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Details on Person Structure-function analysis of the heat shock factor-binding protein reveals a protein composed solely of a highly conserved and dynamic coiled-coil trimerization domain
| Class:Id | LiteratureReference:3371415 |
|---|---|
| _displayName | Structure-function analysis of the heat shock factor-binding protein reveals a protein composed solely of a highly conserved and dynamic coiled-coil trimerization domain |
| _timestamp | 2013-05-13 14:03:55 |
| author | [Person:3371533] Tai, Li-Jung [Person:3371538] McFall, Sally M [Person:3371473] Huang, Kai [Person:190171] Demeler, B [Person:3371499] Fox, Sue G [Person:3371442] Brubaker, Kurt [Person:3371475] Radhakrishnan, Ishwar [Person:3371418] Morimoto, Richard I |
| created | [InstanceEdit:3371552] Shamovsky, V, 2013-05-13 |
| journal | J. Biol. Chem. |
| pages | 735-45 |
| pubMedIdentifier | 11679589 |
| title | Structure-function analysis of the heat shock factor-binding protein reveals a protein composed solely of a highly conserved and dynamic coiled-coil trimerization domain |
| volume | 277 |
| year | 2002 |
| (literatureReference) | [Complex:3371426] HSBP1 hexamer [nucleoplasm] [Homo sapiens] [Complex:3371551] HSBP1 trimer [nucleoplasm] [Homo sapiens] |
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No pathways have been reviewed or authored by Structure-function analysis of the heat shock factor-binding protein reveals a protein composed solely of a highly conserved and dynamic coiled-coil trimerization domain (3371415)
