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262 related items for PubMed ID: 22727666
1. Dynamic tyrosine phosphorylation modulates cycling of the HSP90-P50(CDC37)-AHA1 chaperone machine. Xu W, Mollapour M, Prodromou C, Wang S, Scroggins BT, Palchick Z, Beebe K, Siderius M, Lee MJ, Couvillon A, Trepel JB, Miyata Y, Matts R, Neckers L. Mol Cell; 2012 Aug 10; 47(3):434-43. PubMed ID: 22727666 [Abstract] [Full Text] [Related]
2. Phosphorylation induced cochaperone unfolding promotes kinase recruitment and client class-specific Hsp90 phosphorylation. Bachman AB, Keramisanou D, Xu W, Beebe K, Moses MA, Vasantha Kumar MV, Gray G, Noor RE, van der Vaart A, Neckers L, Gelis I. Nat Commun; 2018 Jan 17; 9(1):265. PubMed ID: 29343704 [Abstract] [Full Text] [Related]
3. Specific regulation of noncanonical p38alpha activation by Hsp90-Cdc37 chaperone complex in cardiomyocyte. Ota A, Zhang J, Ping P, Han J, Wang Y. Circ Res; 2010 Apr 30; 106(8):1404-12. PubMed ID: 20299663 [Abstract] [Full Text] [Related]
4. Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90) motility by interaction with N-terminal and middle domain binding sites. Eckl JM, Rutz DA, Haslbeck V, Zierer BK, Reinstein J, Richter K. J Biol Chem; 2013 May 31; 288(22):16032-42. PubMed ID: 23569206 [Abstract] [Full Text] [Related]
5. Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37. Siligardi G, Panaretou B, Meyer P, Singh S, Woolfson DN, Piper PW, Pearl LH, Prodromou C. J Biol Chem; 2002 Jun 07; 277(23):20151-9. PubMed ID: 11916974 [Abstract] [Full Text] [Related]
12. Cdc37 as a Co-chaperone to Hsp90. Prince TL, Lang BJ, Okusha Y, Eguchi T, Calderwood SK. Subcell Biochem; 2023 Jun 07; 101():141-158. PubMed ID: 36520306 [Abstract] [Full Text] [Related]
15. Restricting direct interaction of CDC37 with HSP90 does not compromise chaperoning of client proteins. Smith JR, de Billy E, Hobbs S, Powers M, Prodromou C, Pearl L, Clarke PA, Workman P. Oncogene; 2015 Jan 02; 34(1):15-26. PubMed ID: 24292678 [Abstract] [Full Text] [Related]
16. Functional Role and Hierarchy of the Intermolecular Interactions in Binding of Protein Kinase Clients to the Hsp90-Cdc37 Chaperone: Structure-Based Network Modeling of Allosteric Regulation. Stetz G, Verkhivker GM. J Chem Inf Model; 2018 Feb 26; 58(2):405-421. PubMed ID: 29432007 [Abstract] [Full Text] [Related]
17. Integration of the accelerator Aha1 in the Hsp90 co-chaperone cycle. Li J, Richter K, Reinstein J, Buchner J. Nat Struct Mol Biol; 2013 Mar 26; 20(3):326-31. PubMed ID: 23396352 [Abstract] [Full Text] [Related]