{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,22]],"date-time":"2026-09-22T18:56:11Z","timestamp":1790103371545,"version":"4.0.1"},"reference-count":147,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2021,4,1]],"date-time":"2021-04-01T00:00:00Z","timestamp":1617235200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2021,4,1]],"date-time":"2021-04-01T00:00:00Z","timestamp":1617235200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100001870","name":"Fundacja na rzecz Nauki Polskiej","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001870","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Biochimie"],"published-print":{"date-parts":[[2021,4]]},"DOI":"10.1016\/j.biochi.2020.09.017","type":"journal-article","created":{"date-parts":[[2020,10,10]],"date-time":"2020-10-10T01:24:27Z","timestamp":1602293067000},"page":"3-12","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":26,"special_numbering":"C","title":["Prolidase \u2013 A protein with many faces"],"prefix":"10.1016","volume":"183","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-7217-4163","authenticated-orcid":false,"given":"Piotr","family":"Wilk","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"El\u017cbieta","family":"W\u0105tor","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Manfred S.","family":"Weiss","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.biochi.2020.09.017_bib1","doi-asserted-by":"crossref","first-page":"2473","DOI":"10.1073\/pnas.91.7.2473","article-title":"Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold","volume":"91","author":"Bazan","year":"2006","journal-title":"Proc. Natl. Acad. Sci. Unit. States Am."},{"key":"10.1016\/j.biochi.2020.09.017_bib2","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0111531","article-title":"Structural basis of substrate selectivity of e. coli prolidase","volume":"9","author":"Weaver","year":"2014","journal-title":"PLoS One"},{"key":"10.1016\/j.biochi.2020.09.017_bib3","doi-asserted-by":"crossref","first-page":"346","DOI":"10.1107\/S1744309113002674","article-title":"Organophosphorus acid anhydrolase from Alteromonas macleodii: structural study and functional relationship to prolidases","volume":"69","author":"Stepankova","year":"2013","journal-title":"Acta Crystallogr Sect F Struct Biol Cryst Commun"},{"key":"10.1016\/j.biochi.2020.09.017_bib4","first-page":"547","article-title":"G-type nerve agent decontamination by Alteromonas prolidase","volume":"49","author":"Cheng","year":"1998","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"10.1016\/j.biochi.2020.09.017_bib5","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1021\/bi9011989","article-title":"Structural insights into the dual activities of the nerve agent degrading organophosphate anhydrolase\/prolidase","volume":"49","author":"Vyas","year":"2010","journal-title":"Biochemistry"},{"key":"10.1016\/j.biochi.2020.09.017_bib6","doi-asserted-by":"crossref","DOI":"10.1016\/S0958-6946(02)00022-5","article-title":"Accelerating cheese proteolysis by enriching Lactococcus lactis proteolytic system with lactobacilli peptidases","author":"Courtin","year":"2002","journal-title":"Int. Dairy J."},{"key":"10.1016\/j.biochi.2020.09.017_bib7","doi-asserted-by":"crossref","DOI":"10.1016\/S0009-2797(99)00058-7","article-title":"Alteromonas prolidase for organophosphorus G-agent decontamination","author":"Cheng","year":"1999","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.biochi.2020.09.017_bib8","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/j.bbapap.2012.09.008","article-title":"A\u00a0Mn(II)-Mn(II) center in human prolidase","volume":"1834","author":"Besio","year":"2013","journal-title":"Biochim. Biophys. Acta Protein Proteonomics"},{"key":"10.1016\/j.biochi.2020.09.017_bib9","doi-asserted-by":"crossref","first-page":"6140","DOI":"10.1016\/j.febslet.2005.09.086","article-title":"Characterization of the dinuclear metal center of Pyrococcus furiosus prolidase by analysis of targeted mutants","volume":"579","author":"Du","year":"2005","journal-title":"FEBS Lett."},{"key":"10.1016\/j.biochi.2020.09.017_bib10","doi-asserted-by":"crossref","first-page":"4581","DOI":"10.1021\/cr0101757","article-title":"Metalloaminopeptidases: common functional themes in disparate structural surroundings","volume":"102","author":"Lowther","year":"2002","journal-title":"Chem. Rev."},{"key":"10.1016\/j.biochi.2020.09.017_bib11","article-title":"The minimal gene complement of Mycoplasma genitalium","volume":"80","author":"Fraser","year":"1995","journal-title":"Science"},{"key":"10.1016\/j.biochi.2020.09.017_bib12","doi-asserted-by":"crossref","DOI":"10.1101\/gr.2674004","article-title":"The complete genome and proteome of Mycoplasma mobile","author":"Jaffe","year":"2004","journal-title":"Genome Res."},{"key":"10.1016\/j.biochi.2020.09.017_bib13","doi-asserted-by":"crossref","DOI":"10.1128\/jb.135.2.603-611.1978","article-title":"Peptidase-deficient mutants of Escherichia coli","author":"Miller","year":"1978","journal-title":"J.\u00a0Bacteriol."},{"key":"10.1016\/j.biochi.2020.09.017_bib14","doi-asserted-by":"crossref","DOI":"10.1128\/AEM.01934-12","article-title":"Osmoprotection of Bacillus subtilis through import and proteolysis of proline-containing peptides","author":"Zaprasis","year":"2013","journal-title":"Appl. Environ. Microbiol."