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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Biophysics· 4 Biochemistry· 3 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Organism:human· 3 Research Focus:protein folding & dynamics· 3 Assay:cryo-EM· 2 Research Focus:host-pathogen & immune response· 2 Approach:microscopy & imaging analysis· 2 Assay:proteomics· 2 Approach:statistical model· 2

Frequent Co-Authors

D. S. Terry· 2 shared M. Lu· 2 shared R. B. Altman· 2 shared W. Mothes· 2 shared A. Bartesaghi· 1 shared A. Brown· 1 shared A. Ferguson· 1 shared A. Finzi· 1 shared

Activity by Year

2018-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

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2 shared papersMicrobiology

D. S. Terry

Mutual co-authors in cluster

Author profile →

8 papers

Recent·Most cited

β-amino acids reduce ternary complex stability and alter the translation elongation mechanism

F. A. Cruz Navarrete, W. C. Griffin, Y.-C. Chan, M. I. Martin, J. L. Alejo, S. K. Natchiar, I. Knudson, R. B. Altman, A. Schepartz, S. J. Miller, S. C. Blanchard

This study investigates how β-amino acid isomers affect ternary complex stability and translation elongation by analyzing their impact on ribosome function and EF-Tu interactions.

bioRxiv · Feb 24, 2024Biochemistry

Structural basis for CFTR inhibition by CFTRinh-172

P. Young, J. Levring, K. Fiedorczuk, S. C. Blanchard, J. Chen

This paper determines the structure of CFTR bound to CFTRinh-172 using cryo-EM, revealing its dual role as a pore blocker and gating modulator.

bioRxiv · Oct 11, 2023 · PreprintBiophysics

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, A. Brown, S. Shao, A. Ferguson, M. R. Wasserman, M. Holm, J. Taunton, 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.

bioRxiv · Aug 1, 2022 · PreprintBiochemistry

Real-time conformational dynamics of SARS-CoV-2 spikes on virus particles

M. Lu, P. D. Uchil, W. Li, D. Zheng, D. S. Terry, J. Gorman, W. Shi, B. Zhang, T. Zhou, S. Ding, R. Gasser, J. Prevost, G. Beaudoin-Bussieres, S. P. Anand, A. Laumaea, , 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.

bioRxiv · Sep 10, 2020Microbiology

The high-energy transition state of a membrane transporter

G. H. M. Huysmans, D. Ciftci, X. Wang, S. C. Blanchard, 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.

bioRxiv · Apr 17, 2020Biophysics

Disruption of the HIV-1 Envelope allosteric network blocks CD4-induced rearrangements

R. Henderson, M. Lu, Y. Zhou, Z. Mu, R. Parks, Q. Han, A. L. Hsu, E. Carter, S. C. Blanchard, R. Edwards, K. Wiehe, K. O. Saunders, M. J. Borgnia, A. Bartesaghi, W. Mothes, , 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.

bioRxiv · Nov 2, 2019Biochemistry

The allosteric mechanism of substrate-specific transport in SLC6 is mediated by a volumetric sensor

M. V. LeVine, D. S. Terry, G. Khelashvili, Z. S. Siegel, M. Quick, J. A. Javitch, S. C. Blanchard, H. Weinstein

The paper identifies an allosteric mechanism involving residues F259 and I359 that modulates Na+ release and substrate transport in SLC6 family proteins.

bioRxiv · Feb 20, 2019Biophysics

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.

bioRxiv · Mar 15, 2018Biophysics