{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T06:15:40Z","timestamp":1788416140366,"version":"build-2803163510"},"reference-count":41,"publisher":"China Science Publishing & Media Ltd.","content-domain":{"domain":["engine.scichina.com"],"crossmark-restriction":false},"short-container-title":["ABBS"],"published-print":{"date-parts":[[2026,8,1]]},"DOI":"10.3724\/abbs.2026141","type":"journal-article","created":{"date-parts":[[2026,8,11]],"date-time":"2026-08-11T07:47:42Z","timestamp":1786434462000},"update-policy":"https:\/\/doi.org\/10.1360\/scp-crossmark-policy-page","source":"Crossref","is-referenced-by-count":0,"title":["Structure and enzymatic properties of human retroviral-like aspartic protease 1 and functional roles of disease-associated mutations"],"prefix":"10.3724","author":[{"given":"Xueqian","family":"Feng","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ziyue","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chao","family":"Lan","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jianping","family":"Ding","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"2026","published-online":{"date-parts":[[2026,8,11]]},"reference":[{"key":"CITATION1","doi-asserted-by":"publisher","first-page":"R144","DOI":"10.1016\/j.cub.2020.01.004","volume":"30","author":"Moreci RS","year":"2020","unstructured":"Moreci RS, Lechler T. Epidermal structure and differentiation. Curr Biol, 2020, 30: R144-R149.","journal-title":"Curr Biol"},{"key":"CITATION2","doi-asserted-by":"publisher","first-page":"e2106633118","DOI":"10.1073\/pnas.2106633118","volume":"118","author":"Moore JL","year":"2021","unstructured":"Moore JL, Greco V. Functional cell death, corneoptosis, requires temporally controlled intracellular acidification. Proc Natl Acad Sci USA, 2021, 118:","journal-title":"Proc Natl Acad Sci USA"},{"key":"CITATION3","doi-asserted-by":"publisher","first-page":"43","DOI":"10.3390\/jdb11040043","volume":"11","author":"Matsui T","year":"2023","unstructured":"Matsui T. Epidermal barrier development via corneoptosis: a unique form of cell death in stratum granulosum cells. J Dev Biol, 2023, 11:","journal-title":"J Dev Biol"},{"key":"CITATION4","doi-asserted-by":"publisher","first-page":"278","DOI":"10.1111\/j.0022-202X.2005.23816.x","volume":"125","author":"Bernard D","year":"2005","unstructured":"Bernard D, M\u00e9hul B, Thomas-Collignon A, Delattre C, Donovan M, Schmidt R. Identification and characterization of a novel retroviral-like aspartic protease specifically expressed in human epidermis. J Investig Dermatol, 2005, 125: 278-287.","journal-title":"J Investig Dermatol"},{"key":"CITATION5","doi-asserted-by":"publisher","first-page":"27512","DOI":"10.1074\/jbc.M603559200","volume":"281","author":"Matsui T","year":"2006","unstructured":"Matsui T, Kinoshita-Ida Y, Hayashi-Kisumi F, Hata M, Matsubara K, Chiba M, Katahira-Tayama S. Mouse homologue of skin-specific retroviral-like aspartic protease involved in wrinkle formation. J Biol Chem, 2006, 281: 27512-27525.","journal-title":"J Biol Chem"},{"key":"CITATION6","doi-asserted-by":"publisher","first-page":"320","DOI":"10.1002\/emmm.201100140","volume":"3","author":"Matsui T","year":"2011","unstructured":"Matsui T, Miyamoto K, Kubo A, Kawasaki H, Ebihara T, Hata K, Tanahashi S. SASPase regulates stratum corneum hydration through profilaggrin-to-filaggrin processing. EMBO Mol Med, 2011, 3: 320-333.","journal-title":"EMBO