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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 conserved arginine 380 of Hsp90 is not a catalytic residue, but stabilizes the closed conformation required for ATP hydrolysis.

Cunningham CN, Southworth DR, Krukenberg KA, Agard DA.

Protein Sci. 2012 Aug;21(8):1162-71. doi: 10.1002/pro.2103.


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.


Intrinsic inhibition of the Hsp90 ATPase activity.

Richter K, Moser S, Hagn F, Friedrich R, Hainzl O, Heller M, Schlee S, Kessler H, Reinstein J, Buchner J.

J Biol Chem. 2006 Apr 21;281(16):11301-11.


Mitochondrial Hsp90 is a ligand-activated molecular chaperone coupling ATP binding to dimer closure through a coiled-coil intermediate.

Sung N, Lee J, Kim JH, Chang C, Joachimiak A, Lee S, Tsai FT.

Proc Natl Acad Sci U S A. 2016 Mar 15;113(11):2952-7. doi: 10.1073/pnas.1516167113.


Intra- and intermonomer interactions are required to synergistically facilitate ATP hydrolysis in Hsp90.

Cunningham CN, Krukenberg KA, Agard DA.

J Biol Chem. 2008 Jul 25;283(30):21170-8. doi: 10.1074/jbc.M800046200.


Cross-monomer substrate contacts reposition the Hsp90 N-terminal domain and prime the chaperone activity.

Street TO, Lavery LA, Verba KA, Lee CT, Mayer MP, Agard DA.

J Mol Biol. 2012 Jan 6;415(1):3-15. doi: 10.1016/j.jmb.2011.10.038.


The ATPase cycle of the mitochondrial Hsp90 analog Trap1.

Leskovar A, Wegele H, Werbeck ND, Buchner J, Reinstein J.

J Biol Chem. 2008 Apr 25;283(17):11677-88. doi: 10.1074/jbc.M709516200.


Conserved conformational changes in the ATPase cycle of human Hsp90.

Richter K, Soroka J, Skalniak L, Leskovar A, Hessling M, Reinstein J, Buchner J.

J Biol Chem. 2008 Jun 27;283(26):17757-65. doi: 10.1074/jbc.M800540200.


Stimulation of the weak ATPase activity of human hsp90 by a client protein.

McLaughlin SH, Smith HW, Jackson SE.

J Mol Biol. 2002 Jan 25;315(4):787-98.


Dissection of the contribution of individual domains to the ATPase mechanism of Hsp90.

Wegele H, Muschler P, Bunck M, Reinstein J, Buchner J.

J Biol Chem. 2003 Oct 10;278(41):39303-10.


In vivo function of Hsp90 is dependent on ATP binding and ATP hydrolysis.

Obermann WM, Sondermann H, Russo AA, Pavletich NP, Hartl FU.

J Cell Biol. 1998 Nov 16;143(4):901-10.


Coordinated ATP hydrolysis by the Hsp90 dimer.

Richter K, Muschler P, Hainzl O, Buchner J.

J Biol Chem. 2001 Sep 7;276(36):33689-96.


Independent ATPase activity of Hsp90 subunits creates a flexible assembly platform.

McLaughlin SH, Ventouras LA, Lobbezoo B, Jackson SE.

J Mol Biol. 2004 Nov 26;344(3):813-26.


Mechanistic Asymmetry in Hsp90 Dimers.

Flynn JM, Mishra P, Bolon DN.

J Mol Biol. 2015 Sep 11;427(18):2904-11. doi: 10.1016/j.jmb.2015.03.017. Review.


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 13;379(4):732-44. doi: 10.1016/j.jmb.2008.02.013.


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.


Conformations of the apo-, substrate-bound and phosphate-bound ATP-binding domain of the Cu(II) ATPase CopB illustrate coupling of domain movement to the catalytic cycle.

Jayakanthan S, Roberts SA, Weichsel A, Arg├╝ello JM, McEvoy MM.

Biosci Rep. 2012 Oct;32(5):443-53. doi: 10.1042/BSR20120048.


Structure insights into mechanisms of ATP hydrolysis and the activation of human heat-shock protein 90.

Li J, Sun L, Xu C, Yu F, Zhou H, Zhao Y, Zhang J, Cai J, Mao C, Tang L, Xu Y, He J.

Acta Biochim Biophys Sin (Shanghai). 2012 Apr;44(4):300-6. doi: 10.1093/abbs/gms001.

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