"13","author":"J Huang","year":"2022","unstructured":"Huang J, Liu X, Wei Y et al (2022) Emerging Role of Dipeptidyl Peptidase-4 in Autoimmune Disease. Front Immunol 13:830863. https:\/\/doi.org\/10.3389\/fimmu.2022.830863","journal-title":"Front Immunol"},{"issue":"23","key":"6669_CR68","doi-asserted-by":"publisher","first-page":"5947","DOI":"10.3390\/cancers13235947","volume":"13","author":"G Chitadze","year":"2021","unstructured":"Chitadze G, Wehkamp U, Janssen O, Br\u00fcggemann M, Lettau M (2021) The Serine Protease CD26\/DPP4 in Non-Transformed and Malignant T Cells. Cancers (Basel) 13(23):5947. https:\/\/doi.org\/10.3390\/cancers13235947","journal-title":"Cancers (Basel)"},{"key":"6669_CR69","doi-asserted-by":"publisher","first-page":"107503","DOI":"10.1016\/j.pharmthera.2020.107503","volume":"209","author":"S Shao","year":"2020","unstructured":"Shao S, Xu Q, Yu X, Pan R, Chen Y (2020) Dipeptidyl peptidase 4 inhibitors and their potential immune modulatory functions. Pharmacol Ther 209:107503. https:\/\/doi.org\/10.1016\/j.pharmthera.2020.107503","journal-title":"Pharmacol Ther"},{"issue":"6","key":"6669_CR70","doi-asserted-by":"publisher","first-page":"295","DOI":"10.1016\/j.it.2008.02.010","volume":"29","author":"K Ohnuma","year":"2008","unstructured":"Ohnuma K, Dang NH, Morimoto C (2008) Revisiting an old acquaintance: CD26 and its molecular mechanisms in T cell function. Trends Immunol 29(6):295\u2013301. https:\/\/doi.org\/10.1016\/j.it.2008.02.010","journal-title":"Trends Immunol"},{"issue":"21","key":"6669_CR71","doi-asserted-by":"publisher","first-page":"12138","DOI":"10.1073\/pnas.211439098","volume":"98","author":"T Ishii","year":"2001","unstructured":"Ishii T, Ohnuma K, Murakami A et al (2001) CD26-mediated signaling for T cell activation occurs in lipid rafts through its association with CD45RO. Proc Natl Acad Sci U S A 98(21):12138\u201312143. https:\/\/doi.org\/10.1073\/pnas.211439098","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"8","key":"6669_CR72","doi-asserted-by":"publisher","first-page":"2514","DOI":"10.4049\/jimmunol.147.8.2514","volume":"147","author":"Y Torimoto","year":"1991","unstructured":"Torimoto Y, Dang NH, Vivier E et al (1991) Coassociation of CD26 (dipeptidyl peptidase IV) with CD45 on the surface of human T lymphocytes. J Immunol 147(8):2514\u20132517. https:\/\/doi.org\/10.4049\/jimmunol.147.8.2514","journal-title":"J Immunol"},{"issue":"22","key":"6669_CR73","doi-asserted-by":"publisher","first-page":"19532","DOI":"10.1074\/jbc.M004586200","volume":"276","author":"C Herrera","year":"2001","unstructured":"Herrera C, Morimoto C, Blanco J et al (2001) Comodulation of CXCR4 and CD26 in Human Lymphocytes. J Biol Chem 276(22):19532\u201319539. https:\/\/doi.org\/10.1074\/jbc.M004586200","journal-title":"J Biol Chem"},{"issue":"15","key":"6669_CR74","doi-asserted-by":"publisher","first-page":"8439","DOI":"10.1073\/pnas.97.15.8439","volume":"97","author":"H Ikushima","year":"2000","unstructured":"Ikushima H, Munakata Y, Ishii T et al (2000) Internalization of CD26 by mannose 6-phosphate\/insulin-like growth factor II receptor contributes to T cell activation. Proc Natl Acad Sci U S A 97(15):8439\u20138444. https:\/\/doi.org\/10.1073\/pnas.97.15.8439","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"1","key":"6669_CR75","doi-asserted-by":"publisher","first-page":"106","DOI":"10.1016\/S0008-8749(02)00010-2","volume":"215","author":"H Ikushima","year":"2002","unstructured":"Ikushima H, Munakata Y, Iwata S et al (2002) Soluble CD26\/dipeptidyl peptidase IV enhances transendothelial migration via its interaction with mannose 6-phosphate\/insulin-like growth factor II receptor. Cell Immunol 215(1):106\u2013110. https:\/\/doi.org\/10.1016\/S0008-8749(02)00010-2","journal-title":"Cell Immunol"},{"issue":"4","key":"6669_CR76","doi-asserted-by":"publisher","first-page":"1349","DOI":"10.4049\/jimmunol.156.4.1349","volume":"156","author":"RP Dong","year":"1996","unstructured":"Dong RP, Kameoka J, Hegen M et al (1996) Characterization of adenosine deaminase binding to human CD26 on T cells and its biologic role in immune response. J Immunol 156(4):1349\u20131355. https:\/\/doi.org\/10.4049\/jimmunol.156.4.1349","journal-title":"J Immunol"},{"issue":"39","key":"6669_CR77","doi-asserted-by":"publisher","first-page":"14186","DOI":"10.1073\/pnas.0405266101","volume":"101","author":"K Ohnuma","year":"2004","unstructured":"Ohnuma K, Yamochi T, Uchiyama M et al (2004) CD26 up-regulates expression of CD86 on antigen-presenting cells by means of caveolin-1. Proc Natl Acad Sci U S A 101(39):14186\u201314191. https:\/\/doi.org\/10.1073\/pnas.0405266101","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"1\u20132","key":"6669_CR78","doi-asserted-by":"publisher","first-page":"123","DOI":"10.1016\/S0014-5793(00)01751-8","volume":"477","author":"J Blanco","year":"2000","unstructured":"Blanco J, Valenzuela A, Herrera C et al (2000) The HIV-1 gp120 inhibits the binding of adenosine deaminase to CD26 by a mechanism modulated by CD4 and CXCR4 expression. FEBS Lett 477(1\u20132):123\u2013128. https:\/\/doi.org\/10.1016\/S0014-5793(00)01751-8","journal-title":"FEBS