Different Grp94 components interact transiently with the myocilin olfactomedin domain in vitro to enhance or retard its amyloid aggregation
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/s41598-019-48751-8.pdf
Reference63 articles.
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3. Mayer, M. P. & Le Breton, L. Hsp90: Breaking the symmetry. Mol Cell 58, 8–20, https://doi.org/10.1016/j.molcel.2015.02.022 (2015).
4. Maharaj, K. A. et al. Exploring the functional complementation between grp94 and hsp90. Plos One 11, https://doi.org/10.1371/journal.pone.0166271 (2016).
5. Marzec, M., Eletto, D. & Argon, Y. Grp94: An hsp90-like protein specialized for protein folding and quality control in the endoplasmic reticulum. Bba-Mol Cell Res 1823, 774–787, https://doi.org/10.1016/j.bbamcr.2011.10.013 (2012).
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