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GRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulum
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Folding and secretion of a very restrictive number of client proteins are solely dependent on GRP94.
“folding and secretion of a very restrictive number of client proteins were solely dependent on GRP94”
From GRP94 Regulates Circulating Cholesterol Levels through Blockade of PCSK9-Induced LDLR Degradation (2015) · cites this paper as Marzec et al., 2012
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Oxidized Redox State of Glutathione in the Endoplasmic Reticulum
Hwang, C., Sinskey, A. J., & Lodish, H. F. (1992) · Science · doi:10.1126/science.1523409 · Cited by 1,968
HDAC6 Regulates Hsp90 Acetylation and Chaperone-Dependent Activation of Glucocorticoid Receptor
Kovacs, J. J., Murphy, P. J. M., Gaillard, S., Zhao, X., Wu, J.-T., Nicchitta, C. V., Yoshida, M., Toft, D. O., Pratt, W. B., & Yao, T.-P. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.04.021 · Cited by 1,153
An 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
Mixed Hsp90–cochaperone complexes are important for the progression of the reaction cycle
Li, J., Richter, K., & Buchner, J. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1965 · Cited by 155
Ko, M. H., & Puglielli, L. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m804901200 · Cited by 111
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Metadata
- Authors
- Marzec, M., Eletto, D., & Argon, Y.
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Publisher
- Elsevier BV
- Published
- 2012-03
- Volume
- 1823
- Issue
- 3
- Pages
- 774-787
- ISSN
- 0167-4889
- PMC
- PMC3443595
- Cited by
- 390
- References
- 5
- Language
- en
- Licence
- Funders
- NIH
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