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Journal Abstract Search

412 related items for PubMed ID: 23396352

  • 1. 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; 20(3):326-31. PubMed ID: 23396352
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  • 3. Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle.
    Siligardi G, Hu B, Panaretou B, Piper PW, Pearl LH, Prodromou C.
    J Biol Chem; 2004 Dec 10; 279(50):51989-98. PubMed ID: 15466438
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  • 4. Asymmetric activation of the hsp90 dimer by its cochaperone aha1.
    Retzlaff M, Hagn F, Mitschke L, Hessling M, Gugel F, Kessler H, Richter K, Buchner J.
    Mol Cell; 2010 Feb 12; 37(3):344-54. PubMed ID: 20159554
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  • 6. Aha1 competes with Hop, p50 and p23 for binding to the molecular chaperone Hsp90 and contributes to kinase and hormone receptor activation.
    Harst A, Lin H, Obermann WM.
    Biochem J; 2005 May 01; 387(Pt 3):789-96. PubMed ID: 15584899
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  • 10. Threonine 22 phosphorylation attenuates Hsp90 interaction with cochaperones and affects its chaperone activity.
    Mollapour M, Tsutsumi S, Truman AW, Xu W, Vaughan CK, Beebe K, Konstantinova A, Vourganti S, Panaretou B, Piper PW, Trepel JB, Prodromou C, Pearl LH, Neckers L.
    Mol Cell; 2011 Mar 18; 41(6):672-81. PubMed ID: 21419342
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  • 12. Biochemical characterization and cooperation with co-chaperones of heat shock protein 90 from Schizosaccharomyces pombe.
    Ishida M, Tomomari T, Kanzaki T, Abe T, Oka T, Yohda M.
    J Biosci Bioeng; 2013 Oct 18; 116(4):444-8. PubMed ID: 23664927
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  • 16. Dissection of the ATP-induced conformational cycle of the molecular chaperone Hsp90.
    Hessling M, Richter K, Buchner J.
    Nat Struct Mol Biol; 2009 Mar 18; 16(3):287-93. PubMed ID: 19234467
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  • 17. 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
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  • 18. Dynamic Aha1 co-chaperone binding to human Hsp90.
    Oroz J, Blair LJ, Zweckstetter M.
    Protein Sci; 2019 Sep 31; 28(9):1545-1551. PubMed ID: 31299134
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  • 19. The conserved NxNNWHW motif in Aha-type co-chaperones modulates the kinetics of Hsp90 ATPase stimulation.
    Mercier R, Wolmarans A, Schubert J, Neuweiler H, Johnson JL, LaPointe P.
    Nat Commun; 2019 Mar 20; 10(1):1273. PubMed ID: 30894538
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