about
Cryo-EM of viruses and vaccine designHIV-1 envelope glycoprotein structureCatching HIV 'in the act' with 3D electron microscopy3D imaging of mammalian cells with ion-abrasion scanning electron microscopyMolecular architectures of trimeric SIV and HIV-1 envelope glycoproteins on intact viruses: strain-dependent variation in quaternary structureCryo-EM Analysis of the Conformational Landscape of Human P-glycoprotein (ABCB1) During its Catalytic Cycle.Protein Secondary Structure Determination by Constrained Single-Particle Cryo-Electron TomographyPrefusion structure of trimeric HIV-1 envelope glycoprotein determined by cryo-electron microscopyStructure of -galactosidase at 3.2-A resolution obtained by cryo-electron microscopy2.2 Å resolution cryo-EM structure of β-galactosidase in complex with a cell-permeant inhibitor2.3 Å resolution cryo-EM structure of human p97 and mechanism of allosteric inhibitionStructural basis of kainate subtype glutamate receptor desensitization.Projection structure and molecular architecture of OxlT, a bacterial membrane transporter.Structure and accessibility of HA trimers on intact 2009 H1N1 pandemic influenza virus to stem region-specific neutralizing antibodiesResolution advances in cryo-EM enable application to drug discovery.Mapping of Ebolavirus Neutralization by Monoclonal Antibodies in the ZMapp Cocktail Using Cryo-Electron Tomography and Studies of Cellular EntryCryo-EM Structures of the Magnesium Channel CorA Reveal Symmetry Break upon Gating.Spatial localization of the Ebola virus glycoprotein mucin-like domain determined by cryo-electron tomography.Cell surface filaments of the gliding bacterium Flavobacterium johnsoniae revealed by cryo-electron tomographyRole of HAMP domains in chemotaxis signaling by bacterial chemoreceptors.3D visualization of HIV transfer at the virological synapse between dendritic cells and T cellsData management challenges in three-dimensional EM.Three-dimensional imaging of HIV-1 virological synapses reveals membrane architectures involved in virus transmission.Structural mechanism of glutamate receptor activation and desensitization.Maturation of the HIV-1 core by a non-diffusional phase transition.Automated data collection with a Tecnai 12 electron microscope: applications for molecular imaging by cryomicroscopy.The crystal structure of human GlnRS provides basis for the development of neurological disorders.Breaking Cryo-EM Resolution Barriers to Facilitate Drug Discovery.Protein conformational changes in the bacteriorhodopsin photocycle: comparison of findings from electron and X-ray crystallographic analyses.Automated image acquisition and processing using a new generation of 4K x 4K CCD cameras for cryo electron microscopic studies of macromolecular assemblies.Projection structure of the bacterial oxalate transporter OxlT at 3.4A resolution.Electron tomography of the contact between T cells and SIV/HIV-1: implications for viral entry.Evaluation of denoising algorithms for biological electron tomography.Cryo-electron tomography of bacteria: progress, challenges and future prospects.Replacement of aspartic residues 85, 96, 115, or 212 affects the quantum yield and kinetics of proton release and uptake by bacteriorhodopsin.Power Grid Protection of the Muscle Mitochondrial Reticulum.The residues Leu 93 and Asp 96 act independently in the bacteriorhodopsin photocycle: studies with the leu 93-->Ala, Asp 96-->Asn double mutant.Three-dimensional structures of soluble CD4-bound states of trimeric simian immunodeficiency virus envelope glycoproteins determined by using cryo-electron tomographyCCD detectors in high-resolution biological electron microscopy.Chemical mapping of mammalian cells by atom probe tomography.
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description
researcher
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wetenschapper
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հետազոտող
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name
Sriram Subramaniam
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Sriram Subramaniam
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Sriram Subramaniam
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Sriram Subramaniam
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type
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Sriram Subramaniam
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Sriram Subramaniam
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Sriram Subramaniam
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Sriram Subramaniam
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Subramaniam S
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Sriram Subramaniam
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Sriram Subramaniam
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Sriram Subramaniam
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Sriram Subramaniam
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P106
P1153
7102872243
P31
P4012
P496
0000-0003-4231-4115