308 related articles for article (PubMed ID: 27251758)
1. The co-chaperone Cdc37 regulates the rabies virus phosphoprotein stability by targeting to Hsp90AA1 machinery.
Xu Y; Liu F; Liu J; Wang D; Yan Y; Ji S; Zan J; Zhou J
Sci Rep; 2016 Jun; 6():27123. PubMed ID: 27251758
[TBL] [Abstract][Full Text] [Related]
2. 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; 58(2):405-421. PubMed ID: 29432007
[TBL] [Abstract][Full Text] [Related]
3. Atomistic simulations and network-based modeling of the Hsp90-Cdc37 chaperone binding with Cdk4 client protein: A mechanism of chaperoning kinase clients by exploiting weak spots of intrinsically dynamic kinase domains.
Czemeres J; Buse K; Verkhivker GM
PLoS One; 2017; 12(12):e0190267. PubMed ID: 29267381
[TBL] [Abstract][Full Text] [Related]
4. Targeting the Hsp90-Cdc37-client protein interaction to disrupt Hsp90 chaperone machinery.
Li T; Jiang HL; Tong YG; Lu JJ
J Hematol Oncol; 2018 Apr; 11(1):59. PubMed ID: 29699578
[TBL] [Abstract][Full Text] [Related]
5. 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; 106(8):1404-12. PubMed ID: 20299663
[TBL] [Abstract][Full Text] [Related]
6. 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]
7. p17-Modulated Hsp90/Cdc37 Complex Governs Oncolytic Avian Reovirus Replication by Chaperoning p17, Which Promotes Viral Protein Synthesis and Accumulation of Viral Proteins σC and σA in Viral Factories.
Huang WR; Li JY; Wu YY; Liao TL; Nielsen BL; Liu HJ
J Virol; 2022 Mar; 96(6):e0007422. PubMed ID: 35107368
[TBL] [Abstract][Full Text] [Related]
8. 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]
9. Hsp90/Cdc37 chaperone/co-chaperone complex, a novel junction anticancer target elucidated by the mode of action of herbal drug Withaferin A.
Grover A; Shandilya A; Agrawal V; Pratik P; Bhasme D; Bisaria VS; Sundar D
BMC Bioinformatics; 2011 Feb; 12 Suppl 1(Suppl 1):S30. PubMed ID: 21342561
[TBL] [Abstract][Full Text] [Related]
10. Hsp90-dependent activation of protein kinases is regulated by chaperone-targeted dephosphorylation of Cdc37.
Vaughan CK; Mollapour M; Smith JR; Truman A; Hu B; Good VM; Panaretou B; Neckers L; Clarke PA; Workman P; Piper PW; Prodromou C; Pearl LH
Mol Cell; 2008 Sep; 31(6):886-95. PubMed ID: 18922470
[TBL] [Abstract][Full Text] [Related]
11. Molecular chaperone complexes with antagonizing activities regulate stability and activity of the tumor suppressor LKB1.
Gaude H; Aznar N; Delay A; Bres A; Buchet-Poyau K; Caillat C; Vigouroux A; Rogon C; Woods A; Vanacker JM; Höhfeld J; Perret C; Meyer P; Billaud M; Forcet C
Oncogene; 2012 Mar; 31(12):1582-91. PubMed ID: 21860411
[TBL] [Abstract][Full Text] [Related]
12. 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; 47(3):434-43. PubMed ID: 22727666
[TBL] [Abstract][Full Text] [Related]
13. Exploring Mechanisms of Communication Switching in the Hsp90-Cdc37 Regulatory Complexes with Client Kinases through Allosteric Coupling of Phosphorylation Sites: Perturbation-Based Modeling and Hierarchical Community Analysis of Residue Interaction Networks.
Stetz G; Astl L; Verkhivker GM
J Chem Theory Comput; 2020 Jul; 16(7):4706-4725. PubMed ID: 32492340
[TBL] [Abstract][Full Text] [Related]
14. Cdc37 is a molecular chaperone with specific functions in signal transduction.
Kimura Y; Rutherford SL; Miyata Y; Yahara I; Freeman BC; Yue L; Morimoto RI; Lindquist S
Genes Dev; 1997 Jul; 11(14):1775-85. PubMed ID: 9242486
[TBL] [Abstract][Full Text] [Related]
15. Withaferin A Regulates LRRK2 Levels by Interfering with the Hsp90- Cdc37 Chaperone Complex.
Narayan M; Zhang J; Braswell K; Gibson C; Zitnyar A; Lee DC; Varghese-Gupta S; Jinwal UK
Curr Aging Sci; 2015; 8(3):259-65. PubMed ID: 25989799
[TBL] [Abstract][Full Text] [Related]
16. Interaction of rabies virus P-protein with STAT proteins is critical to lethal rabies disease.
Wiltzer L; Okada K; Yamaoka S; Larrous F; Kuusisto HV; Sugiyama M; Blondel D; Bourhy H; Jans DA; Ito N; Moseley GW
J Infect Dis; 2014 Jun; 209(11):1744-53. PubMed ID: 24367042
[TBL] [Abstract][Full Text] [Related]
17. Definition of protein kinase sequence motifs that trigger high affinity binding of Hsp90 and Cdc37.
Prince T; Matts RL
J Biol Chem; 2004 Sep; 279(38):39975-81. PubMed ID: 15258137
[TBL] [Abstract][Full Text] [Related]
18. The Activity and Stability of p56Lck and TCR Signaling Do Not Depend on the Co-Chaperone Cdc37.
Kowallik S; Kritikos A; Kästle M; Thurm C; Schraven B; Simeoni L
Int J Mol Sci; 2020 Dec; 22(1):. PubMed ID: 33374422
[TBL] [Abstract][Full Text] [Related]
19. 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; 34(1):15-26. PubMed ID: 24292678
[TBL] [Abstract][Full Text] [Related]
20. Cdc37 as a Co-chaperone to Hsp90.
Prince TL; Lang BJ; Okusha Y; Eguchi T; Calderwood SK
Subcell Biochem; 2023; 101():141-158. PubMed ID: 36520306
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
