Mechanisms of Protein Quality Control in the Endoplasmic Reticulum by a Coordinated Hsp40-Hsp70-Hsp90 System von Kotler, Judy L.M, Street, Timothy O

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The endoplasmic reticulum (ER) chaperones BiP and Grp94 selectively associate when BiP is in the ADP conformation von Sun, Ming, Kotler, Judy L.M., Liu, Shanshan, Street, Timothy O.

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The endoplasmic reticulum chaperone BiP is a closure-accelerating cochaperone of Grp94 von Huang, Bin, Sun, Ming, Hoxie, Reyal, Kotler, Judy L. M., Friedman, Larry J., Gelles, Jeff, Street, Timothy O.

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The ER Chaperones BiP and Grp94 Regulate the Formation of Insulin-Like Growth Factor 2 (IGF2) Oligomers von Jin, Yi, Kotler, Judy L.M., Wang, Shiyu, Huang, Bin, Halpin, Jackson C., Street, Timothy O.

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Electrostatics Drive the Molecular Chaperone BiP to Preferentially Bind Oligomerized States of a Client Protein von Deans, Erin E., Kotler, Judy L.M., Wei, Wei-Shao, Street, Timothy O.

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The Enzymatic Activity of Inosine 5′-Monophosphate Dehydrogenase May Not Be a Vulnerable Target for Staphylococcus aureus Infections von Modi, Gyan, Marqus, Gary M, Vippila, Mohana Rao, Gollapalli, Deviprasad R, Kim, Youngchang, Manna, Adhar C, Chacko, Shibin, Maltseva, Natalia, Wang, Xingyou, Cullinane, Ryan T, Zhang, Yubo, Kotler, Judy L. M, Kuzmic, Petr, Zhang, Minjia, Lawson, Ann P, Joachimiak, Andrzej, Cheung, Ambrose, Snider, Barry B, Rothstein, David M, Cuny, Gregory D, Hedstrom, Lizbeth

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