Lett"},{"issue":"10","key":"6669_CR79","doi-asserted-by":"publisher","first-page":"851","DOI":"10.1089\/aid.1998.14.851","volume":"14","author":"RE SMITH","year":"1998","unstructured":"SMITH RE, TALHOUK JW, BROWN EE, EDGAR SE (1998) The Significance of Hypersialylation of Dipeptidyl Peptidase IV (CD26) in the Inhibition of Its Activity by Tat and Other Cationic Peptides. CD26: A Subverted Adhesion Molecule for HIV Peptide Binding. AIDS Res Hum Retroviruses 14(10):851\u2013868. https:\/\/doi.org\/10.1089\/aid.1998.14.851","journal-title":"AIDS Res Hum Retroviruses"},{"issue":"7440","key":"6669_CR80","doi-asserted-by":"publisher","first-page":"251","DOI":"10.1038\/nature12005","volume":"495","author":"VS Raj","year":"2013","unstructured":"Raj VS, Mou H, Smits SL et al (2013) Dipeptidyl peptidase 4 is a functional receptor for the emerging human coronavirus-EMC. Nature 495(7440):251\u2013254. https:\/\/doi.org\/10.1038\/nature12005","journal-title":"Nature"},{"issue":"16","key":"6669_CR81","doi-asserted-by":"publisher","first-page":"9379","DOI":"10.1128\/JVI.01277-13","volume":"87","author":"H Mou","year":"2013","unstructured":"Mou H, Raj VS, van Kuppeveld FJM et al (2013) The Receptor Binding Domain of the New Middle East Respiratory Syndrome Coronavirus Maps to a 231-Residue Region in the Spike Protein That Efficiently Elicits Neutralizing Antibodies. J Virol 87(16):9379\u20139383. https:\/\/doi.org\/10.1128\/JVI.01277-13","journal-title":"J Virol"},{"issue":"7461","key":"6669_CR82","doi-asserted-by":"publisher","first-page":"227","DOI":"10.1038\/nature12328","volume":"500","author":"G Lu","year":"2013","unstructured":"Lu G, Hu Y, Wang Q et al (2013) Molecular basis of binding between novel human coronavirus MERS-CoV and its receptor CD26. Nature 500(7461):227\u2013231. https:\/\/doi.org\/10.1038\/nature12328","journal-title":"Nature"},{"issue":"8","key":"6669_CR83","doi-asserted-by":"publisher","first-page":"986","DOI":"10.1038\/cr.2013.92","volume":"23","author":"N Wang","year":"2013","unstructured":"Wang N, Shi X, Jiang L et al (2013) Structure of MERS-CoV spike receptor-binding domain complexed with human receptor DPP4. Cell Res 23(8):986\u2013993. https:\/\/doi.org\/10.1038\/cr.2013.92","journal-title":"Cell Res"},{"issue":"4","key":"6669_CR84","doi-asserted-by":"publisher","first-page":"850","DOI":"10.1016\/j.cell.2023.01.019","volume":"186","author":"J Chen","year":"2023","unstructured":"Chen J, Yang X, Si H et al (2023) A bat MERS-like coronavirus circulates in pangolins and utilizes human DPP4 and host proteases for cell entry. Cell 186(4):850\u2013863e16. https:\/\/doi.org\/10.1016\/j.cell.2023.01.019","journal-title":"Cell"},{"issue":"3","key":"6669_CR85","doi-asserted-by":"publisher","first-page":"328","DOI":"10.1016\/j.chom.2014.08.009","volume":"16","author":"Q Wang","year":"2014","unstructured":"Wang Q, Qi J, Yuan Y et al (2014) Bat Origins of MERS-CoV Supported by Bat Coronavirus HKU4 Usage of Human Receptor CD26. Cell Host Microbe 16(3):328\u2013337. https:\/\/doi.org\/10.1016\/j.chom.2014.08.009","journal-title":"Cell Host Microbe"},{"issue":"1","key":"6669_CR86","doi-asserted-by":"publisher","first-page":"216","DOI":"10.1038\/s41467-020-20458-9","volume":"12","author":"SKP Lau","year":"2021","unstructured":"Lau SKP, Fan RYY, Zhu L et al (2021) Isolation of MERS-related coronavirus from lesser bamboo bats that uses DPP4 and infects human-DPP4-transgenic mice. Nat Commun 12(1):216. https:\/\/doi.org\/10.1038\/s41467-020-20458-9","journal-title":"Nat Commun"},{"key":"6669_CR87","doi-asserted-by":"publisher","unstructured":"Shi J, Hu S, Wei H et al (2024) Dipeptidyl peptidase 4 interacts with porcine coronavirus PHEV spikes and mediates host range expansion. J Virol 98(7). https:\/\/doi.org\/10.1128\/jvi.00753-24","DOI":"10.1128\/jvi.00753-24"},{"issue":"1","key":"6669_CR88","doi-asserted-by":"publisher","first-page":"308","DOI":"10.1172\/JCI40594","volume":"121","author":"A Casrouge","year":"2011","unstructured":"Casrouge A, Decalf J, Ahloulay M et al (2011) Evidence for an antagonist form of the chemokine CXCL10 in patients chronically infected with HCV. J Clin Invest 121(1):308\u2013317. https:\/\/doi.org\/10.1172\/JCI40594","journal-title":"J Clin Invest"},{"issue":"2","key":"6669_CR89","doi-asserted-by":"publisher","first-page":"487","DOI":"10.1002\/hep.27139","volume":"60","author":"A Riva","year":"2014","unstructured":"Riva A, Laird M, Casrouge A et al (2014) Truncated CXCL10 is associated with failure to achieve spontaneous clearance of acute hepatitis C infection. Hepatology 60(2):487\u2013496. https:\/\/doi.org\/10.1002\/hep.27139","journal-title":"Hepatology"},{"issue":"7","key":"6669_CR90","doi-asserted-by":"publisher","first-page":"e1013316","DOI":"10.1371\/journal.ppat.1013316","volume":"21","author":"C Aguilera-Flores","year":"2025","unstructured":"Aguilera-Flores C, Valencia-Morales M, del L\u00f3pez P T, et al (2025) Functional characterization of DPP4 and FcRn as receptor and coreceptor for classical human astroviruses in Caco-2 cells. PLoS Pathog 21(7):e1013316. https:\/\/doi.org\/10.1371\/journal.ppat.1013316","journal-title":"PLoS Pathog"},{"issue":"11","key":"6669_CR91","doi-asserted-by":"publisher","first-page":"983","DOI":"10.1111\/gtc.13160","volume":"29","author":"K