{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,15]],"date-time":"2026-04-15T23:58:05Z","timestamp":1776297485393,"version":"3.50.1"},"reference-count":14,"publisher":"Oxford University Press (OUP)","issue":"3","license":[{"start":{"date-parts":[[2019,8,8]],"date-time":"2019-08-08T00:00:00Z","timestamp":1565222400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"funder":[{"name":"European Research Council under the European Union's Horizon 2020","award":["647458"],"award-info":[{"award-number":["647458"]}]},{"name":"University of Leuven"},{"name":"Scientific Research Flanders"},{"name":"Flanders Agency for innovation by Science and Technology","award":["60839"],"award-info":[{"award-number":["60839"]}]},{"name":"Federal Office for Scientific Affairs of Belgium"},{"name":"Erasmus Mundus fellowship"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2020,2,1]]},"abstract":"<jats:title>Abstract<\/jats:title>\n               <jats:sec>\n                  <jats:title>Motivation<\/jats:title>\n                  <jats:p>In vivo protein folding is governed by molecular chaperones, that escort proteins from their translational birth to their proteolytic degradation. In E.coli the main classes of chaperones that interact with the nascent chain are trigger factor, DnaK\/J and GroEL\/ES and several authors have performed whole-genome experiments to construct exhaustive client lists for each of these.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec>\n                  <jats:title>Results<\/jats:title>\n                  <jats:p>We constructed a database collecting all publicly available data of experimental chaperone-interaction and -dependency data for the E.coli proteome, and enriched it with an extensive set of protein-specific as well as cell context-dependent proteostatic parameters. We made this publicly accessible via a web interface that allows to search for proteins or chaperone client lists, but also to profile user-specified datasets against all the collected parameters. We hope this will accelerate research in this field by quickly identifying differentiating features in datasets.<\/jats:p>\n               <\/jats:sec>\n               <jats:sec>\n                  <jats:title>Availability and implementation<\/jats:title>\n                  <jats:p>The Protein Homeostasis Database is freely available without any registration requirement at http:\/\/PHDB.switchlab.org\/.<\/jats:p>\n               <\/jats:sec>","DOI":"10.1093\/bioinformatics\/btz628","type":"journal-article","created":{"date-parts":[[2019,8,6]],"date-time":"2019-08-06T19:17:18Z","timestamp":1565119038000},"page":"948-949","source":"Crossref","is-referenced-by-count":5,"title":["Protein Homeostasis Database: protein quality control in <i>E.coli<\/i>"],"prefix":"10.1093","volume":"36","author":[{"given":"Reshmi","family":"Ramakrishnan","sequence":"first","affiliation":[{"name":"Switch Laboratory, VIB-KU Leuven Center for Brain & Disease Research , VIB, Leuven 3000, Belgium"},{"name":"Department of Cellular and Molecular Medicine, KU Leuven , Leuven 3000, Belgium"}]},{"given":"Bert","family":"Houben","sequence":"additional","affiliation":[{"name":"Switch Laboratory, VIB-KU Leuven Center for Brain & Disease Research , VIB, Leuven 3000, Belgium"},{"name":"Department of Cellular and Molecular Medicine, KU Leuven , Leuven 3000, Belgium"}]},{"given":"\u0141ukasz","family":"Kreft","sequence":"additional","affiliation":[{"name":"VIB Bioinformatics Core , VIB, Gent 9052, Belgium"}]},{"given":"Alexander","family":"Botzki","sequence":"additional","affiliation":[{"name":"VIB Bioinformatics Core , VIB, Gent 9052, Belgium"}]},{"ORCID":"https:\/\/orcid.org\/0000-0003-2020-0168","authenticated-orcid":false,"given":"Joost","family":"Schymkowitz","sequence":"additional","affiliation":[{"name":"Switch Laboratory, VIB-KU Leuven Center for Brain & Disease Research , VIB, Leuven 3000, Belgium"},{"name":"Department of Cellular and Molecular Medicine, KU Leuven , Leuven 3000, Belgium"}]},{"given":"Frederic","family":"Rousseau","sequence":"additional","affiliation":[{"name":"Switch Laboratory, VIB-KU Leuven Center for Brain & Disease Research , VIB, Leuven 3000, Belgium"},{"name":"Department of Cellular and Molecular Medicine, KU Leuven , Leuven 3000, Belgium"}]}],"member":"286","published-online":{"date-parts":[[2019,8,8]]},"reference":[{"key":"2023013110090003000_btz628-B1","doi-asserted-by":"crossref","first-page":"686","DOI":"10.1101\/gr.4527806","article-title":"Large-scale identification of protein-protein interaction of Escherichia coli K-12","volume":"16","author":"Arifuzzaman","year":"2006","journal-title":"Genome Res"},{"key":"2023013110090003000_btz628-B2","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1016\/j.celrep.2011.12.007","article-title":"DnaK functions as a central hub in the E. coli chaperone network","volume":"1","author":"Calloni","year":"2012","journal-title":"Cell Rep"},{"key":"2023013110090003000_btz628-B3","doi-asserted-by":"crossref","first-page":"15800","DOI":"10.1073\/pnas.0607534103","article-title":"Global aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL","volume":"103","author":"Chapman","year":"2006","journal-title":"Proc. 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