Author

J. Guatelli

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· 4 Biochemistry· 3 Cell Biology· 1

Signature Assays, Organisms & Methods

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Organism:human· 8 Approach:experimental assay· 7 Research Focus:host-pathogen & immune response· 4 Assay:proteomics· 4 Research Focus:cell type annotation· 3 Research Focus:differential expression· 2 Research Focus:protein folding & dynamics· 2 Assay:structural biology· 2

Frequent Co-Authors

C. Stoneham· 5 shared A. L. Oom· 3 shared M. Suarez· 3 shared P. W. Ramirez· 3 shared R. Singh· 3 shared X. Jia· 3 shared C. A. Stoneham· 2 shared C. Lim· 2 shared

Activity by Year

2018-2021 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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5 shared papersBiochemistry

C. Stoneham

Mutual co-authors in cluster

Author profile →

8 papers

Recent·Most cited

Interactions of SARS-CoV-2 envelope protein with amilorides correlate with antiviral activity

S. H. Park, H. Siddiqi, D. Castro, A. De Angelis, A. L. Oom, C. Stoneham, M. Lewinski, A. Clark, B. Croker, A. Carlin, J. Guatelli, S. J. Opella

This study investigates the structure of SARS-CoV-2 E protein and its interactions with amilorides, finding that binding affinity correlates with antiviral activity and that residue Asn15 is critical for maintaining the binding site conformation.

bioRxiv · Apr 6, 2021Biochemistry

Comparative Analysis of T Cell Spatial Proteomics and the Influence of HIV Expression

A. L. Oom, C. A. Stoneham, M. K. Lewinski, A. Richards, J. Wozniak, K. Shams-Ud-Doha, D. Gonzalez, N. J. Krogan, J. Guatelli

The paper compares machine learning methods for spatial proteome classification in HIV-expressing T cells and identifies Nef-dependent interactors.

bioRxiv · Mar 17, 2021Cell Biology

A combined EM and proteomic analysis places HIV-1 Vpu at the crossroads of retromer and ESCRT complexes: PTPN23 is a Vpu-cofactor

C. A. Stoneham, S. Langer, P. De Jesus, J. Wozniak, J. Lapek, T. Deerinck, A. Thor, L. Pache, S. Chanda, D. Gonzalez, M. Ellisman, J. Guatelli

This paper identifies PTPN23 as a Vpu-cofactor and maps Vpu's interactions with retromer and ESCRT complexes using EM and proteomics.

bioRxiv · Feb 22, 2021Microbiology

Functional Landscape of SARS-CoV-2 Cellular Restriction

L. Martin-Sancho, M. K. Lewinski, L. Pache, C. Stoneham, X. YIN, D. Pratt, C. Churas, S. B. Rosenthal, S. Liu, P. D. De Jesus, A. M. O'Neill, A. P. Gounder, C. Nguyen, Y. Pu, A. L. Oom, , S. Chanda

This study identifies key interferon stimulated genes (ISGs) that restrict SARS-CoV-2 infection by inhibiting viral entry, RNA synthesis, and release.

bioRxiv · Sep 29, 2020Microbiology

Nef enhances HIV-1 replication and infectivity independently of SERINC3 and SERINC5 in CEM T cells

P. W. Ramirez, T. Vollbrecht, F. M. Acosta, M. Suarez, A. A. Angerstein, J. Wallace, R. M. O'Connell, J. Guatelli

This study shows that HIV-1 Nef enhances replication and infectivity in CEM T cells without relying on SERINC3 or SERINC5 antagonism.

bioRxiv · Jul 15, 2020Microbiology

Structural Basis of CD4 Downregulation by HIV-1 Nef

Y. Kwon, R. Kaake, I. Echeverria, M. Suarez, C. Stoneham, P. W. Ramirez, J. Kress, R. Singh, A. Sali, N. J. Krogan, J. Guatelli, X. Jia

This paper presents a high-resolution crystal structure of HIV-1 Nef interacting with AP2, revealing how Nef sequesters CD4 for degradation and identifying a dual-function pocket crucial for both MHC recruitment and CD4 binding.

bioRxiv · Apr 21, 2020Biochemistry

A conserved acidic cluster motif in SERINC5 confers resistance to antagonism by HIV-1 Nef

C. Stoneham, P. W. Ramirez, R. Singh, M. Suarez, A. Debray, C. Lim, X. Jia, Y. Xiong, J. Guatelli

This paper identifies an acidic cluster motif in SERINC5 that mediates resistance to HIV-1 Nef antagonism, showing its importance in Nef sensitivity without affecting intrinsic antiviral activity.

bioRxiv · Mar 27, 2019Microbiology

Phosphoserine acidic cluster motifs in the cytoplasmic domains of transmembrane proteins bind distinct basic regions on the μ subunits of clathrin adaptor protein complexes

R. Singh, C. Stoneham, C. Lim, X. jia, J. Guenaga, R. Wyatt, J. o. Wertheim, Y. Xiong, J. Guatelli

The paper identifies that phosphoserine acidic cluster motifs in transmembrane proteins bind distinct basic regions on clathrin adaptor protein μ subunits, revealing potential for virus-specific inhibition.

bioRxiv · Mar 21, 2018Biochemistry