},{"key":"10.1016\/j.biochi.2020.09.017_bib15","author":"Almeida"},{"key":"10.1016\/j.biochi.2020.09.017_bib16","doi-asserted-by":"crossref","DOI":"10.1016\/j.abb.2004.06.022","article-title":"Catalytic properties of the PepQ prolidase from Escherichia coli","author":"Park","year":"2004","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.biochi.2020.09.017_bib17","doi-asserted-by":"crossref","DOI":"10.1016\/S0021-9258(18)83768-1","article-title":"Primary structure and gene localization of human prolidase","author":"Endo","year":"1989","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2020.09.017_bib18","doi-asserted-by":"crossref","first-page":"11306","DOI":"10.1016\/S0021-9258(19)38592-8","article-title":"Structural organization of the gene for human prolidase (peptidase D) and demonstration of a partial gene deletion in a patient with prolidase deficiency","volume":"265","author":"Tanoue","year":"1990","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.biochi.2020.09.017_bib19","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/s41598-018-27789-0","article-title":"Comprehensive in-silico prediction of damage associated SNPs in Human Prolidase gene","volume":"8","author":"Bhatnager","year":"2018","journal-title":"Sci. Rep."},{"key":"10.1016\/j.biochi.2020.09.017_bib20","doi-asserted-by":"crossref","first-page":"2771","DOI":"10.1021\/bi0356451","article-title":"Structure of the prolidase from Pyrococcus furiosus","volume":"43","author":"Maher","year":"2004","journal-title":"Biochemistry"},{"key":"10.1016\/j.biochi.2020.09.017_bib21","first-page":"428","article-title":"Crystallization and characterization of the prolidase from Pyrococcus furiosus","author":"Willingham","year":"2006","journal-title":"Acta Crystallogr. D"},{"key":"10.1016\/j.biochi.2020.09.017_bib22","doi-asserted-by":"crossref","first-page":"951","DOI":"10.1107\/S2053230X15009498","article-title":"Structure of recombinant prolidase from Thermococcus sibiricus in space group P21221","volume":"71","author":"Timofeev","year":"2015","journal-title":"Acta Crystallogr Sect Struct Biol Commun"},{"key":"10.1016\/j.biochi.2020.09.017_bib23","doi-asserted-by":"crossref","first-page":"2870","DOI":"10.1111\/febs.14158","article-title":"Substrate specificity and reaction mechanism of human prolidase","volume":"284","author":"Wilk","year":"2017","journal-title":"FEBS J."},{"key":"10.1016\/j.biochi.2020.09.017_bib24","doi-asserted-by":"crossref","first-page":"3394","DOI":"10.1021\/ic1022517","article-title":"Can human prolidase enzyme use different metals for full catalytic activity?","volume":"50","author":"Alberto","year":"2011","journal-title":"Inorg. Chem."},{"key":"10.1016\/j.biochi.2020.09.017_bib25","doi-asserted-by":"crossref","DOI":"10.7717\/peerj.5863","article-title":"High-level expression and molecular characterization of a recombinant prolidase from Escherichia coli NovaBlue","volume":"6","author":"Wang","year":"2018","journal-title":"PeerJ"},{"key":"10.1016\/j.biochi.2020.09.017_bib26","doi-asserted-by":"crossref","first-page":"2256","DOI":"10.1107\/S0907444904026460","article-title":"Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions","volume":"60","author":"Krissinel","year":"2004","journal-title":"Acta Crystallogr. Sect. D Biol. Crystallogr."},{"key":"10.1016\/j.biochi.2020.09.017_bib27","doi-asserted-by":"crossref","DOI":"10.1007\/BF01805618","article-title":"Substrate specificity of manganese-activated prolidase in control and prolidase-deficient cultured skin fibroblasts","author":"Butterworth","year":"1984","journal-title":"J.\u00a0Inherit. Metab. Dis."},{"key":"10.1016\/j.biochi.2020.09.017_bib28","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1016\/0009-8981(84)90385-1","article-title":"Prolidase deficiency: characteristics of human skin fibroblast prolidase using colorimetric and fluorimetric assays","volume":"142","author":"Priestman","year":"1984","journal-title":"Clin. Chim. Acta"},{"key":"10.1016\/j.biochi.2020.09.017_bib29","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbapap.2009.01.008","article-title":"Deregulation of allosteric response of Lactococcus lactis prolidase and its effects on enzyme activity","author":"Zhang","year":"2009","journal-title":"Biochim. Biophys. Acta Protein Proteonomics"},{"key":"10.1016\/j.biochi.2020.09.017_bib30","doi-asserted-by":"crossref","DOI":"10.1128\/JB.180.18.4781-4789.1998","article-title":"Characterization of native and recombinant forms of an unusual cobalt- dependent proline dipeptidase (prolidase) from the hyperthermophilic archaeon Pyrococcus furiosus","author":"Ghosh","year":"1998","journal-title":"J.\u00a0Bacteriol."},{"key":"10.1016\/j.biochi.2020.09.017_bib31","doi-asserted-by":"crossref","DOI":"10.1111\/j.1742-4658.2007.06197.x","article-title":"Characterization of recombinant prolidase from Lactococcus lactis - changes in substrate specificity by metal cations, and allosteric behavior of the peptidase","author":"Yang","year":"2008","journal-title":"FEBS J."},{"key":"10.1016\/j.biochi.2020.09.017_bib32","doi-asserted-by":"crossref","first-page":"935","DOI":"10.1007\/s00249-009-0459-4","article-title":"Identifying the structure of the active sites of human recombinant prolidase","volume":"39","author":"Besio","year":"2010","journal-title":"Eur. Biophys. J."},{"key":"10.1016\/j.biochi.2020.09.017_bib33","doi-asserted-by":"crossref","first-page":"1715","DOI":"10.1016\/j.bbapap.2009.08.005","article-title":"S1 site residues of Lactococcus lactis prolidase affect substrate specificity and allosteric behaviour","volume":"1794","author":"Hu","year":"2009","journal-title":"Biochim. Biophys. Acta Protein Proteonomics"},{"key":"10.1016\/j.biochi.2020.09.017_bib34","doi-asserted-by":"crossref","DOI":"10.1155\/2011\/565127","article-title":"Improving the Catalytic Activity of Hyperthermophilic Pyrococcus Horikoshii Prolidase for Detoxification of Organophosphorus Nerve Agents over a Broad Range of Temperatures","author":"Theriot","year":"2011","journal-title":"Archaea"},{"key":"10.1016\/j.biochi.2020.09.017_bib35","article-title":"Characterization of two proline dipeptidases (prolidases) from the hyperthermophilic archaeon Pyrococcus horikoshii","author":"Theriot","year":"2010","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.1016\/j.biochi.2020.09.017_bib36","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1007\/s00726-008-0055-4","article-title":"Human prolidase and prolidase deficiency: an overview on the characterization of the enzyme involved in proline recycling and on the effects of its mutations","volume":"35","author":"Lupi","year":"2008","journal-title":"Amino Acids"},{"key":"10.1016\/j.biochi.2020.09.017_bib37","doi-asserted-by":"crossref","DOI":"10.1007\/s00204-004-0634-4","article-title":"Purification and characterization of recombinant human liver prolidase expressed in Saccharomyces cerevisiae","author":"Wang","year":"2005","journal-title":"Arch. Toxicol."