Mol Med"},{"key":"CITATION7","doi-asserted-by":"publisher","first-page":"1507","DOI":"10.1038\/jid.2011.479","volume":"132","author":"Sandilands A","year":"2012","unstructured":"Sandilands A, Brown SJ, Goh CS, Pohler E, Wilson NJ, Campbell LE, Miyamoto K. Mutations in the SASPase gene (ASPRV1) are not associated with atopic eczema or clinically dry skin. J Investig Dermatol, 2012, 132: 1507-1510.","journal-title":"J Investig Dermatol"},{"key":"CITATION8","doi-asserted-by":"publisher","first-page":"1004","DOI":"10.3390\/biom10071004","volume":"10","author":"Golda M","year":"2020","unstructured":"Golda M,  Motyan  JA, Nagy K. Biochemical characterization of human retroviral-like aspartic protease 1 (ASPRV1). Biomolecules, 2020, 10:","journal-title":"Biomolecules"},{"key":"CITATION9","doi-asserted-by":"publisher","first-page":"107634","DOI":"10.1016\/j.jbc.2024.107634","volume":"300","author":"Motyan  JA","year":"2024","unstructured":"Motyan  JA,  Tozser  J.  The human retroviral-like aspartic protease 1 (ASPRV1): from in vitro studies to clinical correlations . J Biol Chem, 2024, 300:","journal-title":"J Biol Chem"},{"key":"CITATION10","doi-asserted-by":"publisher","first-page":"e96882","DOI":"10.1172\/jci.insight.96882","volume":"2","author":"Whittaker Hawkins RF","year":"2017","unstructured":"Whittaker Hawkins RF, Patenaude A, Dumas A. ICAM1+ neutrophils promote chronic inflammation via ASPRV1 in B cell-dependent autoimmune encephalomyelitis. JCI Insight, 2017, 2:","journal-title":"JCI Insight"},{"key":"CITATION11","doi-asserted-by":"publisher","first-page":"e1006651","DOI":"10.1371\/journal.pgen.1006651","volume":"13","author":"Bauer A","year":"2017","unstructured":"Bauer A, Waluk DP, Galichet A, Timm K, Jagannathan V, Sayar BS, Wiener DJ.  A de novo variant in the ASPRV1 gene in a dog with ichthyosis . PLoS Genet, 2017, 13:","journal-title":"PLoS Genet"},{"key":"CITATION12","doi-asserted-by":"publisher","first-page":"158","DOI":"10.1016\/j.ajhg.2020.05.013","volume":"107","author":"Boyden LM","year":"2020","unstructured":"Boyden LM, Zhou J, Hu R, Zaki T, Loring E, Scott J, Traupe H. Mutations in ASPRV1 cause dominantly inherited ichthyosis. Am J Hum Genet, 2020, 107: 158-163.","journal-title":"Am J Hum Genet"},{"key":"CITATION13","doi-asserted-by":"publisher","first-page":"490","DOI":"10.1111\/age.13423","volume":"55","author":"Kiener S","year":"2024","unstructured":"Kiener S, \u00c5hman S, Cikota R, Jagannathan V, Blatter S, Cvitas I, Soto S.  Heterozygous ASPRV1 frameshift variant in a pembroke welsh corgi with ichthyosis . Anim Genet, 2024, 55: 490-492.","journal-title":"Anim Genet"},{"key":"CITATION14","doi-asserted-by":"publisher","first-page":"msae154","DOI":"10.1093\/molbev\/msae154","volume":"41","author":"Cagliani R","year":"2024","unstructured":"Cagliani R, Forni D, Mozzi A, Fuchs R, Tussia-Cohen D, Arrigoni F, Pozzoli U. Evolution of virus-like features and intrinsically disordered regions in retrotransposon-derived mammalian genes. Mol Biol Evol, 2024, 41:","journal-title":"Mol Biol Evol"},{"key":"CITATION15","doi-asserted-by":"publisher","first-page":"355","DOI":"10.1038\/s41579-019-0189-2","volume":"17","author":"Johnson WE","year":"2019","unstructured":"Johnson WE. Origins and evolutionary consequences of ancient endogenous retroviruses. Nat Rev Microbiol, 2019, 17: 355-370.","journal-title":"Nat Rev