The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
Asymmetric Activation of the Hsp90 Dimer by Its Cochaperone Aha1
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Citations
Cites
Global analysis of protein expression in yeast
Ghaemmaghami, S., Huh, W.-K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., & Weissman, J. S. (2003) · Nature · doi:10.1038/nature02046 · Cited by 3,750
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 1×
“Prominent examples are the Hsp40/DnaJ proteins (Bukau et al., 2006; Fan et al., 2003).”
Diverse Cellular Functions of the Hsp90 Molecular Chaperone Uncovered Using Systems Approaches
McClellan, A. J., Xia, Y., Deutschbauer, A. M., Davis, R. W., Gerstein, M., & Frydman, J. (2007) · Cell · doi:10.1016/j.cell.2007.07.036 · Cited by 474
The Hsp90‐binding peptidylprolyl isomerase FKBP52 potentiates glucocorticoid signaling in vivo
Riggs, D. L., Roberts, P. J., Chirillo, S. C., Cheung‐Flynn, J., Prapapanich, V., Ratajczak, T., Gaber, R., Picard, D., & Smith, D. F. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg108 · Cited by 353 · cited 2×
“In eukaryotes, accessory factors (so-called cochaperones) have been identified, which regulate the ATP turnover, induce structural changes in Hsp90, or are involved in the substrate activation process (Forafonov et al., 2008; Johnson et al., 1994, 1996; Pirkl and Buchner, 2001; Riggs et al., 2003; Siligardi et al., 20…”
BackgroundTwo chaperone sites in Hsp90 differing in substrate specificity and ATP dependence
Scheibel, T., Weikl, T., & Buchner, J. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.4.1495 · Cited by 243
Co-chaperone regulation of conformational switching in the Hsp90 ATPase cycle
Siligardi, G., Hu, B., Panaretou, B., Piper, P. W., Pearl, L. H., & Prodromou, C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410562200 · Cited by 207 · cited 2×
“In eukaryotes, accessory factors (so-called cochaperones) have been identified, which regulate the ATP turnover, induce structural changes in Hsp90, or are involved in the substrate activation process (Forafonov et al., 2008; Johnson et al., 1994, 1996; Pirkl and Buchner, 2001; Riggs et al., 2003; Siligardi et al., 20…”
BackgroundThe 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 14×
“Our results on the presence of an activating and inhibiting chaperone suggest that ternary complexes are possible and that, in these, the activator Aha1 and either Hop/Sti1 or p23/Sba1 could act on Hsp90 at the same time.”
BackgroundInfluentialPirkl, F., & Buchner, J. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4595 · Cited by 179 · cited 2×
“In eukaryotes, accessory factors (so-called cochaperones) have been identified, which regulate the ATP turnover, induce structural changes in Hsp90, or are involved in the substrate activation process (Forafonov et al., 2008; Johnson et al., 1994, 1996; Pirkl and Buchner, 2001; Riggs et al., 2003; Siligardi et al., 20…”
BackgroundRichter, K., Walter, S., & Buchner, J. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.07.064 · Cited by 159 · cited 5×
“For Hsp90-p23/Sba1 and Hsp90-Hop/Sti1 complexes, a competitive binding mode has been suggested (Richter et al., 2004).”
BackgroundMethodInfluentialSelf-citationThe Middle Domain of Hsp90 Acts as a Discriminator between Different Types of Client Proteins
Hawle, P., Siepmann, M., Harst, A., Siderius, M., Reusch, H. P., & Obermann, W. M. J. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.02188-05 · Cited by 127 · cited 2×
“344 Molecular Cell 37, 344–354, February 12, 2010 ª2010 Elsevier In Hsp90 is a dimeric protein with an N-terminal nucleotidebinding pocket, a middle domain that is known to act as a discriminator between Hsp90 substrates (Hawle et al., 2006), and a C-terminal dimerization domain.”
Background
Cited by
HSP90 at the hub of protein homeostasis: emerging mechanistic insights
Taipale, M., Jarosz, D. F., & Lindquist, S. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2918 · Cited by 1,818
Schopf, F. H., Biebl, M. M., & Buchner, J. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.20 · Cited by 1,540
The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones
Li, J., Soroka, J., & Buchner, J. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.09.003 · Cited by 498
Hsp90-Tau complex reveals molecular basis for specificity in chaperone action
Karagöz, G. E., Duarte, A. M. S., Akoury, E., Ippel, H., Biernat, J., Morán Luengo, T., Radli, M., Didenko, T., Nordhues, B. A., Veprintsev, D. B., et al. (2014) · Cell · doi:10.1016/j.cell.2014.01.037 · Cited by 318
“While there is no evidence to support the first possibility, conformational asymmetry is characteristic for several previously described Hsp90 complexes (i.e., Hsp90-p23, Hsp90-Cdk4-Cdc37, and Hsp90Aha1) (Karagöz et al., 2011; Retzlaff et al., 2010; Vaughan et al., 2006).”
Conformational dynamics of the molecular chaperone Hsp90
Krukenberg, K. A., Street, T. O., Lavery, L. A., & Agard, D. A. (2011) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583510000314 · Cited by 308
Metadata
- Authors
- Retzlaff, M., Hagn, F., Mitschke, L., Hessling, M., Gugel, F., Kessler, H., Richter, K., & Buchner, J.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2010-02
- Volume
- 37
- Issue
- 3
- Pages
- 344-354
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2095099777
- Cited by
- 244
- References
- 12
- FWCI
- 7.56
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Retzlaff, M., Hagn, F., Mitschke, L., Hessling, M., Gugel, F., Kessler, H., Richter, K., & Buchner, J. (2010). Asymmetric Activation of the Hsp90 Dimer by Its Cochaperone Aha1. Molecular Cell. https://doi.org/10.1016/j.molcel.2010.01.006
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