Author

C. A. Escobar

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· 3 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:protein folding & dynamics· 2 Research Focus:cell signaling & trafficking· 1 Organism:human· 1 Assay:protein structure· 1

Frequent Co-Authors

H.-X. Zhou· 3 shared T. A. Cross· 3 shared A. Hicks· 2 shared B. Barbat· 1 shared B. Douzi· 1 shared G. Ball· 1 shared K. T. Forest· 1 shared L. Quinton· 1 shared

Activity by Year

2020-2022 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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3 shared papersBiophysics

H.-X. Zhou

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Author profile →

4 papers

Recent·Most cited

An Arg/Ala-Rich Helix in the N-Terminal Region of M. tuberculosis FtsQ Anchors FtsZ to Membranes

S. T. Smrt, C. A. Escobar, S. Dey, T. A. Cross, H.-X. Zhou

This paper identifies an Arg/Ala-rich helix in M. tuberculosis FtsQ that anchors FtsZ to membranes, influencing Z-ring formation and curvature.

bioRxiv · Sep 2, 2022 · PreprintBiophysics

Multidisciplinary Interrogation of a Crucial Protein Interface in the Type II Secretion System

C. A. Escobar, B. Douzi, G. Ball, B. Barbat, S. Alphonse, L. Quinton, R. Vouhoux, K. T. Forest

The paper determines the structural role of XcpH in the T2SS by showing it bridges XcpIJK and XcpG, revealing its adapter function through unwinding of its N-terminal helix.

bioRxiv · Dec 11, 2020 · PreprintMicrobiology

Extreme Fuzzy Association of an Intrinsically Disordered Protein with Acidic Membranes

A. Hicks, C. A. Escobar, T. A. Cross, H.-X. Zhou

The paper characterizes the extreme fuzzy membrane association of the disordered N-terminal region of ChiZ using NMR and simulations, revealing sequence-interaction dynamics.

bioRxiv · Sep 16, 2020Biophysics

Sequence-dependent correlated segments in the intrinsically disordered region of ChiZ

A. Hicks, C. A. Escobar, T. A. Cross, H.-X. Zhou

The paper characterizes the conformational dynamics of an intrinsically disordered protein using NMR, SAXS, and MD simulations, identifying sequence-dependent correlated segments.

bioRxiv · Apr 22, 2020Biophysics