Microbiol"},{"key":"CITATION16","doi-asserted-by":"publisher","first-page":"275","DOI":"10.1016\/j.cell.2018.03.024","volume":"173","author":"Pastuzyn ED","year":"2018","unstructured":"Pastuzyn ED, Day CE, Kearns RB, Kyrke-Smith M, Taibi AV, McCormick J, Yoder N. The neuronal gene arc encodes a repurposed retrotransposon gag protein that mediates intercellular RNA transfer. Cell, 2018, 173:","journal-title":"Cell"},{"key":"CITATION17","doi-asserted-by":"publisher","first-page":"882","DOI":"10.1126\/science.abg6155","volume":"373","author":"Segel M","year":"2021","unstructured":"Segel M, Lash B, Song J, Ladha A, Liu CC, Jin X, Mekhedov SL. Mammalian retrovirus-like protein PEG10 packages its own mRNA and can be pseudotyped for mRNA delivery. Science, 2021, 373: 882-889.","journal-title":"Science"},{"key":"CITATION18","doi-asserted-by":"publisher","first-page":"89","DOI":"10.1080\/713609213","volume":"38","author":"Dash C","year":"2003","unstructured":"Dash C, Kulkarni A, Dunn B, Rao M. Aspartic peptidase inhibitors: implications in drug development. Crit Rev Biochem Mol Biol, 2003, 38: 89-119.","journal-title":"Crit Rev Biochem Mol Biol"},{"key":"CITATION19","doi-asserted-by":"publisher","first-page":"1108","DOI":"10.1110\/ps.03468904","volume":"13","author":"Perryman AL","year":"2004","unstructured":"Perryman AL, Lin JH, McCammon JA. HIV-1 protease molecular dynamics of a wild-type and of the V82F\/I84V mutant: possible contributions to drug resistance and a potential new target site for drugs. Protein Sci, 2004, 13: 1108-1123.","journal-title":"Protein Sci"},{"key":"CITATION20","doi-asserted-by":"publisher","first-page":"2282","DOI":"10.1002\/prot.23054","volume":"79","author":"Lexa KW","year":"2011","unstructured":"Lexa KW, Carlson HA. Binding to the open conformation of HIV-1 protease. Proteins, 2011, 79: 2282-2290.","journal-title":"Proteins"},{"key":"CITATION21","doi-asserted-by":"publisher","first-page":"915","DOI":"10.1073\/pnas.0508452103","volume":"103","author":"Hornak V","year":"2006","unstructured":"Hornak V, Okur A, Rizzo RC, Simmerling C. HIV-1 protease flaps spontaneously open and reclose in molecular dynamics simulations. Proc Natl Acad Sci USA, 2006, 103: 915-920.","journal-title":"Proc Natl Acad Sci USA"},{"key":"CITATION22","doi-asserted-by":"publisher","first-page":"9748","DOI":"10.1021\/acsomega.2c08279","volume":"8","author":"Dakshinamoorthy Avinash","year":"2023","unstructured":"Dakshinamoorthy Avinash, Asmita Ananya, Senapati Sanjib. Comprehending the structure, dynamics, and mechanism of action of drug-resistant HIV protease. ACS Omega, 2023, 8: 9748-9763.","journal-title":"ACS Omega"},{"key":"CITATION23","doi-asserted-by":"crossref","unstructured":"Venkatachalam S, Krishnan S R, Sayed Y, et al. Structural and functional studies on HIV protease: mechanism of action, subtypes, inhibitors, and drug resistance.  Methods Mol Biol , 2025, 2867: 185\u2013200 .","DOI":"10.1007\/978-1-0716-4196-5_11"},{"key":"CITATION24","doi-asserted-by":"crossref","unstructured":"Otwinowski Z, Minor W. Processing of X-ray diffraction data collected in oscillation mode.  Methods Enzymol , 1997, 276: 307\u201326 .","DOI":"10.1016\/S0076-6879(97)76066-X"},{"key":"CITATION25","doi-asserted-by":"publisher","first-page":"125","DOI":"10.1107\/S0907444909047337","volume":"66","author":"Kabsch W","year":"2010","unstructured":"Kabsch W. XDS. Acta Crystlogr D Biol Crystlogr, 2010, 66: 125-132.","journal-title":"Acta Crystlogr D Biol Crystlogr"},{"key":"CITATION26","doi-asserted-by":"publisher","first-page":"486","DOI":"10.1107\/S0907444910007493","volume":"66","author":"Emsley P","year":"2010","unstructured":"Emsley P, Lohkamp B, Scott WG, Cowtan K.  