Pub. Date : 2018 Sep
PMID : 29941666
5 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Here, we examined the activity of human Hsp90alpha and Hsp90beta in a purified five-protein chaperone machinery that assembles glucocorticoid receptor (GR) Hsp90 heterocomplexes to generate high-affinity steroid-binding activity. | Steroids | heat shock protein 90 alpha family class A member 1 | Homo sapiens |
| 2 | Here, we examined the activity of human Hsp90alpha and Hsp90beta in a purified five-protein chaperone machinery that assembles glucocorticoid receptor (GR) Hsp90 heterocomplexes to generate high-affinity steroid-binding activity. | Steroids | heat shock protein 90 alpha family class A member 1 | Homo sapiens |
| 3 | We showed that the phosphomimetic mutant Hsp90alpha T5/7D has the same intrinsic chaperone activity as wild-type human Hsp90alpha in activation of GR steroid-binding activity by the five-protein machinery, supporting the conclusion that T5/7 phosphorylation does not affect Hsp90alpha chaperone activity. | Steroids | heat shock protein 90 alpha family class A member 1 | Homo sapiens |
| 4 | We showed that the phosphomimetic mutant Hsp90alpha T5/7D has the same intrinsic chaperone activity as wild-type human Hsp90alpha in activation of GR steroid-binding activity by the five-protein machinery, supporting the conclusion that T5/7 phosphorylation does not affect Hsp90alpha chaperone activity. | Steroids | heat shock protein 90 alpha family class A member 1 | Homo sapiens |
| 5 | We showed that the phosphomimetic mutant Hsp90alpha T5/7D has the same intrinsic chaperone activity as wild-type human Hsp90alpha in activation of GR steroid-binding activity by the five-protein machinery, supporting the conclusion that T5/7 phosphorylation does not affect Hsp90alpha chaperone activity. | Steroids | heat shock protein 90 alpha family class A member 1 | Homo sapiens |