Haga","year":"2024","unstructured":"Haga K, Tokui T, Miyamoto K et al (2024) Neonatal Fc receptor is a functional receptor for classical human astrovirus. Genes Cells 29(11):983\u20131001. https:\/\/doi.org\/10.1111\/gtc.13160","journal-title":"Genes Cells"},{"issue":"12","key":"6669_CR92","doi-asserted-by":"publisher","first-page":"3321","DOI":"10.1038\/s41564-024-01855-y","volume":"9","author":"H Ingle","year":"2024","unstructured":"Ingle H, Molleston JM, Hall PD et al (2024) The neonatal Fc receptor is a cellular receptor for human astrovirus. Nat Microbiol 9(12):3321\u20133331. https:\/\/doi.org\/10.1038\/s41564-024-01855-y","journal-title":"Nat Microbiol"},{"issue":"7","key":"6669_CR93","doi-asserted-by":"publisher","first-page":"291","DOI":"10.1089\/apc.2016.0100","volume":"30","author":"AW Woodham","year":"2016","unstructured":"Woodham AW, Skeate JG, Sanna AM et al (2016) Human Immunodeficiency Virus Immune Cell Receptors, Coreceptors, and Cofactors: Implications for Prevention and Treatment. AIDS Patient Care STDS 30(7):291\u2013306. https:\/\/doi.org\/10.1089\/apc.2016.0100","journal-title":"AIDS Patient Care STDS"},{"issue":"1","key":"6669_CR94","doi-asserted-by":"publisher","first-page":"42","DOI":"10.1038\/s41572-023-00452-3","volume":"9","author":"L-G Bekker","year":"2023","unstructured":"Bekker L-G, Beyrer C, Mgodi N et al (2023) HIV infection. Nat Rev Dis Primers 9(1):42. https:\/\/doi.org\/10.1038\/s41572-023-00452-3","journal-title":"Nat Rev Dis Primers"},{"issue":"6584","key":"6669_CR95","doi-asserted-by":"publisher","first-page":"667","DOI":"10.1038\/381667a0","volume":"381","author":"T Dragic","year":"1996","unstructured":"Dragic T, Litwin V, Allaway GP et al (1996) HIV-1 entry into CD4\u2009+\u2009cells is mediated by the chemokine receptor CC-CKR-5. Nature 381(6584):667\u2013673. https:\/\/doi.org\/10.1038\/381667a0","journal-title":"Nature"},{"issue":"5","key":"6669_CR96","doi-asserted-by":"publisher","first-page":"1925","DOI":"10.1073\/pnas.94.5.1925","volume":"94","author":"CC Bleul","year":"1997","unstructured":"Bleul CC, Wu L, Hoxie JA, Springer TA, Mackay CR (1997) The HIV coreceptors CXCR4 and CCR5 are differentially expressed and regulated on human T lymphocytes. Proc Natl Acad Sci U S A 94(5):1925\u20131930. https:\/\/doi.org\/10.1073\/pnas.94.5.1925","journal-title":"Proc Natl Acad Sci U S A"},{"key":"6669_CR97","doi-asserted-by":"publisher","unstructured":"Ploquin MJ, Casrouge A, Madec Y et al (2018) Systemic DPP4 activity is reduced during primary HIV-1 infection and is associated with intestinal RORC+CD4\u2009+\u2009cell levels: a surrogate marker candidate of HIV-induced intestinal damage. J Int AIDS Soc 21(7). https:\/\/doi.org\/10.1002\/jia2.25144","DOI":"10.1002\/jia2.25144"},{"key":"6669_CR98","doi-asserted-by":"publisher","first-page":"108824","DOI":"10.1016\/j.clim.2021.108824","volume":"230","author":"Y Govender","year":"2021","unstructured":"Govender Y, Shalekoff S, Ebrahim O et al (2021) Systemic DPP4\/CD26 is associated with natural HIV-1 control: Implications for COVID-19 susceptibility. Clin Immunol 230:108824. https:\/\/doi.org\/10.1016\/j.clim.2021.108824","journal-title":"Clin Immunol"},{"issue":"7739","key":"6669_CR99","doi-asserted-by":"publisher","first-page":"318","DOI":"10.1038\/s41586-018-0804-9","volume":"565","author":"MM Shaik","year":"2019","unstructured":"Shaik MM, Peng H, Lu J et al (2019) Structural basis of coreceptor recognition by HIV-1 envelope spike. Nature 565(7739):318\u2013323. https:\/\/doi.org\/10.1038\/s41586-018-0804-9","journal-title":"Nature"},{"key":"6669_CR100","doi-asserted-by":"publisher","unstructured":"Pu J, Wang Q, Xu W, Lu L, Jiang S (2019) Development of Protein- and Peptide-Based HIV Entry Inhibitors Targeting gp120 or gp41. Viruses 11(8):705. https:\/\/doi.org\/10.3390\/v11080705","DOI":"10.3390\/v11080705"},{"issue":"8","key":"6669_CR101","doi-asserted-by":"publisher","first-page":"3721","DOI":"10.4049\/jimmunol.158.8.3721","volume":"158","author":"A Valenzuela","year":"1997","unstructured":"Valenzuela A, Blanco J, Callebaut C et al (1997) Adenosine deaminase binding to human CD26 is inhibited by HIV-1 envelope glycoprotein gp120 and viral particles. J Immunol 158(8):3721\u20133729. https:\/\/doi.org\/10.4049\/jimmunol.158.8.3721","journal-title":"J Immunol"},{"issue":"23","key":"6669_CR102","doi-asserted-by":"publisher","first-page":"6996","DOI":"10.1093\/emboj\/16.23.6996","volume":"16","author":"MP Crump","year":"1997","unstructured":"Crump MP (1997) Solution structure and basis for functional activity of stromal cell-derived factor-1; dissociation of CXCR4 activation from binding and inhibition of HIV-1. EMBO J 16(23):6996\u20137007. https:\/\/doi.org\/10.1093\/emboj\/16.23.6996","journal-title":"EMBO J"},{"issue":"11","key":"6669_CR103","doi-asserted-by":"publisher","first-page":"1865","DOI":"10.1084\/jem.186.11.1865","volume":"186","author":"T Oravecz","year":"1997","unstructured":"Oravecz T, Pall M, Roderiquez G et al (1997) Regulation of the Receptor Specificity and Function of the Chemokine RANTES (Regulated on Activation, Normal T Cell Expressed and Secreted) by Dipeptidyl Peptidase IV (CD26)-mediated Cleavage. J Exp Med 