Search Results - "Agard, David A"

Glucocorticoid Receptor Function Regulated by Coordinated Action of the Hsp90 and Hsp70 Chaperone Cycles by Kirschke, Elaine, Goswami, Devrishi, Southworth, Daniel, Griffin, Patrick R., Agard, David A.

“…The glucocorticoid receptor (GR), like many signaling proteins, depends on the Hsp90 molecular chaperone for in vivo function. Although Hsp90 is required for…”
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MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy by Zheng, Shawn Q, Palovcak, Eugene, Armache, Jean-Paul, Verba, Kliment A, Cheng, Yifan, Agard, David A

“…MotionCor2 software corrects for beam-induced sample motion, improving the resolution of cryo-EM reconstructions…”
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How Hsp90 and Cdc37 Lubricate Kinase Molecular Switches by Verba, Kliment A., Agard, David A.

“…The Hsp90/Cdc37 chaperone system interacts with and supports 60% of the human kinome. Not only are Hsp90 and Cdc37 generally required for initial folding, but…”
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Structural basis of mitochondrial receptor binding and constriction by DRP1 by Kalia, Raghav, Wang, Ray Yu-Ruei, Yusuf, Ali, Thomas, Paul V., Agard, David A., Shaw, Janet M., Frost, Adam

“…Mitochondrial inheritance, genome maintenance and metabolic adaptation depend on organelle fission by dynamin-related protein 1 (DRP1) and its mitochondrial…”
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A molecular pore spans the double membrane of the coronavirus replication organelle by Wolff, Georg, Limpens, Ronald W. A. L., Zevenhoven-Dobbe, Jessika C., Laugks, Ulrike, Zheng, Shawn, de Jong, Anja W. M., Koning, Roman I., Agard, David A., Grünewald, Kay, Koster, Abraham J., Snijder, Eric J., Bárcena, Montserrat

“…Viral RNA exported from the coronavirus replication organelle is likely to be mediated by a crown-shaped molecular pore. A gateway to the cytosol Coronaviruses…”
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Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM by Li, Xueming, Mooney, Paul, Zheng, Shawn, Booth, Christopher R, Braunfeld, Michael B, Gubbens, Sander, Agard, David A, Cheng, Yifan

“…The combination of a direct electron-detection camera that can count individual electrons and an algorithm for correcting for beam-induced motion in cryo-EM…”
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Structure of Hsp90–Hsp70–Hop–GR reveals the Hsp90 client-loading mechanism by Wang, Ray Yu-Ruei, Noddings, Chari M., Kirschke, Elaine, Myasnikov, Alexander G., Johnson, Jill L., Agard, David A.

“…Maintaining a healthy proteome is fundamental for the survival of all organisms 1 . Integral to this are Hsp90 and Hsp70, molecular chaperones that together…”
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The Cancer Cell Map Initiative: Defining the Hallmark Networks of Cancer by Krogan, Nevan J., Lippman, Scott, Agard, David A., Ashworth, Alan, Ideker, Trey

“…Progress in DNA sequencing has revealed the startling complexity of cancer genomes, which typically carry thousands of somatic mutations. However, it remains…”
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General and robust covalently linked graphene oxide affinity grids for high-resolution cryo-EM by Wang, Feng, Liu, Yanxin, Yu, Zanlin, Li, Sam, Feng, Shengjie, Cheng, Yifan, Agard, David A.

“…Affinity grids have great potential to facilitate rapid preparation of even quite impure samples in single-particle cryo-electron microscopy (EM). Yet despite…”
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Client-Loading Conformation of the Hsp90 Molecular Chaperone Revealed in the Cryo-EM Structure of the Human Hsp90:Hop Complex by Southworth, Daniel R., Agard, David A.

“…Hsp90 is an essential molecular chaperone required for the folding and activation of many hundreds of cellular “client” proteins. The ATP-dependent chaperone…”
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Electron cryotomography of intact motile cilia defines the basal body to axoneme transition by Greenan, Garrett A, Vale, Ronald D, Agard, David A

“…Cells use motile cilia to generate force in the extracellular space. The structure of a cilium can be classified into three subdomains: the intracellular basal…”
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Substrate Binding Drives Large-Scale Conformational Changes in the Hsp90 Molecular Chaperone by Street, Timothy O., Lavery, Laura A., Agard, David A.

