La protéine GroEL appartient à la famille des chaperonines des molécules chaperonnes, et se trouve chez un grand nombre de bactéries. Elle est nécessaire pour le repliement efficace de nombreuses protéines. Afin de fonctionner efficacement, GroEL requiert le complexe protéique couvercle associé GroES.

PropertyValue
dbpedia-owl:abstract
  • La protéine GroEL appartient à la famille des chaperonines des molécules chaperonnes, et se trouve chez un grand nombre de bactéries. Elle est nécessaire pour le repliement efficace de nombreuses protéines. Afin de fonctionner efficacement, GroEL requiert le complexe protéique couvercle associé GroES. Chez les eukaryotes, les protéines Hsp60 et Hsp10 sont structurellement et fonctionnellement presque identiques à GroEL et GroES, respectivement.
  • GroEL belongs to the chaperonin family of molecular chaperones, and is found in a large number of bacteria. It is required for the proper folding of many proteins. To function properly, GroEL requires the lid-like cochaperonin protein complex GroES. In eukaryotes the proteins Hsp60 and Hsp10 are structurally and functionally nearly identical to GroEL and GroES, respectively.
  • GroEL es una chaperona molecular de Escherichia coli de 60 kDa que forma un complejo cilíndrico activo de dos anillos que contienen 7 sub-unidades de GroEL cada uno. GroEL junto con GroES forman parte del complejo molecular llamado GroEL/GroES.
dbpedia-owl:wikiPageExternalLink
dbpedia-owl:wikiPageID
  • 4803532 (xsd:integer)
dbpedia-owl:wikiPageLength
  • 13999 (xsd:integer)
dbpedia-owl:wikiPageOutDegree
  • 22 (xsd:integer)
dbpedia-owl:wikiPageRevisionID
  • 108187733 (xsd:integer)
dbpedia-owl:wikiPageWikiLink
prop-fr:auteur
  • Baca-Estrada ME, Gupta RS, Stead RH, Croitoru K
  • Brudzynski K, Martinez V, Gupta RS
  • Corbett JM, Wheeler CH, Baker CS, et al.
  • Dawson SJ, White LA
  • Hochstrasser DF, Frutiger S, Paquet N, et al.
  • Ikawa S, Weinberg RA
  • Jindal S, Dudani AK, Singh B, et al.
  • Kreisel W, Hildebrandt H, Schiltz E, et al.
  • Liu Y, Steinacker JM
  • Mayhew M, da Silva AC, Martin J, et al.
  • Moseley P
  • Schäfer C, Williams JA
  • Singh B, Patel HV, Ridley RG, et al.
  • Tabibzadeh S, Broome J
  • Tabibzadeh S, Kong QF, Satyaswaroop PG, Babaknia A
  • Van Maele B, Debyser Z
  • Venner TJ, Singh B, Gupta RS
  • Waldinger D, Eckerskorn C, Lottspeich F, Cleve H
  • Ward LD, Hong J, Whitehead RH, Simpson RJ
  • Vélez-Granell CS, Arias AE, Torres-Ruíz JA, Bendayan M
prop-fr:date
  • 1989 (xsd:integer)
  • 1990 (xsd:integer)
  • 1991 (xsd:integer)
  • 1992 (xsd:integer)
  • 1993 (xsd:integer)
  • 1994 (xsd:integer)
  • 1995 (xsd:integer)
  • 1996 (xsd:integer)
  • 1999 (xsd:integer)
  • 2000 (xsd:integer)
  • 2001 (xsd:integer)
  • 2005 (xsd:integer)
prop-fr:doi
  • 10.100200 (xsd:double)
  • 10.100700 (xsd:double)
  • 10.101600 (xsd:double)
  • 10.103800 (xsd:double)
  • 10.107300 (xsd:double)
  • 10.108900 (xsd:double)
  • 10.274100 (xsd:double)
prop-fr:issue
  • 1 (xsd:integer)
  • 2 (xsd:integer)
  • 3 (xsd:integer)
  • 4 (xsd:integer)
  • 5 (xsd:integer)
  • 6 (xsd:integer)
  • 8 (xsd:integer)
  • 10 (xsd:integer)
  • 11 (xsd:integer)
  • 12 (xsd:integer)
  • 6564 (xsd:integer)
prop-fr:journal
  • Nature
  • Mol. Cell. Biol.
  • Proc. Natl. Acad. Sci. U.S.A.
  • Electrophoresis
  • J. Cell. Sci.
  • Biochem. Biophys. Res. Commun.
  • AIDS reviews
  • Acta Histochem.
  • Biol. Chem. Hoppe-Seyler
  • DNA Cell Biol.
  • Diabetologia
  • Dig. Dis. Sci.
  • Front. Biosci.
  • Hum. Reprod.
  • Immunopharmacology
  • Infectious diseases in obstetrics and gynecology
  • J. Gastroenterol.