186(11):1865\u20131872. https:\/\/doi.org\/10.1084\/jem.186.11.1865","journal-title":"J Exp Med"},{"issue":"14","key":"6669_CR104","doi-asserted-by":"publisher","first-page":"6594","DOI":"10.1073\/pnas.91.14.6594","volume":"91","author":"WG Gutheil","year":"1994","unstructured":"Gutheil WG, Subramanyam M, Flentke GR et al (1994) Human immunodeficiency virus 1 Tat binds to dipeptidyl aminopeptidase IV (CD26): a possible mechanism for Tat\u2019s immunosuppressive activity. Proc Natl Acad Sci U S A 91(14):6594\u20136598. https:\/\/doi.org\/10.1073\/pnas.91.14.6594","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"3","key":"6669_CR105","doi-asserted-by":"publisher","first-page":"145","DOI":"10.1016\/0014-5793(96)00221-9","volume":"383","author":"S Wrenger","year":"1996","unstructured":"Wrenger S, Reinhold D, Hoffmann T et al (1996) The N-terminal X\u2010X\u2010Pro sequence of the HIV\u20101 Tat protein is important for the inhibition of dipeptidyl peptidase IV (DP IV\/CD26) and the suppression of mitogen\u2010induced proliferation of human T cells. FEBS Lett 383(3):145\u2013149. https:\/\/doi.org\/10.1016\/0014-5793(96)00221-9","journal-title":"FEBS Lett"},{"issue":"15","key":"6669_CR106","doi-asserted-by":"publisher","first-page":"14911","DOI":"10.1074\/jbc.M413400200","volume":"280","author":"WA Weihofen","year":"2005","unstructured":"Weihofen WA, Liu J, Reutter W, Saenger W, Fan H (2005) Crystal Structures of HIV-1 Tat-derived Nonapeptides Tat-(1\u20139) and Trp2-Tat-(1\u20139) Bound to the Active Site of Dipeptidyl-peptidase IV (CD26). J Biol Chem 280(15):14911\u201314917. https:\/\/doi.org\/10.1074\/jbc.M413400200","journal-title":"J Biol Chem"},{"issue":"48","key":"6669_CR107","doi-asserted-by":"publisher","first-page":"30283","DOI":"10.1074\/jbc.272.48.30283","volume":"272","author":"S Wrenger","year":"1997","unstructured":"Wrenger S, Hoffmann T, Faust J et al (1997) The N-terminal Structure of HIV-1 Tat Is Required for Suppression of CD26-dependent T Cell Growth. J Biol Chem 272(48):30283\u201330288. https:\/\/doi.org\/10.1074\/jbc.272.48.30283","journal-title":"J Biol Chem"},{"issue":"19","key":"6669_CR108","doi-asserted-by":"publisher","first-page":"1814","DOI":"10.1056\/NEJMoa1211721","volume":"367","author":"AM Zaki","year":"2012","unstructured":"Zaki AM, van Boheemen S, Bestebroer TM, Osterhaus ADME, Fouchier RAM (2012) Isolation of a Novel Coronavirus from a Man with Pneumonia in Saudi Arabia. N Engl J Med 367(19):1814\u20131820. https:\/\/doi.org\/10.1056\/NEJMoa1211721","journal-title":"N Engl J Med"},{"issue":"26","key":"6669_CR109","doi-asserted-by":"publisher","first-page":"2499","DOI":"10.1056\/NEJMoa1401505","volume":"370","author":"EI Azhar","year":"2014","unstructured":"Azhar EI, El-Kafrawy SA, Farraj SA et al (2014) Evidence for Camel-to-Human Transmission of MERS Coronavirus. N Engl J Med 370(26):2499\u20132505. https:\/\/doi.org\/10.1056\/NEJMoa1401505","journal-title":"N Engl J Med"},{"issue":"1","key":"6669_CR110","doi-asserted-by":"publisher","first-page":"87","DOI":"10.1186\/s12985-016-0544-0","volume":"13","author":"HA Mohd","year":"2016","unstructured":"Mohd HA, Al-Tawfiq JA, Memish ZA (2016) Middle East Respiratory Syndrome Coronavirus (MERS-CoV) origin and animal reservoir. Virol J 13(1):87. https:\/\/doi.org\/10.1186\/s12985-016-0544-0","journal-title":"Virol J"},{"issue":"1","key":"6669_CR111","doi-asserted-by":"publisher","first-page":"10705","DOI":"10.1038\/s41467-024-55384-7","volume":"15","author":"A Latinne","year":"2024","unstructured":"Latinne A, Hu B, Olival KJ et al (2024) Origin and cross-species transmission of bat coronaviruses in China. Nat Commun 15(1):10705. https:\/\/doi.org\/10.1038\/s41467-024-55384-7","journal-title":"Nat Commun"},{"issue":"3","key":"6669_CR112","doi-asserted-by":"publisher","first-page":"181","DOI":"10.1038\/s41579-018-0118-9","volume":"17","author":"J Cui","year":"2019","unstructured":"Cui J, Li F, Shi Z-L (2019) Origin and evolution of pathogenic coronaviruses. Nat Rev Microbiol 17(3):181\u2013192. https:\/\/doi.org\/10.1038\/s41579-018-0118-9","journal-title":"Nat Rev Microbiol"},{"issue":"2","key":"6669_CR113","doi-asserted-by":"publisher","first-page":"e00373","DOI":"10.1128\/mBio.00373-17","volume":"8","author":"SJ Anthony","year":"2017","unstructured":"Anthony SJ, Gilardi K, Menachery VD et al (2017) Further Evidence for Bats as the Evolutionary Source of Middle East Respiratory Syndrome Coronavirus. mBio 8(2):e00373\u2013e00317. https:\/\/doi.org\/10.1128\/mBio.00373-17","journal-title":"mBio"},{"issue":"1","key":"6669_CR114","doi-asserted-by":"publisher","first-page":"180","DOI":"10.1016\/j.virol.2006.02.041","volume":"351","author":"PCY Woo","year":"2006","unstructured":"Woo PCY, Lau SKP, Li KSM et al (2006) Molecular diversity of coronaviruses in bats. Virology 351(1):180\u2013187. https:\/\/doi.org\/10.1016\/j.virol.2006.02.041","journal-title":"Virology"},{"issue":"11","key":"6669_CR115","doi-asserted-by":"publisher","first-page":"e1012695","DOI":"10.1371\/journal.ppat.1012695","volume":"20","author":"M Yang","year":"2024","unstructured":"Yang M, Li Z, Chen J et al (2024) Structural basis for human DPP4 receptor recognition by a pangolin MERS-like coronavirus. PLoS Pathog 