Author
S. C. Blanchard
Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.
Biology Disciplines
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2018-2023 · peak 2/yrCo-Author Collaboration Network
10 top collaborators · 20 mutual co-author links7 papers
Recent·Most cited
- BiochemistrybioRxivPreprint
Didemnin B and ternatin-4 inhibit conformational changes in eEF1A required for aminoacyl-tRNA accommodation into mammalian ribosomes
M. F. Juette, J. D. Carelli, E. J. Rundlet…·S. C. Blanchard
This study shows how didemnin B and ternatin-4 inhibit translation by trapping eEF1A in a GTPase-activated conformation using single-molecule imaging and cryo-EM.
- MicrobiologybioRxiv
Real-time conformational dynamics of SARS-CoV-2 spikes on virus particles
M. Lu, P. D. Uchil, W. Li…·W. Mothes
This study uses smFRET to observe real-time conformational dynamics of SARS-CoV-2 spikes on virus particles, revealing multiple states and mechanisms of neutralization by antibodies and convalescent plasma.
DOI 10.1016/j.chom.2020.11.001 - BiophysicsbioRxiv
The high-energy transition state of a membrane transporter
G. H. M. Huysmans, D. Ciftci, X. Wang…·O. Boudker
The paper identifies the high-energy transition state of a membrane transporter and proposes an approach for allosteric modulation based on structural analysis.
DOI 10.15252/embj.2020105415 - BiochemistrybioRxiv
Disruption of the HIV-1 Envelope allosteric network blocks CD4-induced rearrangements
R. Henderson, M. Lu, Y. Zhou…·S. M. Alam
This study identifies a critical role for W571 in HIV-1 Env allostery by showing mutations disrupting CD4-induced rearrangements and rendering Env insensitive to CD4 binding.
DOI 10.1038/s41467-019-14196-w - BiophysicsbioRxiv
The allosteric mechanism of substrate-specific transport in SLC6 is mediated by a volumetric sensor
M. V. LeVine, D. S. Terry, G. Khelashvili…·H. Weinstein
The paper identifies an allosteric mechanism involving residues F259 and I359 that modulates Na+ release and substrate transport in SLC6 family proteins.
DOI 10.1073/pnas.1903020116 - BiophysicsbioRxiv
ERASE: a novel surface reconditioning strategy for single-molecule experiments
D. W. B. Broadwater, R. B. Altman, S. C. Blanchard, H. D. Kim
The paper introduces ERASE, a method to reuse single-molecule experiment surfaces by removing biomolecules via DNA strand displacement, enabling repeated use and parallel molecule analysis.
DOI 10.1093/nar/gky1168