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PMID:11470816
| Citation |
Young, JC, Moarefi, I and Hartl, FU (2001) Hsp90: a specialized but essential protein-folding tool. J. Cell Biol. 154:267-73 |
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| Abstract |
Hsp90 is unique among molecular chaperones. The majority of its known substrates are signal transduction proteins, and recent work indicates that it uses a novel protein-folding strategy. |
| Links | |
| Keywords |
Adenosine Triphosphatases/metabolism; Animals; Cytosol/metabolism; Evolution, Molecular; HSP90 Heat-Shock Proteins/metabolism; Humans; Models, Molecular; Protein Folding; Protein Structure, Tertiary/physiology; Proteins/metabolism; Signal Transduction/physiology |
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Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
|
enables |
GO:0005524: ATP binding |
ECO:0000304: author statement supported by traceable reference used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0000166: nucleotide binding |
ECO:0000304: author statement supported by traceable reference used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
enables |
GO:0042803: protein homodimerization activity |
ECO:0000304: author statement supported by traceable reference used in manual assertion |
F |
Seeded From UniProt |
complete | |||
|
involved_in |
GO:0007165: signal transduction |
ECO:0000303: author statement without traceable support used in manual assertion |
P |
Seeded From UniProt |
complete | |||
See also
References
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