20(11):e1012695. https:\/\/doi.org\/10.1371\/journal.ppat.1012695","journal-title":"PLoS Pathog"},{"issue":"1","key":"6669_CR116","doi-asserted-by":"publisher","first-page":"155","DOI":"10.1080\/22221751.2020.1713705","volume":"9","author":"H Kleine-Weber","year":"2020","unstructured":"Kleine-Weber H, Schroeder S, Kr\u00fcger N et al (2020) Polymorphisms in dipeptidyl peptidase 4 reduce host cell entry of Middle East respiratory syndrome coronavirus. Emerg Microbes Infect 9(1):155\u2013168. https:\/\/doi.org\/10.1080\/22221751.2020.1713705","journal-title":"Emerg Microbes Infect"},{"issue":"1","key":"6669_CR117","doi-asserted-by":"publisher","first-page":"78","DOI":"10.1016\/j.ajpath.2015.09.014","volume":"186","author":"DK Meyerholz","year":"2016","unstructured":"Meyerholz DK, Lambertz AM, McCray PB (2016) Dipeptidyl Peptidase 4 Distribution in the Human Respiratory Tract. Am J Pathol 186(1):78\u201386. https:\/\/doi.org\/10.1016\/j.ajpath.2015.09.014","journal-title":"Am J Pathol"},{"issue":"9","key":"6669_CR118","doi-asserted-by":"publisher","first-page":"4838","DOI":"10.1128\/JVI.02994-15","volume":"90","author":"W Widagdo","year":"2016","unstructured":"Widagdo W, Raj VS, Schipper D et al (2016) Differential Expression of the Middle East Respiratory Syndrome Coronavirus Receptor in the Upper Respiratory Tracts of Humans and Dromedary Camels. J Virol 90(9):4838\u20134842. https:\/\/doi.org\/10.1128\/JVI.02994-15","journal-title":"J Virol"},{"issue":"6","key":"6669_CR119","doi-asserted-by":"publisher","first-page":"645","DOI":"10.1016\/0021-9975(86)90061-7","volume":"96","author":"K Yagami","year":"1986","unstructured":"Yagami K, Hirai K, Hirano N (1986) Pathogenesis of haemagglutinating encephalomyelitis virus (HEV) in mice experimentally infected by different routes. J Comp Pathol 96(6):645\u2013657. https:\/\/doi.org\/10.1016\/0021-9975(86)90061-7","journal-title":"J Comp Pathol"},{"key":"6669_CR120","doi-asserted-by":"publisher","unstructured":"Mora-D\u00edaz JC, Pi\u00f1eyro PE, Houston E, Zimmerman J, Gim\u00e9nez-Lirola LG (2019) Porcine Hemagglutinating Encephalomyelitis Virus: A Review. Front Vet Sci 6(FEB):435768. https:\/\/doi.org\/10.3389\/fvets.2019.00053","DOI":"10.3389\/fvets.2019.00053"},{"issue":"8","key":"6669_CR121","doi-asserted-by":"publisher","first-page":"4696","DOI":"10.1128\/JVI.03445-14","volume":"89","author":"KM Peck","year":"2015","unstructured":"Peck KM, Cockrell AS, Yount BL et al (2015) Glycosylation of Mouse DPP4 Plays a Role in Inhibiting Middle East Respiratory Syndrome Coronavirus Infection. J Virol 89(8):4696\u20134699. https:\/\/doi.org\/10.1128\/JVI.03445-14","journal-title":"J Virol"},{"issue":"28","key":"6669_CR122","doi-asserted-by":"publisher","first-page":"7296","DOI":"10.1126\/sciadv.adv7296","volume":"11","author":"H Yuan","year":"2025","unstructured":"Yuan H, Wang J, Ma Y et al (2025) Structures and receptor binding activities of merbecovirus spike proteins reveal key signatures for human DPP4 adaptation. Sci Adv 11(28):7296. https:\/\/doi.org\/10.1126\/sciadv.adv7296","journal-title":"Sci Adv"},{"issue":"1","key":"6669_CR123","doi-asserted-by":"publisher","first-page":"601","DOI":"10.1080\/22221751.2020.1739565","volume":"9","author":"N Vankadari","year":"2020","unstructured":"Vankadari N, Wilce JA (2020) Emerging COVID-19 coronavirus: glycan shield and structure prediction of spike glycoprotein and its interaction with human CD26. Emerg Microbes Infect 9(1):601\u2013604. https:\/\/doi.org\/10.1080\/22221751.2020.1739565","journal-title":"Emerg Microbes Infect"},{"key":"6669_CR124","doi-asserted-by":"publisher","first-page":"1161","DOI":"10.3389\/fphar.2020.01161","volume":"11","author":"I Valencia","year":"2020","unstructured":"Valencia I, Peir\u00f3 C, Lorenzo \u00d3 et al (2020) DPP4 and ACE2 in Diabetes and COVID-19: Therapeutic Targets for Cardiovascular Complications? Front Pharmacol 11:1161. https:\/\/doi.org\/10.3389\/fphar.2020.01161","journal-title":"Front Pharmacol"},{"issue":"9","key":"6669_CR125","doi-asserted-by":"publisher","first-page":"649","DOI":"10.1111\/1753-0407.13052","volume":"12","author":"MF Bassendine","year":"2020","unstructured":"Bassendine MF, Bridge SH, McCaughan GW, Gorrell MD (2020) COVID-19 and comorbidities: A role for dipeptidyl peptidase 4 (DPP4) in disease severity? J Diabetes 12(9):649\u2013658. https:\/\/doi.org\/10.1111\/1753-0407.13052","journal-title":"J Diabetes"},{"issue":"13","key":"6669_CR126","doi-asserted-by":"publisher","first-page":"7001","DOI":"10.3390\/ijms22137001","volume":"22","author":"K Cameron","year":"2021","unstructured":"Cameron K, Rozano L, Falasca M, Mancera RL (2021) Does the SARS-CoV-2 Spike Protein Receptor Binding Domain Interact Effectively with the DPP4 (CD26) Receptor? A Molecular Docking Study. Int J Mol Sci 22(13):7001. https:\/\/doi.org\/10.3390\/ijms22137001","journal-title":"Int J Mol Sci"},{"issue":"22","key":"6669_CR127","doi-asserted-by":"publisher","first-page":"5392","DOI":"10.3390\/molecules25225392","volume":"25","author":"CR Xi","year":"2020","unstructured":"Xi CR, Di Fazio A, Nadvi NA et al (2020) A Novel Purification Procedure for Active Recombinant Human DPP4 and the Inability of DPP4 to Bind SARS-CoV-2. Molecules 