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Species-Dependent Ensembles of Conserved Conformational States Define the Hsp90 Chaperone ATPase Cycle
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Crystal structure of an Hsp90–nucleotide–p23/Sba1 closed chaperone complex
Ali, M. M. U., Roe, S. M., Vaughan, C. K., Meyer, P., Panaretou, B., Piper, P. W., Prodromou, C., & Pearl, L. H. (2006) · Nature · doi:10.1038/nature04716 · Cited by 962 · cited 4×
“(C) thefinal HtpG:AMPPNP 3D map is shown, and in(D) the yeast Hsp90 structure ( Ali et al., 2006 ) was fit into the EM map.”
BackgroundMethodInfluentialZhao, R., Davey, M., Hsu, Y.-C., Kaplanek, P., Tong, A., Parsons, A. B., Krogan, N., Cagney, G., Mai, D., Greenblatt, J., et al. (2005) · Cell · doi:10.1016/j.cell.2004.12.024 · Cited by 819
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Picard, D., Khursheed, B., Garabedian, M. J., Fortin, M. G., Lindquist, S., & Yamamoto, K. R. (1990) · Nature · doi:10.1038/348166a0 · Cited by 787 · cited 2×
“Although client proteins have not been definitively identified for HtpG, in higher organisms Hsp90 activity is essential for the activation of many proteins including steroid hormone nuclear receptors (Picard et al., 1990; Pratt et al., 2004), protein kinases (Richter and Buchner, 2001; Sato et al.”
BackgroundMeyer, P., Prodromou, C., Hu, B., Vaughan, C., Roe, S. M., Panaretou, B., Piper, P. W., & Pearl, L. H. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00065-0 · Cited by 491
The Co-chaperone p23 Arrests the Hsp90 ATPase Cycle to Trap Client Proteins
McLaughlin, S. H., Sobott, F., Yao, Z.-P., Zhang, W., Nielsen, P. R., Grossmann, J. G., Laue, E. D., Robinson, C. V., & Jackson, S. E. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.11.085 · Cited by 196 · cited 1×
“This interaction is known to significantly slow the hydrolysis rate and stabilize client-bound Hsp90 complexes (McLaughlin et al., 2006).”
BackgroundKrukenberg, K. A., Förster, F., Rice, L. M., Sali, A., & Agard, D. A. (2008) · Structure · doi:10.1016/j.str.2008.01.021 · Cited by 160 · cited 5×
“In the absence of nucleotide HtpG, Hsc82 and Hsp90a adopt a heterogeneous ensemble of open and extended conformations with an overall shape that is consistent with previous studies (Krukenberg et al., 2008; Bron et al., 2008).”
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Cited by
HSP90 at the hub of protein homeostasis: emerging mechanistic insights
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The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones
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Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase
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Conformational dynamics of the molecular chaperone Hsp90
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Metadata
- Authors
- Southworth, D. R., & Agard, D. A.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2008-12
- Volume
- 32
- Issue
- 5
- Pages
- 631-640
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2085898992
- Cited by
- 224
- References
- 7
- FWCI
- 6.58
- Type
- journal article
- Language
- en
- Open access
- bronze
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 1689 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Funders
- American Cancer Society
- University of California (bio03-10401)
- Howard Hughes Medical Institute
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