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The Molecular Chaperone gp96/GRP94 Interacts with Toll-like Receptors and Integrins via Its C-terminal Hydrophobic Domain

The structural basis for molecular chaperones to discern misfolded proteins has long been an enigma. As the endoplasmic reticulum paralogue of the cytosolic HSP90, gp96 (GRP94, HSP90b1) is an essential molecular chaperone for Toll-like receptors (TLRs) and integrins. However, little is known about i...

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Bibliografiset tiedot
Päätekijät: Wu, Shuang, Hong, Feng, Gewirth, Daniel, Guo, Beichu, Liu, Bei, Li, Zihai
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: American Society for Biochemistry and Molecular Biology 2012
Aiheet:
Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC3307303/
https://ncbi.nlm.nih.gov/pubmed/22223641
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M111.309526
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