},{"key":"10.1016\/j.biochi.2020.09.017_bib38","doi-asserted-by":"crossref","first-page":"5466","DOI":"10.1111\/j.1742-4658.2006.05538.x","article-title":"Human recombinant prolidase from eukaryotic and prokaryotic sources: expression, purification, characterization and long-term stability studies","volume":"273","author":"Lupi","year":"2006","journal-title":"FEBS J."},{"key":"10.1016\/j.biochi.2020.09.017_bib39","doi-asserted-by":"crossref","DOI":"10.1002\/1873-3468.13877","article-title":"Co-expression with chaperones can affect protein 3D-structure as exemplified by loss-of-function variants of human prolidase","author":"W\u0105tor","year":"2020","journal-title":"FEBS Lett."},{"key":"10.1016\/j.biochi.2020.09.017_bib40","article-title":"Phosphorylation of prolidase increases the enzyme activity","author":"Surazy\u0144ski","year":"2001","journal-title":"Mol. Cell. Biochem."},{"key":"10.1016\/j.biochi.2020.09.017_bib41","doi-asserted-by":"crossref","first-page":"554","DOI":"10.1007\/s10295-005-0059-y","article-title":"Detoxification of the organophosphate nerve agent coumaphos using organophosphorus hydrolase immobilized on cellulose materials","volume":"32","author":"Mansee","year":"2005","journal-title":"J.\u00a0Ind. Microbiol. Biotechnol."},{"key":"10.1016\/j.biochi.2020.09.017_bib42","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1016\/j.bbapap.2017.02.004","article-title":"Crystallographic structure of recombinant Lactococcus lactis prolidase to support proposed structure-function relationships","volume":"1865","author":"Kgosisejo","year":"2017","journal-title":"Biochim. Biophys. Acta Protein Proteonomics"},{"key":"10.1016\/j.biochi.2020.09.017_bib43","doi-asserted-by":"crossref","first-page":"1255","DOI":"10.1126\/science.7058344","article-title":"Hydrolysis of nerve gas by squid-type diisopropyl phosphorofluoridate hydrolyzing enzyme on agarose resin","volume":"215","author":"Hoskin","year":"1982","journal-title":"Science"},{"key":"10.1016\/j.biochi.2020.09.017_bib44","doi-asserted-by":"crossref","DOI":"10.1002\/jat.2550070107","article-title":"Discovery of multiple organofluorophosphate hydrolyzing activities in the protozoan Tetrahymena thermophila","author":"Landis","year":"1987","journal-title":"J.\u00a0Appl. Toxicol."},{"key":"10.1016\/j.biochi.2020.09.017_bib45","doi-asserted-by":"crossref","DOI":"10.1016\/0742-8413(88)90080-1","article-title":"Organofluorophosphate-hydrolyzing activity in an estuarine clam, Rangia cuneata","author":"Anderson","year":"1988","journal-title":"Comp. Biochem. Physiol. Part C, Comp"},{"key":"10.1016\/j.biochi.2020.09.017_bib46","doi-asserted-by":"crossref","DOI":"10.1016\/0006-2952(89)90144-5","article-title":"Partial characterization of an enzyme that hydrolyzes sarin, soman, tabun, and diisopropyl phosphorofluoridate (DFP)","author":"Little","year":"1989","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.biochi.2020.09.017_bib47","doi-asserted-by":"crossref","first-page":"1685","DOI":"10.1128\/aem.53.7.1685-1689.1987","article-title":"Bacterial detoxification of diisopropyl fluorophosphate","volume":"53","author":"Attaway","year":"1987","journal-title":"Appl. Environ. Microbiol."},{"key":"10.1016\/j.biochi.2020.09.017_bib48","article-title":"Affinity immobilization of a bacterial prolidase onto metal-ion-chelated magnetic nanoparticles for the hydrolysis of organophosphorus compounds","volume":"20","author":"Wang","year":"2019","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.biochi.2020.09.017_bib49","doi-asserted-by":"crossref","DOI":"10.2174\/0929866524666170428143759","article-title":"Improved hydrolysis of organophosphorus compounds by engineered human prolidases","author":"Yun","year":"2017","journal-title":"Protein Pept. Lett."},{"key":"10.1016\/j.biochi.2020.09.017_bib50","doi-asserted-by":"crossref","DOI":"10.1002\/bit.27455","article-title":"Repurposing a bacterial prolidase for organophosphorus hydrolysis: reshaped catalytic cavity switches substrate selectivity","author":"Yang","year":"2020","journal-title":"Biotechnol. Bioeng."},{"key":"10.1016\/j.biochi.2020.09.017_bib51","article-title":"Bitter taste of enzymic hydrolysates of casein - I. Isolation, structural and sensorial analysis of peptides from tryptic hydrolysates of \u03b2-casein","author":"Bumberger","year":"1993","journal-title":"Z.\u00a0Lebensm. Unters. Forsch."},{"key":"10.1016\/j.biochi.2020.09.017_bib52","article-title":"A\u00a0mechanism for bitter taste sensibility in peptides","author":"Kouge","year":"1988","journal-title":"Agric. Biol. Chem."},{"key":"10.1016\/j.biochi.2020.09.017_bib53","doi-asserted-by":"crossref","DOI":"10.1051\/lait:2004032","article-title":"Formation of bitter peptides during ripening of ovine milk cheese made with different coagulants","author":"Agboola","year":"2004","journal-title":"Lait"},{"key":"10.1016\/j.biochi.2020.09.017_bib54","doi-asserted-by":"crossref","DOI":"10.1128\/AEM.67.3.1232-1238.2001","article-title":"Expression of six peptidases from lactobacillus helveticus in Lactococcus lactis","author":"Luoma","year":"2001","journal-title":"Appl. Environ. Microbiol."