Author

F. Khalili-Araghi

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· 2 Pathology· 1 Physiology· 1

Signature Assays, Organisms & Methods

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Approach:mechanistic / dynamical model· 3 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Assay:protein structure· 2 Assay:bulk RNA-seq· 1 Research Focus:cell type annotation· 1 Research Focus:cell-cell communication· 1 Research Focus:chromatin & epigenetic regulation· 1

Frequent Co-Authors

L. Shen· 3 shared S. Fuladi· 3 shared S. McGuinness· 3 shared C. R. Weber· 2 shared M. Sidahmed· 2 shared Y. Li· 2 shared A. Holder· 1 shared C. Weber· 1 shared

Activity by Year

2021-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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3 shared papersPathology

L. Shen

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Inflammation-Induced Claudin-2 Upregulation Limits Pancreatitis Progression by Enhancing Tight Junction-Controlled Pancreatic Ductal Transport

S. Kesaraju, Y. Li, J. Xing, M. Tracy, K. Wannemo, A. Holder, P. Zhao, M. A. Khan, J. Kainov, N. Rana, M. Sidahmed, S. Hyoju, L. Smith, J. Matthews, S. Tay, , C. Weber

This study shows CLDN2 upregulation during pancreatitis limits disease progression by enhancing tight junction-controlled fluid transport in pancreatic ductal epithelium.

bioRxiv · Sep 1, 2023 · PreprintPathology

Molecular dynamics analyses of CLDN15 pore size and charge selectivity

S. McGuinness, P. Li, Y. Li, S. Fuladi, S. Konar, S. S. Bafghi, M. Sidahmed, Y. Li, L. Shen, F. Khalili-Araghi, C. R. Weber

The paper uses molecular dynamics simulations and cell culture experiments to study how the D55 residue in CLDN15 affects ion size and charge selectivity in tight junctions.

bioRxiv · Aug 16, 2023Physiology

Role of TM3 in claudin-15 strand flexibility: a molecular dynamics study

S. Fuladi, S. McGuinness, F. Khalili-Araghi

This study uses molecular dynamics to show that the A134P mutation in claudin-15 TM3 increases strand persistence length by reducing lateral flexibility without altering intermolecular contacts.

bioRxiv · Jun 8, 2022Biophysics

Molecular mechanism of claudin-15 strand flexibility

S. Fuladi, S. McGuinness, L. Shen, C. R. Weber, F. Khalili-Araghi

This study uses molecular dynamics simulations to investigate the flexibility of claudin-15 strands and identifies interfacial interaction networks as the source of their lateral flexibility.

bioRxiv · Dec 7, 2021Biophysics