Author

V. L. Lam

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· 1 Cell Biology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:human· 2 Research Focus:cancer & tumor microenvironment· 1 Research Focus:cell type annotation· 1 Assay:cryo-EM· 1 Approach:deep learning· 1 Approach:genetic perturbation / CRISPR· 1 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

J. D. Gross· 2 shared A. Cruz· 1 shared A. Diallo· 1 shared A. F. Brilot· 1 shared A. Fossati· 1 shared A. J. Samelson· 1 shared A. M. Smith· 1 shared A. Mancino· 1 shared

Activity by Year

2021-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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2 shared papersCell Biology

J. D. Gross

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

CRISPR screens in iPSC-derived neurons reveal principles of tau proteostasis

A. J. Samelson, N. Ariqat, J. McKetney, G. Rohanitazangi, C. Parra Bravo, R. Bose, K. J. Travaglini, V. L. Lam, D. Goodness, G. Dixon, E. Marzette, J. Jin, R. Tian, E. Tse, R. Abskharon, , M. Kampmann

The paper uses CRISPR screens in iPSC-derived neurons to identify factors controlling tau aggregation, finding new pathways and potential therapeutic targets for tauopathies.

bioRxiv · Jun 16, 2023Cell Biology

SIRT5 is a proviral factor that interacts with SARS-CoV-2 Nsp14 protein

M. Walter, I. P. Chen, A. Vallejo-Gracia, I.-J. Kim, O. Bielska, V. L. Lam, J. M. Hayashi, A. Cruz, S. Shah, J. D. Gross, N. J. Krogan, B. Schilling, M. Ott, E. Verdin

This study identifies SIRT5 as a proviral factor that interacts with SARS-CoV-2 Nsp14, enhancing viral replication and suggesting it as a therapeutic target.

bioRxiv · Jan 4, 2022Microbiology

CryoEM and AI reveal a structure of SARS-CoV-2 Nsp2, a multifunctional protein involved in key host processes.

M. Gupta, C. M. Azumaya, M. Moritz, S. Pourmal, A. Diallo, G. E. Merz, G. M. Jang, M. Bouhaddou, A. Fossati, A. F. Brilot, D. Diwanji, E. Hernandez, N. Herrera, H. T. Kratochvil, V. L. Lam, , K. I Pawar

The paper uses cryo-EM and AlphaFold2 to determine the structure of SARS-CoV-2 Nsp2, revealing its zinc-binding site and potential interactions with host proteins.

bioRxiv · May 10, 2021 · PreprintBiophysics