},{"key":"10.1016\/j.biochi.2020.09.017_bib55","doi-asserted-by":"crossref","DOI":"10.1023\/A:1002001919720","article-title":"Peptidases and amino acid catabolism in lactic acid bacteria","author":"Christensen","year":"1999","journal-title":"Antonie van Leeuwenhoek, Int. J. Gen. Mol. Microbiol."},{"key":"10.1016\/j.biochi.2020.09.017_bib56","doi-asserted-by":"crossref","first-page":"3413","DOI":"10.1099\/00221287-148-11-3413","article-title":"Cell-wall proteinases PrtS and PrtB have a different role in Streptococcus thermophilus\/Lactobacillus bulgaricus mixed cultures in milk","volume":"148","author":"Courtin","year":"2002","journal-title":"Microbiology"},{"key":"10.1016\/j.biochi.2020.09.017_bib57","volume":"vol. 68","author":"Theriot","year":"2009"},{"key":"10.1016\/j.biochi.2020.09.017_bib58","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1111\/j.1365-2672.2012.05310.x","article-title":"Prolidase function in proline metabolism and its medical and biotechnological applications","volume":"113","author":"Kitchener","year":"2012","journal-title":"J.\u00a0Appl. Microbiol."},{"key":"10.1016\/j.biochi.2020.09.017_bib59","doi-asserted-by":"crossref","first-page":"689","DOI":"10.1001\/archderm.1981.01650110011009","article-title":"Autosomal recessive prolidase deficiency","volume":"117","author":"Ogata","year":"1981","journal-title":"Arch. Dermatol."},{"key":"10.1016\/j.biochi.2020.09.017_bib60","doi-asserted-by":"crossref","DOI":"10.1093\/jn\/138.10.2016S","article-title":"Inborn errors of proline metabolism","author":"Mitsubuchi","year":"2008","journal-title":"J.\u00a0Nutr."},{"key":"10.1016\/j.biochi.2020.09.017_bib61","doi-asserted-by":"crossref","first-page":"818","DOI":"10.1016\/0190-9622(93)70245-O","article-title":"Prolidase deficiency: a multisystemic hereditary disorder","volume":"29","author":"Bissonnette","year":"1993","journal-title":"J.\u00a0Am. Acad. Dermatol."},{"key":"10.1016\/j.biochi.2020.09.017_bib62","article-title":"Iminodipeptiduria: a genetic defect in recycling collagen; a method for determining prolidase in erythrocytes","author":"Jackson","year":"1975","journal-title":"Can. Med. Assoc. J."},{"key":"10.1016\/j.biochi.2020.09.017_bib63","doi-asserted-by":"crossref","DOI":"10.1172\/JCI114407","article-title":"Biochemical basis of prolidase deficiency: polypeptide and RNA phenotypes and the relation to clinical phenotypes","author":"Endo","year":"1990","journal-title":"J.\u00a0Clin. Invest."},{"key":"10.1016\/j.biochi.2020.09.017_bib64","article-title":"Prolidase deficiency: biochemical classification of alleles","author":"Boright","year":"1989","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.biochi.2020.09.017_bib65","doi-asserted-by":"crossref","first-page":"16970","DOI":"10.1073\/pnas.1011751107","article-title":"Polyamine pathway contributes to the pathogenesis of Parkinson disease","volume":"107","author":"Lewandowski","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"key":"10.1016\/j.biochi.2020.09.017_bib66","article-title":"Expression and molecular analysis of mutations in prolidase deficiency","author":"Ledoux","year":"1996","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.biochi.2020.09.017_bib67","first-page":"1","article-title":"Clinical genetics of prolidase deficiency: an updated review","volume":"9","author":"Spodenkiewicz","year":"2020","journal-title":"Biology (Basel)"},{"key":"10.1016\/j.biochi.2020.09.017_bib68","doi-asserted-by":"crossref","first-page":"314","DOI":"10.1007\/s00439-002-0792-5","article-title":"Mutation analysis of five new patients affected by prolidase deficiency: the lack of enzyme activity causes necrosis-like cell death in cultured fibroblasts","volume":"111","author":"Forlino","year":"2002","journal-title":"Hum. Genet."},{"key":"10.1016\/j.biochi.2020.09.017_bib69","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1111\/j.1365-2230.2006.02112.x","article-title":"A\u00a0homozygous missense mutation in PEPD encoding peptidase D causes prolidase deficiency associated with hyper-IgE syndrome","volume":"31","author":"Hershkovitz","year":"2006","journal-title":"Clin. Exp. Dermatol."},{"key":"10.1016\/j.biochi.2020.09.017_bib70","doi-asserted-by":"crossref","first-page":"500","DOI":"10.1007\/s10038-004-0180-1","article-title":"Characterization of a new PEPD allele causing prolidase deficiency in two unrelated patients: natural-occurrent mutations as a tool to investigate structure-function relationship","volume":"49","author":"Lupi","year":"2004","journal-title":"J.\u00a0Hum. Genet."},{"key":"10.1016\/j.biochi.2020.09.017_bib71","doi-asserted-by":"crossref","DOI":"10.1136\/jmg.2006.043315","article-title":"Molecular characterisation of six patients with prolidase deficiency: identification of the first small duplication in the prolidase gene and of a mutation generating symptomatic and asymptomatic outcomes within the same family","author":"Lupi","year":"2006","journal-title":"J.\u00a0Med. Genet."},{"key":"10.1016\/j.biochi.2020.09.017_bib72","article-title":"Four novel PEPD alleles causing prolidase deficiency","author":"Ledoux","year":"1994","journal-title":"Am. J. Hum. Genet."},{"key":"10.1016\/j.biochi.2020.09.017_bib73","doi-asserted-by":"crossref","first-page":"3422","DOI":"10.1111\/febs.14620","article-title":"Structural basis for prolidase deficiency disease mechanisms","volume":"285","author":"Wilk","year":"2018","journal-title":"FEBS J."