Features and development of Coot . Acta Crystlogr D Biol Crystlogr, 2010, 66: 486-501.","journal-title":"Acta Crystlogr D Biol Crystlogr"},{"key":"CITATION27","doi-asserted-by":"publisher","first-page":"213","DOI":"10.1107\/S0907444909052925","volume":"66","author":"Adams PD","year":"2010","unstructured":"Adams PD, Afonine PV, Bunk\u00f3czi G, Chen VB, Davis IW, Echols N, Headd JJ.  PHENIX: a comprehensive Python-based system for macromolecular structure solution . Acta Crystlogr D Biol Crystlogr, 2010, 66: 213-221.","journal-title":"Acta Crystlogr D Biol Crystlogr"},{"key":"CITATION28","unstructured":"Schrodinger, Llc. The PyMOL Molecular Graphics System, Version 1.8, 2015 ."},{"key":"CITATION29","doi-asserted-by":"publisher","first-page":"5458","DOI":"10.1074\/jbc.271.10.5458","volume":"271","author":"Szeltner Z","year":"1996","unstructured":"Szeltner Z, Polg\u00e1r L. Conformational stability and catalytic activity of HIV-1 protease are both enhanced at high salt concentration. J Biol Chem, 1996, 271: 5458-5463.","journal-title":"J Biol Chem"},{"key":"CITATION30","doi-asserted-by":"publisher","first-page":"49110","DOI":"10.1074\/jbc.M108136200","volume":"276","author":"Ishima R","year":"2001","unstructured":"Ishima R, Ghirlando R, T\u00f6zs\u00e9r J, Gronenborn AM, Torchia DA, Louis JM. Folded monomer of HIV-1 protease. J Biol Chem, 2001, 276: 49110-49116.","journal-title":"J Biol Chem"},{"key":"CITATION31","doi-asserted-by":"publisher","first-page":"6085","DOI":"10.1074\/jbc.M209726200","volume":"278","author":"Louis JM","year":"2003","unstructured":"Louis JM, Ishima R, Nesheiwat I, Pannell LK, Lynch SM, Torchia DA, Gronenborn AM. Revisiting monomeric HIV-1 protease. J Biol Chem, 2003, 278: 6085-6092.","journal-title":"J Biol Chem"},{"key":"CITATION32","doi-asserted-by":"publisher","first-page":"369","DOI":"10.1016\/S0969-2126(02)00720-7","volume":"10","author":"Prabu-Jeyabalan M","year":"2002","unstructured":"Prabu-Jeyabalan M, Nalivaika E, Schiffer CA. Substrate shape determines specificity of recognition for HIV-1 protease. Structure, 2002, 10: 369-381.","journal-title":"Structure"},{"key":"CITATION33","doi-asserted-by":"publisher","first-page":"12933","DOI":"10.1021\/bi9612733","volume":"35","author":"Rose RB","year":"1996","unstructured":"Rose RB, Craik CS, Douglas NL, Stroud RM.  Three-dimensional structures of HIV-1 and SIV protease product complexes, . Biochemistry, 1996, 35: 12933-12944.","journal-title":"Biochemistry"},{"key":"CITATION34","doi-asserted-by":"publisher","first-page":"1464","DOI":"10.1021\/acscatal.8b04142","volume":"9","author":"Windsor IW","year":"2019","unstructured":"Windsor IW, Gold B, Raines RT.  