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Items: 15


Protein conformational flexibility modulates kinetics and thermodynamics of drug binding.

Amaral M, Kokh DB, Bomke J, Wegener A, Buchstaller HP, Eggenweiler HM, Matias P, Sirrenberg C, Wade RC, Frech M.

Nat Commun. 2017 Dec 22;8(1):2276. doi: 10.1038/s41467-017-02258-w.


The Mechanism of Hsp90 ATPase Stimulation by Aha1.

Wolmarans A, Lee B, Spyracopoulos L, LaPointe P.

Sci Rep. 2016 Sep 12;6:33179. doi: 10.1038/srep33179.


Cooperation of local motions in the Hsp90 molecular chaperone ATPase mechanism.

Schulze A, Beliu G, Helmerich DA, Schubert J, Pearl LH, Prodromou C, Neuweiler H.

Nat Chem Biol. 2016 Aug;12(8):628-35. doi: 10.1038/nchembio.2111. Epub 2016 Jun 20.


A novel N-terminal extension in mitochondrial TRAP1 serves as a thermal regulator of chaperone activity.

Partridge JR, Lavery LA, Elnatan D, Naber N, Cooke R, Agard DA.

Elife. 2014 Dec 22;3. doi: 10.7554/eLife.03487.


Both the charged linker region and ATPase domain of Hsp90 are essential for Rad51-dependent DNA repair.

Suhane T, Laskar S, Advani S, Roy N, Varunan S, Bhattacharyya D, Bhattacharyya S, Bhattacharyya MK.

Eukaryot Cell. 2015 Jan;14(1):64-77. doi: 10.1128/EC.00159-14. Epub 2014 Nov 7.


Structural asymmetry in the closed state of mitochondrial Hsp90 (TRAP1) supports a two-step ATP hydrolysis mechanism.

Lavery LA, Partridge JR, Ramelot TA, Elnatan D, Kennedy MA, Agard DA.

Mol Cell. 2014 Jan 23;53(2):330-43. doi: 10.1016/j.molcel.2013.12.023.


The regulatory mechanism of a client kinase controlling its own release from Hsp90 chaperone machinery through phosphorylation.

Lu XA, Wang X, Zhuo W, Jia L, Jiang Y, Fu Y, Luo Y.

Biochem J. 2014 Jan 1;457(1):171-83. doi: 10.1042/BJ20130963.


Heat shock protein 90's mechanochemical cycle is dominated by thermal fluctuations.

Ratzke C, Berkemeier F, Hugel T.

Proc Natl Acad Sci U S A. 2012 Jan 3;109(1):161-6. doi: 10.1073/pnas.1107930108. Epub 2011 Dec 19.


Downregulation of the Hsp90 system causes defects in muscle cells of Caenorhabditis elegans.

Gaiser AM, Kaiser CJ, Haslbeck V, Richter K.

PLoS One. 2011;6(9):e25485. doi: 10.1371/journal.pone.0025485. Epub 2011 Sep 28.


Enforced N-domain proximity stimulates Hsp90 ATPase activity and is compatible with function in vivo.

Pullen L, Bolon DN.

J Biol Chem. 2011 Apr 1;286(13):11091-8. doi: 10.1074/jbc.M111.223131. Epub 2011 Jan 28.


Dynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle.

Ratzke C, Mickler M, Hellenkamp B, Buchner J, Hugel T.

Proc Natl Acad Sci U S A. 2010 Sep 14;107(37):16101-6. doi: 10.1073/pnas.1000916107. Epub 2010 Aug 24.


The charged linker region is an important regulator of Hsp90 function.

Hainzl O, Lapina MC, Buchner J, Richter K.

J Biol Chem. 2009 Aug 21;284(34):22559-67. doi: 10.1074/jbc.M109.031658. Epub 2009 Jun 24.


Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine.

Graf C, Stankiewicz M, Kramer G, Mayer MP.

EMBO J. 2009 Mar 4;28(5):602-13. doi: 10.1038/emboj.2008.306. Epub 2009 Jan 22.


Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex.

Ali MM, Roe SM, Vaughan CK, Meyer P, Panaretou B, Piper PW, Prodromou C, Pearl LH.

Nature. 2006 Apr 20;440(7087):1013-7.

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