},{"key":"10.1016\/j.biochi.2020.09.017_bib74","doi-asserted-by":"crossref","DOI":"10.1016\/j.gene.2012.12.070","article-title":"Identification and analysis of a novel mutation in PEPD gene in two Kashmiri siblings with prolidase enzyme deficiency","author":"Pandit","year":"2013","journal-title":"Gene"},{"key":"10.1016\/j.biochi.2020.09.017_bib75","doi-asserted-by":"crossref","DOI":"10.1002\/ajmg.b.30945","article-title":"A\u00a0broad spectrum of developmental delay in a large cohort of prolidase deficiency patients demonstrates marked interfamilial and intrafamilial phenotypic variability","author":"Falik-Zaccai","year":"2010","journal-title":"Am. J. Med. Genet. Part B Neuropsychiatr Genet"},{"key":"10.1016\/j.biochi.2020.09.017_bib76","doi-asserted-by":"crossref","DOI":"10.1001\/archderm.1979.04010010034010","article-title":"Prolidase deficiency: its dermatological manifestations and some additional biochemical studies","author":"Arata","year":"1979","journal-title":"Arch. Dermatol."},{"key":"10.1016\/j.biochi.2020.09.017_bib77","doi-asserted-by":"crossref","DOI":"10.1136\/adc.76.5.441","article-title":"Prolidase deficiency and systemic lupus erythematosus","author":"Shrinath","year":"1997","journal-title":"Arch. Dis. Child."},{"key":"10.1016\/j.biochi.2020.09.017_bib78","doi-asserted-by":"crossref","first-page":"814","DOI":"10.1007\/s10545-007-0496-z","article-title":"Systemic lupus erythematosus-like disease in a 6-year-old boy with prolidase deficiency","volume":"30","author":"Di Rocco","year":"2007","journal-title":"J.\u00a0Inherit. Metab. Dis."},{"key":"10.1016\/j.biochi.2020.09.017_bib79","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1111\/j.1651-2227.1983.tb09815.x","article-title":"Prolidase deficiency","author":"Pedersen","year":"1983","journal-title":"Acta Pediactr Scand"},{"key":"10.1016\/j.biochi.2020.09.017_bib80","doi-asserted-by":"crossref","DOI":"10.1186\/1546-0096-10-18","article-title":"Prolidase deficiency associated with systemic lupus erythematosus (SLE): single site experience and literature review","volume":"10","author":"Butbul Aviel","year":"2012","journal-title":"Pediatr. Rheumatol."},{"key":"10.1016\/j.biochi.2020.09.017_bib81","doi-asserted-by":"crossref","DOI":"10.1136\/bcr-2016-217329","article-title":"Hyperbaric oxygen therapy in the management of severe leg ulcers from prolidase deficiency","author":"Vestita","year":"2017","journal-title":"BMJ Case Rep."},{"key":"10.1016\/j.biochi.2020.09.017_bib82","doi-asserted-by":"crossref","first-page":"709","DOI":"10.1203\/00006450-198812000-00012","article-title":"In situ activation of human erythrocyte prolidase: potential for enzyme replacement therapy in prolidase deficiency","volume":"24","author":"Hechtman","year":"1988","journal-title":"Pediatr. Res."},{"key":"10.1016\/j.biochi.2020.09.017_bib83","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/j.jconrel.2004.09.013","article-title":"Intracellular delivery of liposome-encapsulated prolidase in cultured fibroblasts from prolidase-deficient patients","volume":"102","author":"Perugini","year":"2005","journal-title":"J.\u00a0Contr. Release"},{"key":"10.1016\/j.biochi.2020.09.017_bib84","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0058792","article-title":"Kinetic and structural evidences on human prolidase pathological mutants suggest strategies for enzyme functional rescue","volume":"8","author":"Besio","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.biochi.2020.09.017_bib85","doi-asserted-by":"crossref","DOI":"10.1038\/ncomms15934","article-title":"GroEL actively stimulates folding of the endogenous substrate protein PepQ","author":"Weaver","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.biochi.2020.09.017_bib86","doi-asserted-by":"crossref","DOI":"10.1038\/s41467-017-02097-9","article-title":"PEPD is a pivotal regulator of p53 tumor suppressor","volume":"8","author":"Yang","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.biochi.2020.09.017_bib87","article-title":"Prolidase and prolinase activities in moderately and poorly differentiated lung adenocarcinoma","author":"Karna","year":"1997","journal-title":"Rocz Akad Med w Bia\u0142ymstoku"},{"key":"10.1016\/j.biochi.2020.09.017_bib88","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/S0304-3835(98)00011-1","article-title":"Prolidase in human breast cancer MCF-7 cells","volume":"127","author":"Palka","year":"1998","journal-title":"Canc. Lett."},{"key":"10.1016\/j.biochi.2020.09.017_bib89","article-title":"The decrease in prolidase activity in myeloproliferative neoplasms","author":"Nowicka","year":"2012","journal-title":"Adv. Clin. Exp. Med."},{"key":"10.1016\/j.biochi.2020.09.017_bib90","doi-asserted-by":"crossref","DOI":"10.1021\/mp049922p","article-title":"Prolidase, a potential enzyme target for melanoma: design of proline-containing dipeptide-like prodrugs","author":"Mittal","year":"2005","journal-title":"Mol. Pharm."},{"key":"10.1016\/j.biochi.2020.09.017_bib91","doi-asserted-by":"crossref","first-page":"1435","DOI":"10.1002\/ijc.23263","article-title":"Extracellular matrix and HIF-1 signaling: the role of prolidase","volume":"122","author":"Surazynski","year":"2008","journal-title":"Int. J. Canc."},{"key":"10.1016\/j.biochi.2020.09.017_bib92","doi-asserted-by":"crossref","DOI":"10.4149\/neo_2013_047","article-title":"The effect of prolactin and estrogen cross-talk on prolidase- dependent signaling in MCF-7 cells","author":"Surazynski","year":"2013","journal-title":"Neoplasma"},{"key":"10.1016\/j.biochi.2020.09.017_bib93","article-title":"HIF-1\u03b1 in colorectal carcinoma: review of the literature","author":"Ioannou","year":"2015","journal-title":"J\u00a0BUON"},{"key":"10.1016\/j.biochi.2020.09.017_bib94","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejphar.2010.09.034","article-title":"Prolidase-dependent regulation of TGF c and TGF \u03b2 receptor expressions in human skin fibroblasts","author":"Surazynski","year":"2010","journal-title":"Eur. J. Pharmacol."