  • J. Infect.
prop-fr:langue
  • en
prop-fr:pages
  • 1 (xsd:integer)
  • 5 (xsd:integer)
  • 26 (xsd:integer)
  • 51 (xsd:integer)
  • 299 (xsd:integer)
  • 316 (xsd:integer)
  • 317 (xsd:integer)
  • 391 (xsd:integer)
  • 420 (xsd:integer)
  • 498 (xsd:integer)
  • 539 (xsd:integer)
  • 545 (xsd:integer)
  • 633 (xsd:integer)
  • 883 (xsd:integer)
  • 992 (xsd:integer)
  • 1185 (xsd:integer)
  • 1459 (xsd:integer)
  • 2012 (xsd:integer)
  • 2279 (xsd:integer)
  • D12–25
prop-fr:pmid
  • 1286669 (xsd:integer)
  • 1347942 (xsd:integer)
  • 1516759 (xsd:integer)
  • 1602151 (xsd:integer)
  • 1972619 (xsd:integer)
  • 1980192 (xsd:integer)
  • 2079031 (xsd:integer)
  • 2568584 (xsd:integer)
  • 2907406 (xsd:integer)
  • 7518175 (xsd:integer)
  • 7895732 (xsd:integer)
  • 7907543 (xsd:integer)
  • 7911805 (xsd:integer)
  • 8559246 (xsd:integer)
  • 8671282 (xsd:integer)
  • 10231001 (xsd:integer)
  • 10632533 (xsd:integer)
  • 10960671 (xsd:integer)
  • 11145923 (xsd:integer)
  • 15875659 (xsd:integer)
prop-fr:titre
  • Immunocytochemical localization of heat-shock protein 60-related protein in beta-cell secretory granules and its altered distribution in non-obese diabetic mice
  • Molecular chaperones in pancreatic tissue: the presence of cpn10, cpn60 and hsp70 in distinct compartments along the secretory pathway of the acinar cells
  • The human myocardial two-dimensional gel protein database: update 1994
  • Changes in skeletal muscle heat shock proteins: pathological significance
  • HIV-1 integration: an interplay between HIV-1 integrase, cellular and viral proteins
  • Palaeos Bacteria: Pieces: GroEL
  • Stress proteins and the immune response
  • Nucleotide sequences and novel structural features of human and Chinese hamster hsp60 gene families
  • Intestinal expression and cellular immune responses to human heat-shock protein 60 in Crohn's disease
  • Protein folding in the central cavity of the GroEL-GroES chaperonin complex
  • Amino-acid sequence homology of a polymorphic cellular protein from human lymphocytes and the chaperonins from Escherichia coli and chloroplasts
  • Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin
  • Primary structure of a human mitochondrial protein homologous to the bacterial and plant chaperonins and to the 65-kilodalton mycobacterial antigen
  • Immuno-gold electron microscopical detection of heat shock protein 60 in mitochondria of rat hepatocytes and myocardiocytes
  • Heat shock proteins in human endometrium throughout the menstrual cycle
  • Stress kinases and heat shock proteins in the pancreas: possible roles in normal function and disease
  • Mitochondrial import of the human chaperonin protein
  • Development of a database of amino acid sequences for human colon carcinoma proteins separated by two-dimensional polyacrylamide gel electrophoresis
  • An interaction between p21ras and heat shock protein hsp60, a chaperonin
  • Human liver protein map: a reference database established by microsequencing and gel comparison
prop-fr:url
prop-fr:volume
  • 6 (xsd:integer)
  • 7 (xsd:integer)
  • 9 (xsd:integer)
  • 11 (xsd:integer)
  • 13 (xsd:integer)
  • 15 (xsd:integer)
  • 24 (xsd:integer)
  • 35 (xsd:integer)
  • 39 (xsd:integer)
  • 48 (xsd:integer)
  • 89 (xsd:integer)
  • 96 (xsd:integer)
  • 107 (xsd:integer)
  • 169 (xsd:integer)
  • 369 (xsd:integer)
  • 379 (xsd:integer)
prop-fr:wikiPageUsesTemplate
dcterms:subject
rdfs:comment
  • La protéine GroEL appartient à la famille des chaperonines des molécules chaperonnes, et se trouve chez un grand nombre de bactéries. Elle est nécessaire pour le repliement efficace de nombreuses protéines. Afin de fonctionner efficacement, GroEL requiert le complexe protéique couvercle associé GroES.
  • GroEL belongs to the chaperonin family of molecular chaperones, and is found in a large number of bacteria. It is required for the proper folding of many proteins. To function properly, GroEL requires the lid-like cochaperonin protein complex GroES. In eukaryotes the proteins Hsp60 and Hsp10 are structurally and functionally nearly identical to GroEL and GroES, respectively.
  • GroEL es una chaperona molecular de Escherichia coli de 60 kDa que forma un complejo cilíndrico activo de dos anillos que contienen 7 sub-unidades de GroEL cada uno. GroEL junto con GroES forman parte del complejo molecular llamado GroEL/GroES.
rdfs:label
  • GroEL
  • GroEL
  • GroEL
owl:sameAs
http://www.w3.org/ns/prov#wasDerivedFrom
foaf:isPrimaryTopicOf
is dbpedia-owl:wikiPageWikiLink of
is foaf:primaryTopic of