Author

C. Stoneham

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· 3 Microbiology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Organism:human· 5 Research Focus:host-pathogen & immune response· 3 Research Focus:protein folding & dynamics· 2 Assay:proteomics· 2 Assay:structural biology· 2 Research Focus:protein structure prediction· 1

Frequent Co-Authors

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

Activity by Year

2018-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

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5 shared papersBiochemistry

J. Guatelli

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Author profile →

5 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

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

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