An n\u2192\u03c0* Interaction in the bound substrate of aspartic proteases replicates the oxyanion hole . ACS Catal, 2019, 9: 1464-1471.","journal-title":"ACS Catal"},{"key":"CITATION35","doi-asserted-by":"publisher","first-page":"11638","DOI":"10.1073\/pnas.90.24.11638","volume":"90","author":"Baca M","year":"1993","unstructured":"Baca M, Kent SBH. Catalytic contribution of flap-substrate hydrogen bonds in \u201cHIV-1 protease\u201d explored by chemical synthesis. Proc Natl Acad Sci USA, 1993, 90: 11638-11642.","journal-title":"Proc Natl Acad Sci USA"},{"key":"CITATION36","doi-asserted-by":"publisher","first-page":"1022","DOI":"10.1016\/j.bbrc.2012.12.045","volume":"430","author":"Liu Z","year":"2013","unstructured":"Liu Z, Wang Y, Yedidi RS, Dewdney TG, Reiter SJ, Brunzelle JS, Kovari IA. Conserved hydrogen bonds and water molecules in MDR HIV-1 protease substrate complexes. Biochem Biophys Res Commun, 2013, 430: 1022-1027.","journal-title":"Biochem Biophys Res Commun"},{"key":"CITATION37","doi-asserted-by":"publisher","first-page":"669","DOI":"10.1111\/exd.12740","volume":"24","author":"Thakoersing VS","year":"2015","unstructured":"Thakoersing VS, van Smeden J, Boiten WA, Gooris GS, Mulder AA, Vreeken RJ, El Ghalbzouri A. Modulation of stratum corneum lipid composition and organization of human skin equivalents by specific medium supplements. Exp Dermatol, 2015, 24: 669-674.","journal-title":"Exp Dermatol"},{"key":"CITATION38","doi-asserted-by":"publisher","first-page":"105305","DOI":"10.1016\/j.chemphyslip.2023.105305","volume":"254","author":"Uchino T","year":"2023","unstructured":"Uchino T, Kamiya D, Yagi H, Fujino-Shimaya H, Hatta I, Fujimori S, Miyazaki Y. Comparative analysis of intercellular lipid organization and composition between psoriatic and healthy stratum corneum. Chem Phys Lipids, 2023, 254:","journal-title":"Chem Phys Lipids"},{"key":"CITATION39","doi-asserted-by":"publisher","first-page":"6006","DOI":"10.1021\/ja060483s","volume":"128","author":"Minh DDL","year":"2006","unstructured":"Minh DDL, Chang C, Trylska J, Tozzini V, McCammon JA. The influence of macromolecular crowding on HIV-1 protease internal dynamics. J Am Chem Soc, 2006, 128: 6006-6007.","journal-title":"J Am Chem Soc"},{"key":"CITATION40","doi-asserted-by":"publisher","first-page":"2360","DOI":"10.1016\/j.jmb.2015.05.007","volume":"427","author":"Potempa M","year":"2015","unstructured":"Potempa M, Nalivaika E, Ragland D, Lee SK, Schiffer CA, Swanstrom R.  A direct interaction with RNA dramatically enhances the catalytic activity of the HIV-1 protease in vitro . J Mol Biol, 2015, 427: 2360-2378.","journal-title":"J Mol Biol"},{"key":"CITATION41","doi-asserted-by":"publisher","first-page":"685","DOI":"10.1007\/s00249-019-01392-1","volume":"48","author":"Maximova K","year":"2019","unstructured":"Maximova K, Wojtczak J, Trylska J. Enzymatic activity of human immunodeficiency virus type 1 protease in crowded solutions. Eur Biophys J, 2019, 48: 685-689.","journal-title":"Eur Biophys J"}],"container-title":["Acta Biochimica et Biophysica Sinica"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.sciengine.com\/sci-open\/api\/v1\/open\/file\/pdf\/08015C5E264740F1BA5689C05C9299C3","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.sciengine.com\/doi\/10.3724\/abbs.2026141","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.sciengine.com\/sci-open\/api\/v1\/open\/file\/pdf\/08015C5E264740F1BA5689C05C9299C3","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T05:39:12Z","timestamp":1788413952000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.sciengine.com\/doi\/10.3724\/abbs.2026141"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,8,1]]},"references-count":41,"URL":"https:\/\/doi.org\/10.3724\/abbs.2026141","relation":{},"ISSN":["1672-9145"],"issn-type":[{"value":"1672-9145","type":"print"}],"subject":[],"published":{"date-parts":[[2026,8,1]]}}}