25(22):5392. https:\/\/doi.org\/10.3390\/molecules25225392","journal-title":"Molecules"},{"issue":"2","key":"6669_CR128","doi-asserted-by":"publisher","first-page":"271","DOI":"10.1016\/j.cell.2020.02.052","volume":"181","author":"M Hoffmann","year":"2020","unstructured":"Hoffmann M, Kleine-Weber H, Schroeder S et al (2020) SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor. Cell 181(2):271\u2013280e8. https:\/\/doi.org\/10.1016\/j.cell.2020.02.052","journal-title":"Cell"},{"issue":"10407","key":"6669_CR129","doi-asserted-by":"publisher","first-page":"1085","DOI":"10.1016\/S0140-6736(23)01320-X","volume":"402","author":"M Martinello","year":"2023","unstructured":"Martinello M, Solomon SS, Terrault NA, Dore GJ (2023) Hepatitis C. Lancet 402(10407):1085\u20131096. https:\/\/doi.org\/10.1016\/S0140-6736(23)01320-X","journal-title":"Lancet"},{"issue":"3","key":"6669_CR130","doi-asserted-by":"publisher","first-page":"161","DOI":"10.1016\/S2468-1253(16)30181-9","volume":"2","author":"S Blach","year":"2017","unstructured":"Blach S, Zeuzem S, Manns M et al (2017) Global prevalence and genotype distribution of hepatitis C virus infection in 2015: a modelling study. Lancet Gastroenterol Hepatol 2(3):161\u2013176. https:\/\/doi.org\/10.1016\/S2468-1253(16)30181-9","journal-title":"Lancet Gastroenterol Hepatol"},{"key":"6669_CR131","doi-asserted-by":"publisher","first-page":"711723","DOI":"10.3389\/fpubh.2021.711723","volume":"9","author":"W-H Hsu","year":"2021","unstructured":"Hsu W-H, Sue S-P, Liang H-L et al (2021) Dipeptidyl Peptidase 4 Inhibitors Decrease the Risk of Hepatocellular Carcinoma in Patients With Chronic Hepatitis C Infection and Type 2 Diabetes Mellitus: A Nationwide Study in Taiwan. Front Public Health 9:711723. https:\/\/doi.org\/10.3389\/fpubh.2021.711723","journal-title":"Front Public Health"},{"issue":"5","key":"6669_CR132","doi-asserted-by":"publisher","first-page":"556","DOI":"10.1016\/S1499-3872(14)60308-8","volume":"13","author":"H Yanai","year":"2014","unstructured":"Yanai H (2014) Dipeptidyl peptidase-4 inhibitor sitagliptin significantly reduced hepatitis C virus replication in a diabetic patient with chronic hepatitis C virus infection. Hepatobiliary Pancreat Dis Int 13(5):556. https:\/\/doi.org\/10.1016\/S1499-3872(14)60308-8","journal-title":"Hepatobiliary Pancreat Dis Int"},{"issue":"15","key":"6669_CR133","doi-asserted-by":"publisher","first-page":"2298","DOI":"10.3748\/wjg.v19.i15.2298","volume":"19","author":"M Itou","year":"2013","unstructured":"Itou M (2013) Dipeptidyl peptidase-4: A key player in chronic liver disease. World J Gastroenterol 19(15):2298. https:\/\/doi.org\/10.3748\/wjg.v19.i15.2298","journal-title":"World J Gastroenterol"},{"issue":"2","key":"6669_CR134","doi-asserted-by":"publisher","first-page":"e56991","DOI":"10.1371\/journal.pone.0056991","volume":"8","author":"J S\u00f6derholm","year":"2013","unstructured":"S\u00f6derholm J, Waldenstr\u00f6m J, Askarieh G et al (2013) Impact of Soluble CD26 on Treatment Outcome and Hepatitis C Virus-Specific T Cells in Chronic Hepatitis C Virus Genotype 1 Infection. PLoS ONE 8(2):e56991. https:\/\/doi.org\/10.1371\/journal.pone.0056991","journal-title":"PLoS ONE"},{"issue":"6","key":"6669_CR135","doi-asserted-by":"publisher","first-page":"524","DOI":"10.1111\/j.1872-034X.2011.00798.x","volume":"41","author":"Y Arase","year":"2011","unstructured":"Arase Y, Suzuki F, Kobayashi M et al (2011) Efficacy and safety in sitagliptin therapy for diabetes complicated by chronic liver disease caused by hepatitis C virus. Hepatol Res 41(6):524\u2013529. https:\/\/doi.org\/10.1111\/j.1872-034X.2011.00798.x","journal-title":"Hepatol Res"},{"key":"6669_CR136","doi-asserted-by":"publisher","first-page":"1845","DOI":"10.2147\/DMSO.S369712","volume":"15","author":"A Sharma","year":"2022","unstructured":"Sharma A, Virmani T, Sharma A et al (2022) Potential Effect of DPP-4 Inhibitors Towards Hepatic Diseases and Associated Glucose Intolerance. Diabetes Metab Syndr Obes Volume 15:1845\u20131864. https:\/\/doi.org\/10.2147\/DMSO.S369712","journal-title":"Diabetes Metab Syndr Obes Volume"},{"issue":"1","key":"6669_CR137","doi-asserted-by":"publisher","first-page":"327","DOI":"10.1146\/annurev-virology-101416-041742","volume":"4","author":"V Cortez","year":"2017","unstructured":"Cortez V, Meliopoulos VA, Karlsson EA et al (2017) Astrovirus Biology and Pathogenesis. Annu Rev Virol 4(1):327\u2013348. https:\/\/doi.org\/10.1146\/annurev-virology-101416-041742","journal-title":"Annu Rev Virol"},{"issue":"1","key":"6669_CR138","doi-asserted-by":"publisher","first-page":"35","DOI":"10.1038\/nrd.2017.162","volume":"17","author":"SHE Kaufmann","year":"2018","unstructured":"Kaufmann SHE, Dorhoi A, Hotchkiss RS, Bartenschlager R (2018) Host-directed therapies for bacterial and viral infections. Nat Rev Drug Discov 17(1):35\u201356. https:\/\/doi.org\/10.1038\/nrd.2017.162","journal-title":"Nat Rev Drug Discov"},{"issue":"8","key":"6669_CR139","doi-asserted-by":"publisher","first-page":"e3000003","DOI":"10.1371\/journal.pbio.3000003","volume":"16","author":"S Duffy","year":"2018","unstructured":"Duffy S (2018) Why are RNA virus mutation rates so damn high? PLoS Biol 16(8):e3000003. https:\/\/doi.org\/10.1371\/journal.pbio.3000003","journal-title":"PLoS