GroEL binds to and unfolds rhodanese posttranslationally.

GroEL binds to and unfolds rhodanese posttranslationally.

Item
http://www.wikidata.org/entity/Q38360171
Complexes between nascent polypeptides and their molecular chaperones in the cytosol of mammalian cellsProtein targeting to the bacterial cytoplasmic membrane.Direct NMR observation of a substrate protein bound to the chaperonin GroEL.GroEL-mediated protein folding: making the impossible, possible.Conformational changes induced in Hoxb-8/Pbx-1 heterodimers in solution and upon interaction with specific DNAFeedback repression of ornithine decarboxylase synthesis mediated by antizyme.GroEL-mediated protein folding.Cotranslational protein folding.GroEL-induced topological dislocation of a substrate protein β-sheet core: a solution EPR spin-spin distance study.Role of the DnaK and HscA homologs of Hsp70 chaperones in protein folding in E.coli.Protein compactness measured by fluorescence resonance energy transfer. Human carbonic anhydrase ii is considerably expanded by the interaction of GroEL.Partitioning of rhodanese onto GroEL. Chaperonin binds a reversibly oxidized form derived from the native protein.
P2860

GroEL binds to and unfolds rhodanese posttranslationally.

Item
http://www.wikidata.org/entity/Q38360171
description
1996 nî lūn-bûn
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1996年の論文
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1996年学术文章
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1996年学术文章
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1996年学术文章
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1996年学术文章
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1996年学术文章
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1996年學術文章
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1996年學術文章
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1996年學術文章
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name
GroEL binds to and unfolds rhodanese posttranslationally.
@en
type
label
GroEL binds to and unfolds rhodanese posttranslationally.
@en
prefLabel
GroEL binds to and unfolds rhodanese posttranslationally.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P356
P1433
P1476
GroEL binds to and unfolds rhodanese posttranslationally.
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698