The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Hsp90 interaction with clients
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Citations
Cites
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
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×
“Instead of pointing in opposite directions, as in the open conformation, both N-terminal domains must connect to each other and provide a second, transient dimerisation interface [21].”
InfluentialQuantitative Analysis of Hsp90-Client Interactions Reveals Principles of Substrate Recognition
Taipale, M., Krykbaeva, I., Koeva, M., Kayatekin, C., Westover, K. D., Karras, G. I., & Lindquist, S. (2012) · Cell · doi:10.1016/j.cell.2012.06.047 · Cited by 879
Structural Polymorphism of 441-Residue Tau at Single Residue Resolution
Mukrasch, M. D., Bibow, S., Korukottu, J., Jeganathan, S., Biernat, J., Griesinger, C., Mandelkow, E., & Zweckstetter, M. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000034 · Cited by 652
Dickey, C. A., Kamal, A., Lundgren, K., Klosak, N., Bailey, R. M., Dunmore, J., Ash, P., Shoraka, S., Zlatkovic, J., Eckman, C. B., et al. (2007) · Journal of Clinical Investigation · doi:10.1172/jci29715 · Cited by 642
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 · cited 2×
“Human Hsp90 is tightly controlled by a plethora of co-chaperones [61].”
Meyer, 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
Kirschke, E., Goswami, D., Southworth, D., Griffin, P. R., & Agard, D. A. (2014) · Cell · doi:10.1016/j.cell.2014.04.038 · Cited by 399
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 · cited 10×
“Complementary to the NMR data, SAXS data generated a low-resolution picture of the overall shape of the complex [15].”
InfluentialSelf-citationModulation of the Hsp90 Chaperone Cycle by a Stringent Client Protein
Lorenz, O. R., Freiburger, L., Rutz, D. A., Krause, M., Zierer, B. K., Alvira, S., Cuéllar, J., Valpuesta, J. M., Madl, T., Sattler, M., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.02.003 · Cited by 151 · cited 10×
“It is difficult to produce and to keep in solution; even at room temperature, it is unstable and aggregation-prone [32,48].”
Influential
Cited by
Hsp90 and Hsp70 chaperones: Collaborators in protein remodeling
Genest, O., Wickner, S., & Doyle, S. M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev118.002806 · Cited by 382
The Hsp70–Hsp90 Chaperone Cascade in Protein Folding
Morán Luengo, T., Mayer, M. P., & Rüdiger, S. G. D. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.10.004 · Cited by 282
Self-citationEvolution of heat‐shock protein expression underlying adaptive responses to environmental stress
Chen, B., Feder, M. E., & Kang, L. (2018) · Molecular Ecology · doi:10.1111/mec.14769 · Cited by 267
Stewart, E., McEvoy, J., Wang, H., Chen, X., Honnell, V., Ocarz, M., Gordon, B., Dapper, J., Blankenship, K., Yang, Y., et al. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.07.012 · Cited by 153
Huck, J. D., Que, N. L., Hong, F., Li, Z., & Gewirth, D. T. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.08.079 · Cited by 73
Metadata
- Authors
- Karagöz, G. E., & Rüdiger, S. G. D.
- Venue
- Trends in Biochemical Sciences
- Publisher
- Elsevier BV
- Published
- 2015-02
- Volume
- 40
- Issue
- 2
- Pages
- 117-125
- ISSN
- 0968-0004 (ISSN-L)
- OpenAlex
- W2100215915
- Cited by
- 202
- References
- 13
- FWCI
- 1.88
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Karagöz, G. E., & Rüdiger, S. G. D. (2015). Hsp90 interaction with clients. Trends in Biochemical Sciences. https://doi.org/10.1016/j.tibs.2014.12.002
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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