Biol"},{"key":"6669_CR140","doi-asserted-by":"publisher","first-page":"1436557","DOI":"10.3389\/fimmu.2024.1436557","volume":"15","author":"RE Thom","year":"2024","unstructured":"Thom RE, D\u2019Elia RV (2024) Future applications of host direct therapies for infectious disease treatment. Front Immunol 15:1436557. https:\/\/doi.org\/10.3389\/fimmu.2024.1436557","journal-title":"Front Immunol"},{"key":"6669_CR141","doi-asserted-by":"publisher","first-page":"80","DOI":"10.3389\/fendo.2019.00080","volume":"10","author":"CF Deacon","year":"2019","unstructured":"Deacon CF (2019) Physiology and Pharmacology of DPP-4 in Glucose Homeostasis and the Treatment of Type 2 Diabetes. Front Endocrinol (Lausanne) 10:80. https:\/\/doi.org\/10.3389\/fendo.2019.00080","journal-title":"Front Endocrinol (Lausanne)"},{"issue":"JUN","key":"6669_CR142","doi-asserted-by":"publisher","first-page":"464622","DOI":"10.3389\/fendo.2019.00389","volume":"10","author":"B Gallwitz","year":"2019","unstructured":"Gallwitz B (2019) Clinical Use of DPP-4 Inhibitors. Front Endocrinol (Lausanne) 10(JUN):464622. https:\/\/doi.org\/10.3389\/fendo.2019.00389","journal-title":"Front Endocrinol (Lausanne)"},{"issue":"6","key":"6669_CR143","doi-asserted-by":"publisher","first-page":"9053","DOI":"10.18632\/oncotarget.14754","volume":"8","author":"AA Al-Qahtani","year":"2017","unstructured":"Al-Qahtani AA, Lyroni K, Aznaourova M et al (2017) Middle east respiratory syndrome corona virus spike glycoprotein suppresses macrophage responses via DPP4-mediated induction of IRAK-M and PPAR\u03b3. Oncotarget 8(6):9053\u20139066. https:\/\/doi.org\/10.18632\/oncotarget.14754","journal-title":"Oncotarget"},{"issue":"4","key":"6669_CR144","doi-asserted-by":"publisher","first-page":"980","DOI":"10.1177\/08971900221102119","volume":"36","author":"EM Mikhael","year":"2023","unstructured":"Mikhael EM, Ong SC, Sheikh Ghadzi SM (2023) Efficacy and Safety of Sitagliptin in the Treatment of COVID-19. J Pharm Pract 36(4):980\u2013987. https:\/\/doi.org\/10.1177\/08971900221102119","journal-title":"J Pharm Pract"},{"issue":"2","key":"6669_CR145","doi-asserted-by":"publisher","first-page":"743","DOI":"10.1210\/jc.2012-3532","volume":"98","author":"SR Goodwin","year":"2013","unstructured":"Goodwin SR, Reeds DN, Royal M et al (2013) Dipeptidyl Peptidase IV Inhibition Does Not Adversely Affect Immune or Virological Status in HIV Infected Men And Women: A Pilot Safety Study. J Clin Endocrinol Metab 98(2):743\u2013751. https:\/\/doi.org\/10.1210\/jc.2012-3532","journal-title":"J Clin Endocrinol Metab"},{"issue":"7","key":"6669_CR146","doi-asserted-by":"publisher","first-page":"1165","DOI":"10.1093\/cid\/ciy1051","volume":"69","author":"MP Dub\u00e9","year":"2019","unstructured":"Dub\u00e9 MP, Chan ES, Lake JE et al (2019) A Randomized, Double-blinded, Placebo-controlled Trial of Sitagliptin for Reducing Inflammation and Immune Activation in Treated and Suppressed Human Immunodeficiency Virus Infection. Clin Infect Dis 69(7):1165\u20131172. https:\/\/doi.org\/10.1093\/cid\/ciy1051","journal-title":"Clin Infect Dis"},{"issue":"2","key":"6669_CR147","doi-asserted-by":"publisher","first-page":"1307","DOI":"10.1074\/jbc.M112.396317","volume":"288","author":"J Tang","year":"2013","unstructured":"Tang J, Majeti J, Sudom A et al (2013) An Inhibitory Antibody against Dipeptidyl Peptidase IV Improves Glucose Tolerance in Vivo. J Biol Chem 288(2):1307\u20131316. https:\/\/doi.org\/10.1074\/jbc.M112.396317","journal-title":"J Biol Chem"},{"issue":"12","key":"6669_CR148","doi-asserted-by":"publisher","first-page":"1807","DOI":"10.1093\/infdis\/jix209","volume":"215","author":"Z Chen","year":"2017","unstructured":"Chen Z, Bao L, Chen C et al (2017) Human Neutralizing Monoclonal Antibody Inhibition of Middle East Respiratory Syndrome Coronavirus Replication in the Common Marmoset. J Infect Dis 215(12):1807\u20131815. https:\/\/doi.org\/10.1093\/infdis\/jix209","journal-title":"J Infect Dis"},{"issue":"2","key":"6669_CR149","doi-asserted-by":"publisher","first-page":"131","DOI":"10.1080\/14728222.2017.1271415","volume":"21","author":"L Du","year":"2017","unstructured":"Du L, Yang Y, Zhou Y et al (2017) MERS-CoV spike protein: a key target for antivirals. Expert Opin Ther Targets 21(2):131\u2013143. https:\/\/doi.org\/10.1080\/14728222.2017.1271415","journal-title":"Expert Opin Ther Targets"},{"key":"6669_CR150","doi-asserted-by":"publisher","first-page":"2605","DOI":"10.1158\/1538-7445.AM2024-2605","volume":"84","author":"E Angevin","year":"2024","unstructured":"Angevin E, Lelarge V, Capelle R et al (2024) Abstract 2605: STX-1, a potent first-in-class ADC directed against DPP4 (CD26) as a biomarker of senescent tumor cells. Cancer Res 84:2605\u20132605. https:\/\/doi.org\/10.1158\/1538-7445.AM2024-2605","journal-title":"Cancer Res"},{"issue":"6","key":"6669_CR151","doi-asserted-by":"publisher","first-page":"1297","DOI":"10.3390\/v15061297","volume":"15","author":"Z Ren","year":"2023","unstructured":"Ren Z, Shen C, Peng J (2023) Status and Developing Strategies for Neutralizing Monoclonal Antibody Therapy in the Omicron Era of COVID-19. Viruses 