},{"key":"10.1016\/j.biochi.2020.09.017_bib95","doi-asserted-by":"crossref","DOI":"10.1007\/s00018-019-03363-3","article-title":"Proline-dependent regulation of collagen metabolism","author":"Karna","year":"2020","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.biochi.2020.09.017_bib96","doi-asserted-by":"crossref","first-page":"319","DOI":"10.2217\/bmm-2016-0367","article-title":"Potential diagnostic and prognostic significance of plasma prolidase activity in gastric cancer","volume":"11","author":"Celik","year":"2017","journal-title":"Biomarkers Med."},{"key":"10.1016\/j.biochi.2020.09.017_bib97","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1007\/s00232-017-9971-0","article-title":"The prolidase activity, oxidative stress, and nitric oxide levels of bladder tissues with or without tumor in patients with bladder cancer","volume":"250","author":"Gecit","year":"2017","journal-title":"J.\u00a0Membr. Biol."},{"key":"10.1016\/j.biochi.2020.09.017_bib98","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1007\/s00432-011-1136-4","article-title":"Serum prolidase activity, oxidative stress, and nitric oxide levels in patients with bladder cancer","volume":"138","author":"Gecit","year":"2012","journal-title":"J.\u00a0Canc. Res. Clin. Oncol."},{"key":"10.1016\/j.biochi.2020.09.017_bib99","article-title":"Prolidase activity and oxidative stress in patients with breast carcinoma: a prospective randomized case-controlled study","author":"Bayhan","year":"2016","journal-title":"Ann. Ital. Chir."},{"key":"10.1016\/j.biochi.2020.09.017_bib100","doi-asserted-by":"crossref","DOI":"10.1111\/j.1365-2613.2006.00486.x","article-title":"Enhanced prolidase activity and decreased collagen content in breast cancer tissue","author":"Cechowska-Pasko","year":"2006","journal-title":"Int. J. Exp. Pathol."},{"key":"10.1016\/j.biochi.2020.09.017_bib101","doi-asserted-by":"crossref","DOI":"10.1016\/S0009-9120(03)00028-6","article-title":"Serum prolidase I activity and some bone metabolic markers in patients with breast cancer: in relation to menopausal status","author":"Kir","year":"2003","journal-title":"Clin. Biochem."},{"key":"10.1016\/j.biochi.2020.09.017_bib102","doi-asserted-by":"crossref","DOI":"10.1111\/IGC.0b013e3181af711e","article-title":"Serum prolidase activity and oxidative status in patients with stage I endometrial cancer","author":"Arioz","year":"2009","journal-title":"Int. J. Gynecol. Canc."},{"key":"10.1016\/j.biochi.2020.09.017_bib103","article-title":"Prolidase activity disregulation in chronic pancreatitis and pancreatic cancer","author":"Palka","year":"2002","journal-title":"Hepato-Gastroenterology"},{"key":"10.1016\/j.biochi.2020.09.017_bib104","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejogrb.2009.07.012","article-title":"Assessment of preoperative serum prolidase activity in epithelial ovarian cancer","author":"Camuzcuoglu","year":"2009","journal-title":"Eur. J. Obstet. Gynecol. Reprod. Biol."},{"key":"10.1016\/j.biochi.2020.09.017_bib105","doi-asserted-by":"crossref","DOI":"10.1111\/cen.12110","article-title":"Increased prolidase activity and oxidative stress in PCOS","author":"Hilali","year":"2013","journal-title":"Clin. Endocrinol."},{"key":"10.1016\/j.biochi.2020.09.017_bib106","doi-asserted-by":"crossref","first-page":"597","DOI":"10.2217\/bmm-2017-0306","article-title":"Plasma prolidase levels as a biomarker for polycystic ovary syndrome","volume":"12","author":"Bhatnager","year":"2018","journal-title":"Biomarkers Med."},{"key":"10.1016\/j.biochi.2020.09.017_bib107","doi-asserted-by":"crossref","first-page":"193","DOI":"10.1177\/0748233713498924","article-title":"Serum prolidase activity, oxidative stress, and antioxidant enzyme levels in patients with renal cell carcinoma","volume":"32","author":"Pirin\u00e7\u00e7i","year":"2016","journal-title":"Toxicol. Ind. Health"},{"key":"10.1016\/j.biochi.2020.09.017_bib108","doi-asserted-by":"crossref","first-page":"206","DOI":"10.5606\/tgkdc.dergisi.2019.16888","article-title":"Serum prolidase activity, total oxidant\/antioxidant, and nitric oxide levels in patients with esophageal squamous cell carcinoma","volume":"27","author":"Say\u0131r","year":"2019","journal-title":"Turkish J Thorac Cardiovasc Surg"},{"key":"10.1016\/j.biochi.2020.09.017_bib109","doi-asserted-by":"crossref","DOI":"10.2147\/DDDT.S135949","article-title":"Differential effect of platelet-rich plasma fractions on \u03b21-integrin signaling, collagen biosynthesis, and prolidase activity in human skin fibroblasts","author":"Guszczyn","year":"2017","journal-title":"Drug Des. Dev. Ther."},{"key":"10.1016\/j.biochi.2020.09.017_bib110","doi-asserted-by":"crossref","first-page":"670","DOI":"10.1159\/000480653","article-title":"Functional consequences of intracellular proline levels manipulation affecting PRODH\/POX-Dependent pro-apoptotic pathways in a novel in\u00a0vitro cell culture model","volume":"43","author":"Zareba","year":"2017","journal-title":"Cell. Physiol. Biochem."},{"key":"10.1016\/j.biochi.2020.09.017_bib111","article-title":"Cancer progression is mediated by proline catabolism in non-small cell lung cancer","author":"Liu","year":"2020","journal-title":"Oncogene"},{"key":"10.1016\/j.biochi.2020.09.017_bib112","doi-asserted-by":"crossref","DOI":"10.1007\/s11010-020-03685-y","article-title":"Understanding the role of key amino acids in regulation of proline dehydrogenase\/proline oxidase (prodh\/pox)-dependent apoptosis\/autophagy as an approach to targeted cancer therapy","author":"Huynh","year":"2020","journal-title":"Mol. Cell. Biochem."