Author

V. Q. Le

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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Biochemistry· 2 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Assay:structural biology· 2 Research Focus:chromatin & epigenetic regulation· 1 Approach:deep learning· 1 Research Focus:drug response / drug discovery· 1 Organism:mouse· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1

Frequent Co-Authors

T. A. Springer· 3 shared B. Zhao· 2 shared J. R. Engen· 2 shared R. E. Iacob· 2 shared Y. Tian· 2 shared A. Chang· 1 shared A. Fernandez· 1 shared A. K. Bera· 1 shared

Activity by Year

2017-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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3 shared papersBiochemistry

T. A. Springer

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Author profile →

3 papers

Recent·Most cited

De novo design of highly selective miniprotein inhibitors of integrins αvβ6 and αvβ8

A. Roy, L. Shi, A. Chang, X. Dong, A. Fernandez, J. C. Kraft, J. Li, V. Q. Le, R. V. Winegar, G. M. Cherf, D. Slocum, P. D. Poulson, G. E. casper, M. L. Vallecillo-Zuniga, J. C. Valdoz, , D. Baker

This paper designs highly selective miniprotein inhibitors for integrins αvβ6 and αvβ8 with picomolar affinity and therapeutic potential in a mouse fibrosis model.

bioRxiv · Jun 12, 2023 · PreprintBiochemistry

Protection of the prodomain 1-helix correlates with latency in the transforming growth factor- family

V. Q. Le, B. Zhao, R. E. Iacob, Y. Tian, C. Toohey, J. R. Engen, T. A. Springer

The paper investigates the structural basis of latency in TGF-beta family members by comparing conformational states and hydrogen-deuterium exchange patterns across multiple family members.

bioRxiv · Jun 24, 2021Biophysics

Tolloid cleavage activates latent GDF8 by priming the pro-complex for dissociation

V. Q. Le, R. E. Iacob, Y. Tian, W. McConaughy, J. Jackson, Y. Su, B. Zhao, J. R. Engen, M. Pirruccello-Straub, T. A. Springer

This study shows Tolloid cleavage activates latent GDF8 by destabilizing prodomain-growth factor interfaces and priming the growth factor for release.

bioRxiv · Aug 3, 2017Biochemistry