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rdf:type |
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lifeskim:mentions |
umls-concept:C0033684,
umls-concept:C0041538,
umls-concept:C0077678,
umls-concept:C0208355,
umls-concept:C0243041,
umls-concept:C0392337,
umls-concept:C1514562,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C1948027
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pubmed:issue |
20
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pubmed:dateCreated |
2001-10-25
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pubmed:abstractText |
Molecular chaperones recognize nonnative proteins and orchestrate cellular folding processes in conjunction with regulatory cofactors. However, not every attempt to fold a protein is successful, and misfolded proteins can be directed to the cellular degradation machinery for destruction. Molecular mechanisms underlying the cooperation of molecular chaperones with the degradation machinery remain largely enigmatic so far.
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pubmed:commentsCorrections |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/BCL2-associated athanogene 1 protein,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HSC70 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HSP70 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HSPA8 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/STUB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0960-9822
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1569-77
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11676916-Carrier Proteins,
pubmed-meshheading:11676916-Cysteine Endopeptidases,
pubmed-meshheading:11676916-DNA-Binding Proteins,
pubmed-meshheading:11676916-HSC70 Heat-Shock Proteins,
pubmed-meshheading:11676916-HSP70 Heat-Shock Proteins,
pubmed-meshheading:11676916-HeLa Cells,
pubmed-meshheading:11676916-Humans,
pubmed-meshheading:11676916-Hydrolysis,
pubmed-meshheading:11676916-Ligases,
pubmed-meshheading:11676916-Molecular Chaperones,
pubmed-meshheading:11676916-Multienzyme Complexes,
pubmed-meshheading:11676916-Proteasome Endopeptidase Complex,
pubmed-meshheading:11676916-Protein Folding,
pubmed-meshheading:11676916-Transcription Factors,
pubmed-meshheading:11676916-Ubiquitin,
pubmed-meshheading:11676916-Ubiquitin-Protein Ligases
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pubmed:year |
2001
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pubmed:articleTitle |
Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling.
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pubmed:affiliation |
Abteilung für Molekulare Zellbiologie, Max-Planck-Institut für Biochemie, D-82152, Martinsried, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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