},{"key":"10.1016\/j.biochi.2020.09.017_bib113","doi-asserted-by":"crossref","DOI":"10.1038\/cddis.2014.187","article-title":"Identification of prolidase as a high affinity ligand of the ErbB2 receptor and its regulation of ErbB2 signaling and cell growth","volume":"5","author":"Yang","year":"2014","journal-title":"Cell Death Dis."},{"key":"10.1016\/j.biochi.2020.09.017_bib114","doi-asserted-by":"crossref","DOI":"10.1016\/j.jconrel.2010.04.009","article-title":"The role of HER2 in cancer therapy and targeted drug delivery","author":"Tai","year":"2010","journal-title":"J.\u00a0Contr. Release"},{"key":"10.1016\/j.biochi.2020.09.017_bib115","doi-asserted-by":"crossref","DOI":"10.1007\/s12282-015-0587-x","article-title":"HER2-directed therapy: current treatment options for HER2-positive breast cancer","author":"Ahmed","year":"2015","journal-title":"Breast Cancer"},{"key":"10.1016\/j.biochi.2020.09.017_bib116","doi-asserted-by":"crossref","DOI":"10.1016\/j.ajpath.2013.07.005","article-title":"Targeted therapy for breast cancer","author":"Mohamed","year":"2013","journal-title":"Am. J. Pathol."},{"key":"10.1016\/j.biochi.2020.09.017_bib117","doi-asserted-by":"crossref","DOI":"10.1016\/j.ctrv.2008.09.003","article-title":"HER2-targeted therapy in breast cancer. Monoclonal antibodies and tyrosine kinase inhibitors","author":"Nielsen","year":"2009","journal-title":"Canc. Treat Rev."},{"key":"10.1016\/j.biochi.2020.09.017_bib118","doi-asserted-by":"crossref","DOI":"10.1016\/S1535-6108(04)00083-2","article-title":"Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex","author":"Franklin","year":"2004","journal-title":"Canc. Cell"},{"key":"10.1016\/j.biochi.2020.09.017_bib119","doi-asserted-by":"crossref","DOI":"10.1016\/j.ccr.2009.03.020","article-title":"Ligand-independent HER2\/HER3\/PI3K complex is disrupted by trastuzumab and is effectively inhibited by the PI3K inhibitor GDC-0941","author":"Junttila","year":"2009","journal-title":"Canc. Cell"},{"key":"10.1016\/j.biochi.2020.09.017_bib120","doi-asserted-by":"crossref","first-page":"42340","DOI":"10.18632\/oncotarget.9851","article-title":"Dual inhibition of ErbB1 and ErbB2 in cancer by recombinant human prolidase mutant hPEPD-G278D","volume":"7","author":"Yang","year":"2016","journal-title":"Oncotarget"},{"key":"10.1016\/j.biochi.2020.09.017_bib121","doi-asserted-by":"crossref","first-page":"396","DOI":"10.1016\/j.ebiom.2015.03.016","article-title":"Inhibition of ERBB2-overexpressing tumors by recombinant human prolidase and its enzymatically inactive mutant","volume":"2","author":"Yang","year":"2015","journal-title":"EBioMedicine"},{"key":"10.1016\/j.biochi.2020.09.017_bib122","doi-asserted-by":"crossref","DOI":"10.1002\/(SICI)1097-4644(19971101)67:2<166::AID-JCB2>3.0.CO;2-V","article-title":"Prolidase activity in fibroblasts is regulated by interaction of extracellular matrix with cell surface integrin receptors","author":"Palka","year":"1997","journal-title":"J.\u00a0Cell. Biochem."},{"key":"10.1016\/j.biochi.2020.09.017_bib123","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1186\/s13052-014-0095-1","article-title":"Serum prolidase activity and oxidant-antioxidant status in children with chronic hepatitis B virus infection","volume":"40","author":"\u015een","year":"2014","journal-title":"Ital. J. Pediatr."},{"key":"10.1016\/j.biochi.2020.09.017_bib124","doi-asserted-by":"crossref","first-page":"1479","DOI":"10.3906\/sag-1902-122","article-title":"Serum prolidase level in patients with brucellosis and its possible relationship with pathogenesis of the disease: a prospective observational study","volume":"49","author":"Dizdar","year":"2019","journal-title":"Turk. J. Med. Sci."},{"key":"10.1016\/j.biochi.2020.09.017_bib125","first-page":"206","article-title":"Evaluation of serum prolidase activity in patients with slow coronary flow","volume":"11","author":"Suner","year":"2015","journal-title":"Postep w Kardiol Interwencyjnej"},{"key":"10.1016\/j.biochi.2020.09.017_bib126","article-title":"The association of serum prolidase activity with the presence and severity of coronary artery disease","author":"Yildiz","year":"2008","journal-title":"Coron. Artery Dis."},{"key":"10.1016\/j.biochi.2020.09.017_bib127","doi-asserted-by":"crossref","DOI":"10.1007\/s10072-011-0857-0","article-title":"Serum prolidase activity and oxidative status in patients with diabetic neuropathy","author":"Uzar","year":"2012","journal-title":"Neurol. Sci."},{"key":"10.1016\/j.biochi.2020.09.017_bib128","doi-asserted-by":"crossref","DOI":"10.1155\/2014\/291458","article-title":"Serum prolidase activity and oxidative stress in diabetic Nephropathy and End stage renal disease: a correlative study with glucose and creatinine","volume":"2014","author":"Verma","year":"2014","journal-title":"Biochem Res Int"},{"key":"10.1016\/j.biochi.2020.09.017_bib129","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1186\/1758-5996-6-142","article-title":"Serum prolidase activity is associated with non-diabetic metabolic syndrome","volume":"6","author":"Tabur","year":"2014","journal-title":"Diabetol. Metab. Syndrome"},{"key":"10.1016\/j.biochi.2020.09.017_bib130","doi-asserted-by":"crossref","first-page":"69","DOI":"10.2174\/1386207322666190306143317","article-title":"The relationship between prolidase activity and atrial electromechanical changes in patients with paroxysmal atrial fibrillation","volume":"22","author":"Tascanov","year":"2019","journal-title":"Comb. Chem. High Throughput Screen."},{"key":"10.1016\/j.biochi.2020.09.017_bib131","doi-asserted-by":"crossref","first-page":"1339","DOI":"10.1007\/s00417-016-3338-6","article-title":"Serum prolidase activity and oxidative stress in patients with pseudoexfoliation syndrome","volume":"254","author":"Tetiko\u011flu","year":"2016","journal-title":"Graefe\u2019s Arch. Clin. Exp. Ophthalmol."