{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,20]],"date-time":"2026-09-20T14:10:34Z","timestamp":1789913434506,"version":"4.0.1"},"reference-count":68,"publisher":"MDPI AG","issue":"12","license":[{"start":{"date-parts":[[2014,12,17]],"date-time":"2014-12-17T00:00:00Z","timestamp":1418774400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Thioredoxin domain-containing 5 (TXNDC5) is a member of the protein disulfide isomerase family, acting as a chaperone of endoplasmic reticulum under not  fully characterized conditions As a result, TXNDC5 interacts with many cell proteins, contributing to their proper folding and correct formation of disulfide bonds through its thioredoxin domains. Moreover, it can also work as an electron transfer reaction, recovering the functional isoform of other protein disulfide isomerases, replacing reduced glutathione in its role. Finally, it also acts as a cellular adapter, interacting with the N-terminal domain of adiponectin receptor. As can be inferred from all these functions, TXNDC5 plays  an important role in cell physiology; therefore, dysregulation of its expression is associated with oxidative stress, cell ageing and a large range of pathologies such as arthritis, cancer, diabetes, neurodegenerative diseases, vitiligo and virus infections. Its implication in all these important diseases has made TXNDC5 a susceptible biomarker or even a potential pharmacological target.<\/jats:p>","DOI":"10.3390\/ijms151223501","type":"journal-article","created":{"date-parts":[[2014,12,17]],"date-time":"2014-12-17T10:19:28Z","timestamp":1418811568000},"page":"23501-23518","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":79,"title":["TXNDC5, a Newly Discovered Disulfide Isomerase with a Key Role in Cell Physiology and Pathology"],"prefix":"10.3390","volume":"15","author":[{"given":"Elena","family":"Horna-Terr\u00f3n","sequence":"first","affiliation":[{"name":"Grado de Biotecnolog\u00eda, Universidad de Zaragoza, Zaragoza E-50013, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Alberto","family":"Pradilla-Dieste","sequence":"additional","affiliation":[{"name":"Grado de Biotecnolog\u00eda, Universidad de Zaragoza, Zaragoza E-50013, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cristina","family":"S\u00e1nchez-de-Diego","sequence":"additional","affiliation":[{"name":"Grado de Biotecnolog\u00eda, Universidad de Zaragoza, Zaragoza E-50013, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8251-8457","authenticated-orcid":false,"given":"Jes\u00fas","family":"Osada","sequence":"additional","affiliation":[{"name":"Departamento Bioqu\u00edmica y Biolog\u00eda Molecular y Celular, Facultad de Veterinaria,  Instituto de Investigaci\u00f3n Sanitaria de Arag\u00f3n (IIS), Universidad de Zaragoza,  Zaragoza E-50013, Spain"},{"name":"CIBER de Fisiopatolog\u00eda de la Obesidad y Nutrici\u00f3n, Instituto de Salud Carlos III,  Madrid E-28029, Spain"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2014,12,17]]},"reference":[{"key":"ref_1","unstructured":"Thioredoxin Domain Containing 5. 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