Author

N. Herrera

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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Microbiology· 2 Biochemistry· 1 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:protein structure prediction· 2 Assay:proteomics· 2 Approach:statistical model· 2 Organism:virus· 2 Research Focus:cell-cell communication· 1 Assay:cryo-EM· 1 Approach:deep learning· 1

Frequent Co-Authors

A. Sil· 2 shared G. E. Merz· 2 shared H. T. Kratochvil· 2 shared I. D. Young· 2 shared J. K. Peters· 2 shared M. Moritz· 2 shared M. Voorhies· 2 shared T. W. Owens· 2 shared

Activity by Year

2020-2021 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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2 shared papersMicrobiology

A. Sil

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

The ESX-1 secretion system senses bacterial contact and prepares mycobacteria for environmental adaptation

N. Herrera, P. D. Odermatt, M. Voorhies, R. Nakagawa, A. Sil, F. Chang, O. S. Rosenberg

The paper shows the ESX-1 system in mycobacteria senses bacterial contact and environmental nitrogen levels, regulating secretion and adaptation.

bioRxiv · Oct 17, 2021 · PreprintMicrobiology

Cbp1, a rapidly evolving fungal virulence factor, forms an effector complex that drives macrophage lysis

D. Azimova, N. Herrera, L. Duvenage, M. Voorhies, B. C. English, J. C. Hoving, R. Oren, A. Sil

This paper identifies Cbp1 as a rapidly evolving fungal virulence factor that localizes to the host cell cytosol and forms a complex to drive macrophage lysis.

bioRxiv · Sep 16, 2021 · PreprintMicrobiology

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

Fragment binding to the Nsp3 macrodomain of SARS-CoV-2 identified through crystallographic screening and computational docking

M. Schuller, G. J. Correy, S. Gahbauer, D. Fearon, T. Wu, R. E. Diaz, I. D. Young, L. Carvalho Martins, D. H. Smith, U. Schulze-Gahmen, T. W. Owens, I. Deshpande, G. E. Merz, A. C. Thwin, J. T. Biel, , Smi

The paper identifies new chemical fragments binding to the SARS-CoV-2 Nsp3 macrodomain through crystallographic screening and computational docking, validating their binding with biophysical techniques.

bioRxiv · Nov 24, 2020Biochemistry