Agard, David A.

Cryo-EM structures reveal a multistep mechanism of Hsp90 activation by co-chaperone Aha1

Liu, Y., Sun, M., Myasnikov, A. G., Elnatan, D., Delaeter, N., Nguyenquang, M., & Agard, D. A. (2020) · bioRxiv (Cold Spring Harbor Laboratory)

Heat shock proteins researchProtein Structure and Dynamics

Cited by 37

Cryo-EM reveals the dynamic interplay between mitochondrial Hsp90 and SdhB folding intermediates

Liu, Y., Elnatan, D., Sun, M., Myasnikov, A. G., & Agard, D. A. (2020) · bioRxiv (Cold Spring Harbor Laboratory)

Heat shock proteins researchMitochondrial Function and Pathology

Cited by 16

A distributed multi-GPU system for high speed electron microscopic tomographic reconstruction

Zheng, S. Q., Branlund, E., Kesthelyi, B., Braunfeld, M. B., Cheng, Y., Sedat, J. W., & Agard, D. A. (2011) · Ultramicroscopy

Advanced Electron Microscopy Techniques and ApplicationsParallel Computing and Optimization Techniques

Cited by 13

GR chaperone cycle mechanism revealed by cryo-EM: inactivation of GR by GR:Hsp90:Hsp70:Hop client-loading complex

Wang, R. Y.-R., Noddings, C. M., Kirschke, E., Myasnikov, A. G., Johnson, J. L., & Agard, D. A. (2020) · bioRxiv (Cold Spring Harbor Laboratory)

Heat shock proteins researchProtein Structure and Dynamics

Cited by 10

The interplay between Bag-1, Hsp70, and Hsp90 reveals that inhibiting Hsp70 rebinding is essential for Glucocorticoid Receptor activity

Kirschke, E., Roe-Zurz, Z., Noddings, C., & Agard, D. (2020) · bioRxiv (Cold Spring Harbor Laboratory)

Heat shock proteins researchReceptor Mechanisms and Signaling

Cited by 6