},{"key":"10.1016\/j.biochi.2020.09.017_bib132","doi-asserted-by":"crossref","first-page":"29","DOI":"10.4137\/CMAMD.S12602","article-title":"Serum prolidase activity in ankylosing spondylitis and rheumatoid arthritis","volume":"6","author":"U\u00e7ar","year":"2013","journal-title":"Clin. Med. Insights Arthritis Musculoskelet. Disord."},{"key":"10.1016\/j.biochi.2020.09.017_bib133","doi-asserted-by":"crossref","DOI":"10.1016\/S0009-9120(02)00305-3","article-title":"Serum prolidase activity as a marker of osteoporosis in type 2 diabetes mellitus","author":"Erba\u01e7ci","year":"2002","journal-title":"Clin. Biochem."},{"key":"10.1016\/j.biochi.2020.09.017_bib134","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1159\/000183046","article-title":"Prolidase and prolinase activities in the erythrocytes of patients with chronic uremia","volume":"35","author":"Gejyo","year":"1983","journal-title":"Nephron"},{"key":"10.1016\/j.biochi.2020.09.017_bib135","doi-asserted-by":"crossref","first-page":"1020","DOI":"10.1016\/j.clinbiochem.2007.05.015","article-title":"Serum prolidase activity in patients with hypertension and its relation with left ventricular hypertrophy","volume":"40","author":"Demirbag","year":"2007","journal-title":"Clin. Biochem."},{"key":"10.1016\/j.biochi.2020.09.017_bib136","doi-asserted-by":"crossref","first-page":"102242","DOI":"10.1016\/j.ajp.2020.102242","article-title":"Increased prolidase activity in Alzheimer\u2019s dementia: a case-control study","volume":"53","author":"Krishna","year":"2020","journal-title":"Asian J Psychiatr"},{"key":"10.1016\/j.biochi.2020.09.017_bib137","doi-asserted-by":"crossref","first-page":"2117","DOI":"10.1007\/s10072-013-1346-4","article-title":"Relationship of cognitive performance with prolidase and oxidative stress in Alzheimer disease","volume":"34","author":"Arikanoglu","year":"2013","journal-title":"Neurol. Sci."},{"key":"10.1016\/j.biochi.2020.09.017_bib138","article-title":"Plasma prolidase activity and oxidative stress in patients with Parkinson\u2019s disease","volume":"2015","author":"Verma","year":"2015","journal-title":"Parkinsons Dis"},{"key":"10.1016\/j.biochi.2020.09.017_bib139","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1016\/j.ajp.2016.10.008","article-title":"Oxidative status and prolidase activities in generalized anxiety disorder","volume":"25","author":"Ercan","year":"2017","journal-title":"Asian J Psychiatr"},{"key":"10.1016\/j.biochi.2020.09.017_bib140","first-page":"314","article-title":"Prolidase activity and oxidative stress in patients with major depressive disorder","volume":"26","author":"Kokacya","year":"2014","journal-title":"Psychiatr. Danub."},{"key":"10.1016\/j.biochi.2020.09.017_bib141","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1016\/j.psychres.2018.11.066","article-title":"Increased prolidase activity and high blood monocyte counts in pediatric bipolar disorder","volume":"271","author":"Ceylan","year":"2019","journal-title":"Psychiatr. Res."},{"key":"10.1016\/j.biochi.2020.09.017_bib142","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1016\/j.neulet.2015.12.036","article-title":"Diagnostic performance of increased prolidase activity in schizophrenia","volume":"613","author":"G\u00fcne\u015f","year":"2016","journal-title":"Neurosci. Lett."},{"key":"10.1016\/j.biochi.2020.09.017_bib143","doi-asserted-by":"crossref","first-page":"27","DOI":"10.5152\/eurasianjmed.2018.18183","article-title":"Serum prolidase enzyme activity level: not a predictive biomarker for epilepsy","volume":"51","author":"Ozozen Ayas","year":"2019","journal-title":"Eurasian J Med"},{"key":"10.1016\/j.biochi.2020.09.017_bib144","doi-asserted-by":"crossref","DOI":"10.1016\/S0736-5748(02)00109-0","article-title":"Proline induces oxidative stress in cerebral cortex of rats","author":"Delwing","year":"2003","journal-title":"Int. J. Dev. Neurosci."},{"key":"10.1016\/j.biochi.2020.09.017_bib145","doi-asserted-by":"crossref","DOI":"10.1007\/s00726-005-0186-9","article-title":"Effect of hyperprolinemia on acetylcholinesterase and butyrylcholinesterase activities in rat","author":"Delwing","year":"2005","journal-title":"Amino Acids"},{"key":"10.1016\/j.biochi.2020.09.017_bib146","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbagen.2020.129636","article-title":"Human proline specific peptidases: a comprehensive analysis","author":"Dunaevsky","year":"2020","journal-title":"Biochim. Biophys. Acta Gen. Subj."},{"key":"10.1016\/j.biochi.2020.09.017_bib147","doi-asserted-by":"crossref","DOI":"10.1146\/annurev.nutr.012809.104638","article-title":"Proline metabolism and microenvironmental stress","author":"Phang","year":"2010","journal-title":"Annu. Rev. Nutr."}],"container-title":["Biochimie"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908420302236?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0300908420302236?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,4]],"date-time":"2025-10-04T01:16:55Z","timestamp":1759540615000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0300908420302236"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2021,4]]},"references-count":147,"alternative-id":["S0300908420302236"],"URL":"https:\/\/doi.org\/10.1016\/j.biochi.2020.09.017","relation":{},"ISSN":["0300-9084"],"issn-type":[{"value":"0300-9084","type":"print"}],"subject":[],"published":{"date-parts":[[2021,4]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Prolidase \u2013 A protein with many faces","name":"articletitle","label":"Article Title"},{"value":"Biochimie","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.biochi.2020.09.017","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Elsevier B.V. and Soci\u00e9t\u00e9 Fran\u00e7aise de Biochimie et Biologie Mol\u00e9culaire (SFBBM). All rights reserved.","name":"copyright","label":"Copyright"}]}}