The DOI matches its Crossref record; 76 of the 76 references it cites were found in a registry or an index.
Gymnastics of Molecular Chaperones
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Citations
Cites
Hsp70 chaperones: Cellular functions and molecular mechanism
Mayer, M. P., & Bukau, B. (2005) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4464-6 · Cited by 2,865
Self-citationDynamic personalities of proteins
Henzler-Wildman, K., & Kern, D. (2007) · Nature · doi:10.1038/nature06522 · Cited by 2,545
The crystal structure of the bacterial chaperonln GroEL at 2.8 Å
Braig, K., Otwinowski, Z., Hegde, R., Boisvert, D. C., Joachimiak, A., Horwich, A. L., & Sigler, P. B. (1994) · Nature · doi:10.1038/371578a0 · Cited by 1,321
Prodromou, C., Roe, S. M., O'Brien, R., Ladbury, J. E., Piper, P. W., & Pearl, L. H. (1997) · Cell · doi:10.1016/s0092-8674(00)80314-1 · Cited by 1,265
Structural Analysis of Substrate Binding by the Molecular Chaperone DnaK
Zhu, X., Zhao, X., Burkholder, W. F., Gragerov, A., Ogata, C. M., Gottesman, M. E., & Hendrickson, W. A. (1996) · Science · doi:10.1126/science.272.5268.1606 · Cited by 1,258
The crystal structure of the asymmetric GroEL–GroES–(ADP)7 chaperonin complex
Xu, Z., Horwich, A. L., & Sigler, P. B. (1997) · Nature · doi:10.1038/41944 · Cited by 1,239
Converging concepts of protein folding in vitro and in vivo
Hartl, F. U., & Hayer-Hartl, M. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1591 · Cited by 1,185
Folding of Newly Translated Proteins In Vivo: The Role of Molecular Chaperones
Frydman, J. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.603 · Cited by 1,173
Structure and mechanism of the Hsp90 molecular chaperone machinery
Pearl, L. H., & Prodromou, C. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142738 · Cited by 1,103
Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein
Flaherty, K. M., DeLuca-Flaherty, C., & McKay, D. B. (1990) · Nature · doi:10.1038/346623a0 · Cited by 1,030
Cited by
Molecular chaperones in protein folding and proteostasis
Hartl, F. U., Bracher, A., & Hayer-Hartl, M. (2011) · Nature · doi:10.1038/nature10317 · Cited by 3,381
Amm, I., Sommer, T., & Wolf, D. H. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.06.031 · Cited by 493
Crosstalk between Hsp90 and Hsp70 Chaperones and Heat Stress Transcription Factors in Tomato
Hahn, A., Bublak, D., Schleiff, E., & Scharf, K.-D. (2011) · The Plant Cell · doi:10.1105/tpc.110.076018 · Cited by 396
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
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
“Crucial for the chaperone network in the cytoplasm are the ATP-driven Hsp70 and Hsp90 families (Bukau et al., 2006; Mayer, 2010).”
BackgroundInfluential
Metadata
- Authors
- Mayer, M. P.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2010-08
- Volume
- 39
- Issue
- 3
- Pages
- 321-331
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2046629597
- Cited by
- 364
- References
- 76
- FWCI
- 13.23
- Type
- journal article
- Language
- en
- Open access
- bronze
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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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