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Author Details

David A Agard
University of California, USA Quantitative Biosciences Institute (QBI) san francisco
1977
281
87
Trey Ideker (CM4AI)
PMIDPaper TitleJournal TitlePublished Year
36629399Improved Analysis of Cross-Linking Mass Spectrometry Data with Kojak 2.0, Advanced by Integration into the Trans-Proteomic Pipeline.J Proteome Res2023
37865089De novo protein identification in mammalian sperm using in situ cryoelectron tomography and AlphaFold2 docking.Cell2023
38014135Poc1 is a basal body inner junction protein that promotes triplet microtubule integrity and interconnections.bioRxiv2023
37620325Next-generation proteomics for quantitative Jumbophage-bacteria interaction mapping.Nat Commun2023
37546986Functionalized graphene-oxide grids enable high-resolution cryo-EM structures of the SNF2h-nucleosome complex without crosslinking.bioRxiv2023
37945740Cryo-EM reveals how Hsp90 and FKBP immunophilins co-regulate the glucocorticoid receptor.Nat Struct Mol Biol2023
37069154Hsp90 provides a platform for kinase dephosphorylation by PP5.Nat Commun2023
36807264The ϿPA3 phage nucleus is enclosed by a self-assembling 2D crystalline lattice.Nat Commun2023
36711836Next-generation interaction proteomics for quantitative Jumbophage-bacteria interaction mapping.bioRxiv2023
36711821Cryo-EM reveals how Hsp90 and FKBP immunophilins co-regulate the Glucocorticoid Receptor.bioRxiv2023
34937936Structure of Hsp90-p23-GR reveals the Hsp90 client-remodelling mechanism.Nature2022
35601683AreTomo: An integrated software package for automated marker-free, motion-corrected cryo-electron tomographic alignment and reconstruction.J Struct Biol X2022
36644294Solution of the protein structure prediction problem at last: crucial innovations and next frontiers.Fac Rev2022
35926713Interactions between mTORC2 core subunits Rictor and mSin1 dictate selective and context-dependent phosphorylation of substrate kinases SGK1 and Akt.J Biol Chem2022
35132240Author Correction: Structures of the HER2-HER3-NRG1β complex reveal a dynamic dimer interface.Nature2022
34937942Structure of Hsp90-Hsp70-Hop-GR reveals the Hsp90 client-loading mechanism.Nature2022
33949948CM1-driven assembly and activation of yeast γ-tubulin small complex underlies microtubule nucleation.Elife2021
33734292Microtubules form by progressively faster tubulin accretion, not by nucleation-elongation.J Cell Biol2021
34876518Entropy-regularized deconvolution of cellular cryotransmission electron tomograms.Proc Natl Acad Sci U S A2021
34969817Electron cryo-tomography structure of axonemal doublet microtubule from <i>Tetrahymena thermophila</i>.Life Sci Alliance2021
34759323Structures of the HER2-HER3-NRG1β complex reveal a dynamic dimer interface.Nature2021
34406789Proteomic analysis of microtubule inner proteins (MIPs) in Rib72 null <i>Tetrahymena</i> cells reveals functional MIPs.Mol Biol Cell2021
34013269CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes.bioRxiv2021
34031651CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes.Res Sq2021
32296038Author Correction: Sas-4 provides a scaffold for cytoplasmic complexes and tethers them in a centrosome.Nat Commun2020
31874113Electron cryotomography of intact motile cilia defines the basal body to axoneme transition.J Cell Biol2020
31866389Amino and PEG-amino graphene oxide grids enrich and protect samples for high-resolution single particle cryo-electron microscopy.J Struct Biol2020
31987035The mitochondrial HSP90 paralog TRAP1 forms an OXPHOS-regulated tetramer and is involved in mitochondrial metabolic homeostasis.BMC Biol2020
31819262A bacteriophage nucleus-like compartment shields DNA from CRISPR nucleases.Nature2020
33060197Comparative host-coronavirus protein interaction networks reveal pan-viral disease mechanisms.Science2020
32913054General and robust covalently linked graphene oxide affinity grids for high-resolution cryo-EM.Proc Natl Acad Sci U S A2020
32763915A molecular pore spans the double membrane of the coronavirus replication organelle.Science2020
