Evaluation of competing J domain:Hsp70 complex models in light of existing mutational and NMR data
- PMID: 22403069
- PMCID: PMC3323956
- DOI: 10.1073/pnas.1120597109
Evaluation of competing J domain:Hsp70 complex models in light of existing mutational and NMR data
Conflict of interest statement
The authors declare no conflict of interest.
Comment on
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Heat shock protein 70 kDa chaperone/DnaJ cochaperone complex employs an unusual dynamic interface.Proc Natl Acad Sci U S A. 2011 Nov 22;108(47):18966-71. doi: 10.1073/pnas.1111220108. Epub 2011 Nov 7. Proc Natl Acad Sci U S A. 2011. PMID: 22065753 Free PMC article.
References
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- Garimella R, et al. Hsc70 contacts helix III of the J domain from polyomavirus T antigens: Addressing a dilemma in the chaperone hypothesis of how they release E2F from pRb. Biochemistry. 2006;45:6917–6929. - PubMed
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- Sousa R, et al. Evaluation of competing J domain:Hsp70 complex models in light of existing mutational and NMR data. 2011. arXiv:1112.3298v1 [q-bio.BM]. Available at http://arxiv.org/abs/1112.3298. Accessed February 15, 2012. - PMC - PubMed
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