Sriram Subramaniam
Researcher Next ID · RN-033038
Researcher · Biochemistry, Genetics and Molecular Biology
University of British Columbia
Vancouver, Canada
- Works count
- 816
- Citation count
- 20,373
- H-index
- 71
- i10-index
- 188
Research interests
Publications
SARS-CoV-2 Omicron variant: Antibody evasion and cryo-EM structure of spike protein–ACE2 complex
Science · 2022 · https://doi.org/10.1126/science.abn7760
Structure and activity of human TMPRSS2 protease implicated in SARS-CoV-2 activation
Nature Chemical Biology · 2022 · https://doi.org/10.1038/s41589-022-01059-7
Cryo-electron microscopy structures of the N501Y SARS-CoV-2 spike protein in complex with ACE2 and 2 potent neutralizing antibodies
PLoS Biology · 2021 · https://doi.org/10.1371/journal.pbio.3001237
Cryo-EM structure of a dimeric B-Raf:14-3-3 complex reveals asymmetry in the active sites of B-Raf kinases
Science · 2019 · https://doi.org/10.1126/science.aay0543
Cryo-EM structure of human rhodopsin bound to an inhibitory G protein
Nature · 2018 · https://doi.org/10.1038/s41586-018-0215-y
Power Grid Protection of the Muscle Mitochondrial Reticulum
Cell Reports · 2017 · https://doi.org/10.1016/j.celrep.2017.03.063
Cryo-EM Structures Reveal Mechanism and Inhibition of DNA Targeting by a CRISPR-Cas Surveillance Complex
Cell · 2017 · https://doi.org/10.1016/j.cell.2017.09.006
Breaking Cryo-EM Resolution Barriers to Facilitate Drug Discovery
Cell · 2016 · https://doi.org/10.1016/j.cell.2016.05.040
2.3 Å resolution cryo-EM structure of human p97 and mechanism of allosteric inhibition
Science · 2016 · https://doi.org/10.1126/science.aad7974
Focused ion beams in biology
Nature Methods · 2015 · https://doi.org/10.1038/nmeth.3623
2.2 Å resolution cryo-EM structure of β-galactosidase in complex with a cell-permeant inhibitor
Science · 2015 · https://doi.org/10.1126/science.aab1576
Mitochondrial reticulum for cellular energy distribution in muscle
Nature · 2015 · https://doi.org/10.1038/nature14614
Structure of β-galactosidase at 3.2-Å resolution obtained by cryo-electron microscopy
Proceedings of the National Academy of Sciences · 2014 · https://doi.org/10.1073/pnas.1402809111
Structural mechanism of glutamate receptor activation and desensitization
Nature · 2014 · https://doi.org/10.1038/nature13603
A collaborative framework for 3D alignment and classification of heterogeneous subvolumes in cryo-electron tomography
Journal of Structural Biology · 2012 · https://doi.org/10.1016/j.jsb.2012.10.010
Cryo‐electron microscopy – a primer for the non‐microscopist
FEBS Journal · 2012 · https://doi.org/10.1111/febs.12078
Structural Mechanism of Trimeric HIV-1 Envelope Glycoprotein Activation
PLoS Pathogens · 2012 · https://doi.org/10.1371/journal.ppat.1002797
Molecular architecture of native HIV-1 gp120 trimers
Nature · 2008 · https://doi.org/10.1038/nature07159
Electron Tomography of the Contact between T Cells and SIV/HIV-1: Implications for Viral Entry
PLoS Pathogens · 2007 · https://doi.org/10.1371/journal.ppat.0030063
Site-specific 3D imaging of cells and tissues with a dual beam microscope
Journal of Structural Biology · 2006 · https://doi.org/10.1016/j.jsb.2006.03.006
Three-dimensional structure of a bacterial oxalate transporter
Nature Structural Biology · 2002 · https://doi.org/10.1038/nsb821
Molecular mechanism of vectorial proton translocation by bacteriorhodopsin
Nature · 2000 · https://doi.org/10.1038/35020614
Protein conformational changes in the bacteriorhodopsin photocycle 1 1Edited by B. Honig
Journal of Molecular Biology · 1999 · https://doi.org/10.1006/jmbi.1999.2589
Analytical shape computation of macromolecules: II. Inaccessible cavities in proteins.
PubMed · 1998
Electron diffraction analysis of structural changes in the photocycle of bacteriorhodopsin.
The EMBO Journal · 1993 · https://doi.org/10.1002/j.1460-2075.1993.tb05625.x
Current projects
No projects listed.