“…Hsp90 is a ubiquitous molecular chaperone. Previous structural analysis demonstrated that Hsp90 can adopt a large number of structurally distinct…”
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Asynchronous data acquisition and on-the-fly analysis of dose fractionated cryoEM images by UCSFImage by Li, Xueming, Zheng, Shawn, Agard, David A., Cheng, Yifan

“…Newly developed direct electron detection cameras have a high image output frame rate that enables recording dose fractionated image stacks of frozen hydrated…”
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Assembly of a nucleus-like structure during viral replication in bacteria by Chaikeeratisak, Vorrapon, Nguyen, Katrina, Khanna, Kanika, Brilot, Axel F., Erb, Marcella L., Coker, Joanna K. C., Vavilina, Anastasia, Newton, Gerald L., Buschauer, Robert, Pogliano, Kit, Villa, Elizabeth, Agard, David A., Pogliano, Joe

“…We observed the assembly of a nucleus-like structure in bacteria during viral infection. Using fluorescence microscopy and cryo-electron tomography, we showed…”
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Hsp90 provides a platform for kinase dephosphorylation by PP5 by Jaime-Garza, Maru, Nowotny, Carlos A., Coutandin, Daniel, Wang, Feng, Tabios, Mariano, Agard, David A.

“…The Hsp90 molecular chaperone collaborates with the phosphorylated Cdc37 cochaperone for the folding and activation of its many client kinases. As with many…”
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In situ cryo-electron tomography reveals the asymmetric architecture of mammalian sperm axonemes by Chen, Zhen, Greenan, Garrett A., Shiozaki, Momoko, Liu, Yanxin, Skinner, Will M., Zhao, Xiaowei, Zhao, Shumei, Yan, Rui, Yu, Zhiheng, Lishko, Polina V., Agard, David A., Vale, Ronald D.

“…The flagella of mammalian sperm display non-planar, asymmetric beating, in contrast to the planar, symmetric beating of flagella from sea urchin sperm and…”
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Competing protein-protein interactions regulate binding of Hsp27 to its client protein tau by Freilich, Rebecca, Betegon, Miguel, Tse, Eric, Mok, Sue-Ann, Julien, Olivier, Agard, David A., Southworth, Daniel R., Takeuchi, Koh, Gestwicki, Jason E.

“…Small heat shock proteins (sHSPs) are a class of oligomeric molecular chaperones that limit protein aggregation. However, it is often not clear where sHSPs…”
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Uncovering a Region of Heat Shock Protein 90 Important for Client Binding in E. coli and Chaperone Function in Yeast by Genest, Olivier, Reidy, Michael, Street, Timothy O., Hoskins, Joel R., Camberg, Jodi L., Agard, David A., Masison, Daniel C., Wickner, Sue

“…The heat shock protein 90 (Hsp90) family of heat shock proteins is an abundantly expressed and highly conserved family of ATP-dependent molecular chaperones…”
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Mind the gap: Micro-expansion joints drastically decrease the bending of FIB-milled cryo-lamellae by Wolff, Georg, Limpens, Ronald W.A.L., Zheng, Shawn, Snijder, Eric J., Agard, David A., Koster, Abraham J., Bárcena, Montserrat

“…[Display omitted] •Micro-expansion joints greatly increase the cryo-FIB-milling success rate.•These lateral gaps milled in the support prevent cryo-lamellae…”
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The ϕPA3 phage nucleus is enclosed by a self-assembling 2D crystalline lattice by Nieweglowska, Eliza S., Brilot, Axel F., Méndez-Moran, Melissa, Kokontis, Claire, Baek, Minkyung, Li, Junrui, Cheng, Yifan, Baker, David, Bondy-Denomy, Joseph, Agard, David A.

“…To protect themselves from host attack, numerous jumbo bacteriophages establish a phage nucleus—a micron-scale, proteinaceous structure encompassing the…”
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