15(6):1297. https:\/\/doi.org\/10.3390\/v15061297","journal-title":"Viruses"},{"issue":"2","key":"6669_CR152","doi-asserted-by":"publisher","first-page":"100018","DOI":"10.1016\/j.celbio.2025.100018","volume":"1","author":"K Nishioka","year":"2025","unstructured":"Nishioka K, Sakai Y, Motooka D et al (2025) Engineered DPP4 decoy confers broad-spectrum inhibition of MERS-CoV infection. Cell Biomaterials 1(2):100018. https:\/\/doi.org\/10.1016\/j.celbio.2025.100018","journal-title":"Cell Biomaterials"},{"issue":"1","key":"6669_CR153","doi-asserted-by":"publisher","first-page":"53","DOI":"10.1093\/abt\/tbad030","volume":"7","author":"MA Alfaleh","year":"2024","unstructured":"Alfaleh MA, Alsulaiman RM, Almahboub SA et al (2024) ACE2-Fc and DPP4-Fc decoy receptors against SARS-CoV-2 and MERS-CoV variants: a quick therapeutic option for current and future coronaviruses outbreaks. Antib Ther 7(1):53\u201366. https:\/\/doi.org\/10.1093\/abt\/tbad030","journal-title":"Antib Ther"},{"issue":"4","key":"6669_CR154","doi-asserted-by":"publisher","first-page":"e0266603","DOI":"10.1371\/journal.pone.0266603","volume":"17","author":"KR Alkharsah","year":"2022","unstructured":"Alkharsah KR, Aljaroodi SA, Rahman JU et al (2022) Low levels of soluble DPP4 among Saudis may have constituted a risk factor for MERS endemicity. PLoS ONE 17(4):e0266603. https:\/\/doi.org\/10.1371\/journal.pone.0266603","journal-title":"PLoS ONE"},{"key":"6669_CR155","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.00282-26","author":"N Chen","year":"2026","unstructured":"Chen N, Kleine-Weber H, Alkharsah K et al (2026) Q1020R in the spike proteins of MERS-CoV from Arabian camels confers resistance against soluble human DPP4. J Virol. https:\/\/doi.org\/10.1128\/jvi.00282-26","journal-title":"J Virol"},{"issue":"33","key":"6669_CR156","doi-asserted-by":"publisher","first-page":"10473","DOI":"10.1073\/pnas.1510199112","volume":"112","author":"D Corti","year":"2015","unstructured":"Corti D, Zhao J, Pedotti M et al (2015) Prophylactic and postexposure efficacy of a potent human monoclonal antibody against MERS coronavirus. Proc Natl Acad Sci U S A 112(33):10473\u201310478. https:\/\/doi.org\/10.1073\/pnas.1510199112","journal-title":"Proc Natl Acad Sci U S A"},{"issue":"7","key":"6669_CR157","doi-asserted-by":"publisher","first-page":"891","DOI":"10.3390\/ph17070891","volume":"17","author":"M Murdocca","year":"2024","unstructured":"Murdocca M, Romeo I, Citro G et al (2024) A Dynamic and Effective Peptide-Based Strategy for Promptly Addressing Emerging SARS-CoV-2 Variants of Concern. Pharmaceuticals 17(7):891. https:\/\/doi.org\/10.3390\/ph17070891","journal-title":"Pharmaceuticals"},{"issue":"2","key":"6669_CR158","doi-asserted-by":"publisher","first-page":"441","DOI":"10.1016\/j.celrep.2018.06.041","volume":"24","author":"S Zhang","year":"2018","unstructured":"Zhang S, Zhou P, Wang P et al (2018) Structural Definition of a Unique Neutralization Epitope on the Receptor-Binding Domain of MERS-CoV Spike Glycoprotein. Cell Rep 24(2):441\u2013452. https:\/\/doi.org\/10.1016\/j.celrep.2018.06.041","journal-title":"Cell Rep"},{"issue":"8","key":"6669_CR159","doi-asserted-by":"publisher","first-page":"1667","DOI":"10.3390\/v13081667","volume":"13","author":"M Murdocca","year":"2021","unstructured":"Murdocca M, Citro G, Romeo I et al (2021) Peptide Platform as a Powerful Tool in the Fight against COVID-19. Viruses 13(8):1667. https:\/\/doi.org\/10.3390\/v13081667","journal-title":"Viruses"},{"issue":"10","key":"6669_CR160","doi-asserted-by":"publisher","first-page":"2100104","DOI":"10.1002\/adtp.202100104","volume":"4","author":"D Panchal","year":"2021","unstructured":"Panchal D, Kataria J, Patel K et al (2021) Peptide-Based Inhibitors for SARS\u2010CoV\u20102 and SARS\u2010CoV. Adv Ther (Weinh) 4(10):2100104. https:\/\/doi.org\/10.1002\/adtp.202100104","journal-title":"Adv Ther (Weinh)"}],"container-title":["Archives of Virology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s00705-026-06669-3.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/article\/10.1007\/s00705-026-06669-3","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/link.springer.com\/content\/pdf\/10.1007\/s00705-026-06669-3.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,7,27]],"date-time":"2026-07-27T07:02:20Z","timestamp":1785135740000},"score":1,"resource":{"primary":{"URL":"https:\/\/link.springer.com\/10.1007\/s00705-026-06669-3"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,6,13]]},"references-count":160,"journal-issue":{"issue":"7","published-print":{"date-parts":[[2026,7]]}},"alternative-id":["6669"],"URL":"https:\/\/doi.org\/10.1007\/s00705-026-06669-3","relation":{},"ISSN":["0304-8608","1432-8798"],"issn-type":[{"value":"0304-8608","type":"print"},{"value":"1432-8798","type":"electronic"}],"subject":[],"published":{"date-parts":[[2026,6,13]]},"assertion":[{"value":"23 March 2026","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"2 June 2026","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"13 June 2026","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"The authors declare no competing interests.","order":1,"name":"Ethics","label":"Competing interests","group":{"name":"EthicsHeading","label":"Declarations"}}],"article-number":"210"}}