593 related articles for article (PubMed ID: 15223329)
1. Biochemical and structural studies of the interaction of Cdc37 with Hsp90.
Zhang W; Hirshberg M; McLaughlin SH; Lazar GA; Grossmann JG; Nielsen PR; Sobott F; Robinson CV; Jackson SE; Laue ED
J Mol Biol; 2004 Jul; 340(4):891-907. PubMed ID: 15223329
[TBL] [Abstract][Full Text] [Related]
2. Domain-mediated dimerization of the Hsp90 cochaperones Harc and Cdc37.
Roiniotis J; Masendycz P; Ho S; Scholz GM
Biochemistry; 2005 May; 44(17):6662-9. PubMed ID: 15850399
[TBL] [Abstract][Full Text] [Related]
3. Cdc37 maintains cellular viability in Schizosaccharomyces pombe independently of interactions with heat-shock protein 90.
Turnbull EL; Martin IV; Fantes PA
FEBS J; 2005 Aug; 272(16):4129-40. PubMed ID: 16098195
[TBL] [Abstract][Full Text] [Related]
4. A client-binding site of Cdc37.
Terasawa K; Minami Y
FEBS J; 2005 Sep; 272(18):4684-90. PubMed ID: 16156789
[TBL] [Abstract][Full Text] [Related]
5. Functional dissection of cdc37: characterization of domain structure and amino acid residues critical for protein kinase binding.
Shao J; Irwin A; Hartson SD; Matts RL
Biochemistry; 2003 Nov; 42(43):12577-88. PubMed ID: 14580204
[TBL] [Abstract][Full Text] [Related]
6. Structural studies on the co-chaperone Hop and its complexes with Hsp90.
Onuoha SC; Coulstock ET; Grossmann JG; Jackson SE
J Mol Biol; 2008 Jun; 379(4):732-44. PubMed ID: 18485364
[TBL] [Abstract][Full Text] [Related]
7. The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically.
Abbas-Terki T; Briand PA; Donzé O; Picard D
Biol Chem; 2002 Sep; 383(9):1335-42. PubMed ID: 12437126
[TBL] [Abstract][Full Text] [Related]
8. The Co-chaperone Sba1 connects the ATPase reaction of Hsp90 to the progression of the chaperone cycle.
Richter K; Walter S; Buchner J
J Mol Biol; 2004 Oct; 342(5):1403-13. PubMed ID: 15364569
[TBL] [Abstract][Full Text] [Related]
9. Exposure of protein kinase motifs that trigger binding of Hsp90 and Cdc37.
Prince T; Matts RL
Biochem Biophys Res Commun; 2005 Dec; 338(3):1447-54. PubMed ID: 16269130
[TBL] [Abstract][Full Text] [Related]
10. Functional specificity of co-chaperone interactions with Hsp90 client proteins.
Riggs DL; Cox MB; Cheung-Flynn J; Prapapanich V; Carrigan PE; Smith DF
Crit Rev Biochem Mol Biol; 2004; 39(5-6):279-95. PubMed ID: 15763706
[TBL] [Abstract][Full Text] [Related]
11. Stability of the Peutz-Jeghers syndrome kinase LKB1 requires its binding to the molecular chaperones Hsp90/Cdc37.
Nony P; Gaude H; Rossel M; Fournier L; Rouault JP; Billaud M
Oncogene; 2003 Dec; 22(57):9165-75. PubMed ID: 14668798
[TBL] [Abstract][Full Text] [Related]
12. 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; 288(22):16032-42. PubMed ID: 23569206
[TBL] [Abstract][Full Text] [Related]
13. The co-chaperone p23 arrests the Hsp90 ATPase cycle to trap client proteins.
McLaughlin SH; Sobott F; Yao ZP; Zhang W; Nielsen PR; Grossmann JG; Laue ED; Robinson CV; Jackson SE
J Mol Biol; 2006 Feb; 356(3):746-58. PubMed ID: 16403413
[TBL] [Abstract][Full Text] [Related]
14. Cdk2: a genuine protein kinase client of Hsp90 and Cdc37.
Prince T; Sun L; Matts RL
Biochemistry; 2005 Nov; 44(46):15287-95. PubMed ID: 16285732
[TBL] [Abstract][Full Text] [Related]
15. Independent ATPase activity of Hsp90 subunits creates a flexible assembly platform.
McLaughlin SH; Ventouras LA; Lobbezoo B; Jackson SE
J Mol Biol; 2004 Nov; 344(3):813-26. PubMed ID: 15533447
[TBL] [Abstract][Full Text] [Related]
16. Constantly updated knowledge of Hsp90.
Terasawa K; Minami M; Minami Y
J Biochem; 2005 Apr; 137(4):443-7. PubMed ID: 15858167
[TBL] [Abstract][Full Text] [Related]
17. 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; 277(23):20151-9. PubMed ID: 11916974
[TBL] [Abstract][Full Text] [Related]
18. High affinity binding of Hsp90 is triggered by multiple discrete segments of its kinase clients.
Scroggins BT; Prince T; Shao J; Uma S; Huang W; Guo Y; Yun BG; Hedman K; Matts RL; Hartson SD
Biochemistry; 2003 Nov; 42(43):12550-61. PubMed ID: 14580201
[TBL] [Abstract][Full Text] [Related]
19. Blocking the chaperone kinome pathway: mechanistic insights into a novel dual inhibition approach for supra-additive suppression of malignant tumors.
Grover A; Shandilya A; Agrawal V; Pratik P; Bhasme D; Bisaria VS; Sundar D
Biochem Biophys Res Commun; 2011 Jan; 404(1):498-503. PubMed ID: 21144839
[TBL] [Abstract][Full Text] [Related]
20. Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37.
Shao J; Prince T; Hartson SD; Matts RL
J Biol Chem; 2003 Oct; 278(40):38117-20. PubMed ID: 12930845
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
