{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T17:40:16Z","timestamp":1791222016546,"version":"4.1.0"},"reference-count":25,"publisher":"Oxford University Press (OUP)","issue":"2","license":[{"start":{"date-parts":[[2020,4,27]],"date-time":"2020-04-27T00:00:00Z","timestamp":1587945600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"funder":[{"DOI":"10.13039\/501100006143","name":"Department of Science and Technology","doi-asserted-by":"publisher","award":["INT\/RUS\/RSF\/P-09"],"award-info":[{"award-number":["INT\/RUS\/RSF\/P-09"]}],"id":[{"id":"10.13039\/501100006143","id-type":"DOI","asserted-by":"publisher"}]},{"name":"Ministry of Human Resource Development and Initiative for Biological Systems Engineering Travel"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2021,3,22]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:p>The functions of membrane proteins (MPs) are attributed to their structure and stability. Factors influencing the stability of MPs differ from globular proteins due to the presence of membrane spanning regions. Thermodynamic data of MPs aid to understand the relationship among their structure, stability and function. Although a wealth of experimental data on thermodynamics of MPs are reported in the literature, there is no database available explicitly for MPs. In this work, we have developed a database for MP thermodynamics, MPTherm, which contains more than 7000 thermodynamic data from about 320 MPs. Each entry contains protein sequence and structural information, membrane topology, experimental conditions, thermodynamic parameters such as melting temperature, free energy, enthalpy etc. and literature information. MPTherm assists users to retrieve the data by using different search and display options. We have also provided the sequence and structure visualization as well as cross-links to UniProt and PDB databases. MPTherm database is freely available at http:\/\/www.iitm.ac.in\/bioinfo\/mptherm\/. It is implemented in HTML, PHP, MySQL and JavaScript, and supports the latest versions of major browsers, such as Firefox, Chrome and Opera. MPTherm would serve as an effective resource for understanding the stability of MPs, development of prediction tools and identifying drug targets for diseases associated with MPs.<\/jats:p>","DOI":"10.1093\/bib\/bbaa064","type":"journal-article","created":{"date-parts":[[2020,3,31]],"date-time":"2020-03-31T11:10:22Z","timestamp":1585653022000},"page":"2119-2125","source":"Crossref","is-referenced-by-count":28,"title":["MPTherm: database for membrane protein thermodynamics for understanding folding and stability"],"prefix":"10.1093","volume":"22","author":[{"given":"A","family":"Kulandaisamy","sequence":"first","affiliation":[{"name":"Bharathidasan University, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R","family":"Sakthivel","sequence":"additional","affiliation":[{"name":"Medical Biochemistry from University of Madras, India"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M 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