32726183XMAP215 and γ-tubulin additively promote microtubule nucleation in purified solutions.Mol Biol Cell2020
32353859A SARS-CoV-2 protein interaction map reveals targets for drug repurposing.Nature2020
30690142Consideration of sample motion in cryo-tomography based on alignment residual interpolation.J Struct Biol2019
31740740Novel Small Molecules Targeting the Intrinsically Disordered Structural Ensemble of α-Synuclein Protect Against Diverse α-Synuclein Mediated Dysfunctions.Sci Rep2019
31199917Viral Capsid Trafficking along Treadmilling Tubulin Filaments in Bacteria.Cell2019
31536774Mind the gap: Micro-expansion joints drastically decrease the bending of FIB-milled cryo-lamellae.J Struct Biol2019
30741631Electron cryo-tomography provides insight into procentriole architecture and assembly mechanism.Elife2019
29315319The centrosomin CM2 domain is a multi-functional binding domain with distinct cell cycle roles.PLoS One2018
30080137Insights into centriole geometry revealed by cryotomography of doublet and triplet centrioles.Elife2018
30053424The Psychiatric Cell Map Initiative: A Convergent Systems Biological Approach to Illuminating Key Molecular Pathways in Neuropsychiatric Disorders.Cell2018
29991590Calcium binding to a remote site can replace magnesium as cofactor for mitochondrial Hsp90 (TRAP1) ATPase activity.J Biol Chem2018
30017701A simple and robust procedure for preparing graphene-oxide cryo-EM grids.J Struct Biol2018
29899447Structural basis of mitochondrial receptor binding and constriction by DRP1.Nature2018
30385828Competing protein-protein interactions regulate binding of Hsp27 to its client protein tau.Nat Commun2018
29410148Cryo-tomography tilt-series alignment with consideration of the beam-induced sample motion.J Struct Biol2018
29320629The Structural Asymmetry of Mitochondrial Hsp90 (Trap1) Determines Fine Tuning of Functional Dynamics.J Chem Theory Comput2018
27983786Internal Structure and Preferential Protein Binding of Colloidal Aggregates.ACS Chem Biol2017
28082593Assembly of a nucleus-like structure during viral replication in bacteria.Science2017
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Collaborators

Quantitative Bioscience Institute, University of California san francisco
Co-authored papers 16
University of California san francisco
Co-authored papers 14
University of Washington
Co-authored papers 12
University of California, University of California San Francisco
Co-authored papers 11
The Institute for Neurodegenerative Diseases, University of California San Francisco
Co-authored papers 11
University of California san francisco
Co-authored papers 10
University of California San Francisco
Co-authored papers 10
University of California San Francisco
Co-authored papers 9
Harvard Medical School
Co-authored papers 9
University of Washington
Co-authored papers 9
University of Washington
Co-authored papers 9
University of California San Francisco
Co-authored papers 9
Co-authored papers 8
University of California at San Francisco
Co-authored papers 8
University of Washington
Co-authored papers 8
Brandeis University
Co-authored papers 7
University of California san francisco
Co-authored papers 7
University of California San Francisco
Co-authored papers 7
University of California san francisco
Co-authored papers 7
University of Dundee
Co-authored papers 6
Cardiovascular Research Institute, University of California San Francisco
Co-authored papers 6
J. David Gladstone Institutes
Co-authored papers 6
the University of Texas Southwestern Medical Center
Co-authored papers 6
Cardiovascular Research Institute, University of California San Francisco
Co-authored papers 6
National Center for Biotechnology, Spanish National Research Council
Co-authored papers 6
Department of Pharmaceutical Chemistry, University of California san francisco
Co-authored papers 5
Co-authored papers 5
University of California san francisco
Co-authored papers 5
School of Clinical Medicine, University of Hong Kong
Co-authored papers 4
University of California san francisco
Co-authored papers 4