The DOI matches its Crossref record; 44 of the 44 references it cites were found in a registry or an index.
Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s
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Cites
Sikorski, R. S., & Hieter, P. (1989) · Genetics · doi:10.1093/genetics/122.1.19 · Cited by 8,664
Sherman, F., Fink, G. R., & Hicks, J. B. (1979) · Cold Spring Harbor Laboratory eBooks · Cited by 7,430
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
Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein
Hartl, F. U., & Hayer-Hartl, M. (2002) · Science · doi:10.1126/science.1068408 · Cited by 3,347
Self-citationThe Hsp70 and Hsp60 Chaperone Machines
Bukau, B., & Horwich, A. L. (1998) · Cell · doi:10.1016/s0092-8674(00)80928-9 · Cited by 2,815
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
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
JPred: a consensus secondary structure prediction server.
Cuff, J. A., Clamp, M. E., Siddiqui, A. S., Finlay, M., & Barton, G. J. (1998) · Bioinformatics · doi:10.1093/bioinformatics/14.10.892 · Cited by 1,006
The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins
Connell, P., Ballinger, C. A., Jiang, J., Wu, Y., Thompson, L. J., Höhfeld, J., & Patterson, C. (2001) · Nature Cell Biology · doi:10.1038/35050618 · Cited by 997
Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK.
Liberek, K., Marszalek, J., Ang, D., Georgopoulos, C., & Zylicz, M. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.7.2874 · Cited by 845
Cited by
The HSP70 chaperone machinery: J proteins as drivers of functional specificity
Kampinga, H. H., & Craig, E. A. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2941 · Cited by 1,755
Guidelines for the nomenclature of the human heat shock proteins
Kampinga, H. H., Hageman, J., Vos, M. J., Kubota, H., Tanguay, R. M., Bruford, E. A., Cheetham, M. E., Chen, B., & Hightower, L. E. (2009) · Cell Stress and Chaperones · doi:10.1007/s12192-008-0068-7 · Cited by 1,360
Verghese, J., Abrams, J., Wang, Y., & Morano, K. A. (2012) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.05018-11 · Cited by 575
Protein Quality Control in the Cytosol and the Endoplasmic Reticulum: Brothers in Arms
Buchberger, A., Bukau, B., & Sommer, T. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.001 · Cited by 483
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
Metadata
- Authors
- Dragovic, Z., Broadley, S. A., Shomura, Y., Bracher, A., & Hartl, F. U.
- Venue
- The EMBO Journal
- Published
- 2006-05-11
- Volume
- 25
- Issue
- 11
- Pages
- 2519-2528
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- OpenAlex
- W2047477750
- Cited by
- 381
- References
- 44
- FWCI
- 7.37
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s. https://app.cochat.ai/papers/10.1038/sj.emboj.7601138
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- Dragovic, Z., Broadley, S. A., Shomura, Y., Bracher, A., & Hartl, F. U. (2006). Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s. The EMBO Journal. https://doi.org/10.1038/sj.emboj.7601138
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
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.
