The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Hsp90 is regulated by a switch point in the C‐terminal domain
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Citations
Cites
HSP90 and the chaperoning of cancer
Whitesell, L., & Lindquist, S. L. (2005) · Nature Reviews Cancer · doi:10.1038/nrc1716 · Cited by 2,502
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 2×
“The mechanism of ATP hydrolysis is conserved for various Hsp90 family members (Ali et al, 2006; Dollins et al, 2007; Frey et al, 2007; Graf et al, 2009; Hessling et al, 2009; Leskovar et al, 2008; Richter et al, 2008; Shiau et al, 2006).”
BackgroundMutational Analysis of Hsp90 Function: Interactions with a Steroid Receptor and a Protein Kinase
Nathan, D. F., & Lindquist, S. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.7.3917 · Cited by 423 · cited 3×
“A S. cerevisiae strain, carrying an HSC82/ HSP82 double knockout mutation (Nathan & Lindquist, 1995), was transfected with HSP90 variants, cloned in the high-copy vector pRS423 (2 m) and co-transfected with V-SRC present on a vector carrying a URA3 marker.”
BackgroundMethodInfluentialAn Acetylation Site in the Middle Domain of Hsp90 Regulates Chaperone Function
Scroggins, B. T., Robzyk, K., Wang, D., Marcu, M. G., Tsutsumi, S., Beebe, K., Cotter, R. J., Felts, S., Toft, D., Karnitz, L., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2006.12.008 · Cited by 413
Richter, K., Walter, S., & Buchner, J. (2004) · Journal of Molecular Biology · doi:10.1016/j.jmb.2004.07.064 · Cited by 159 · cited 2×
“Keywords: ATPase; chaperone; conformation; FRET; regulation EMBO reports (2009) 10, 1147–1153. doi:10.1038/embor.2009.153”
BackgroundInfluentialThe 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×
“S-nitrosylation of a residue located in the carboxy-terminal domain has been shown to affect Hsp90 activity in vivo.”
Backgroundp23/Sba1p protects against Hsp90 inhibitors independently of its intrinsic chaperone activity
Forafonov, F., Toogun, O. A., Grad, I., Suslova, E., Freeman, B. C., & Picard, D. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.02246-07 · Cited by 84 · cited 1×
“…is modulated by co-chaperones such as the stimulator Aha1 (Meyer et al, 2004; Panaretou et al, 2002) or the inhibitors Hop/Sti1 (Prodromou et al, 1999; Richter et al, 2003) and p23/Sba1 (Forafonov et al, 2008; Johnson et al, 1994; Richter et al, 2004; Prodromou et al, 2000; Young & Hartl, 2000).”
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
Molecular mechanisms underlying the activation of eNOS
Fleming, I. (2010) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-009-0767-7 · Cited by 437
Post-translational modifications of Hsp90 and their contributions to chaperone regulation
Mollapour, M., & Neckers, L. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.07.018 · Cited by 288
Metadata
- Authors
- Retzlaff, M., Stahl, M., Eberl, H. C., Lagleder, S., Beck, J., Kessler, H., & Buchner, J.
- Venue
- EMBO reports
- Published
- 2009-08-21
- Volume
- 10
- Issue
- 10
- Pages
- 1147-1153
- ISSN
- 1469-221X (ISSN-L)
- 1469-3178
- OpenAlex
- W2156992532
- Cited by
- 171
- References
- 7
- FWCI
- 4.08
- Type
- journal article
- Language
- en
- Open access
- green
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- The paper
- Retzlaff, M., Stahl, M., Eberl, H. C., Lagleder, S., Beck, J., Kessler, H., & Buchner, J. (2009). Hsp90 is regulated by a switch point in the C‐terminal domain. EMBO reports. https://doi.org/10.1038/embor.2009.153
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
