Peer-reviewedLicence not statedCell chemical biology
Curved adhesions resist disruption by high-affinity αv integrin inhibitors
4 affiliations
- 1Biophysics Program, Stanford University School of Medicine, Stanford, CA, 94305, USA
- 2Wu-Tsai Neuroscience Institute and ChEM-H Institute, Stanford University, Stanford, CA, 94305, USA
- 3Department of Chemistry, Stanford University, Stanford, CA, 94305, USA
- 4Lead contact
Related
- Engineering Stapled Peptide Inhibitors Reveals Design Principles for Targeting Talin-Induced Integrin Activation
- Peripheral lysosomes recruit PLEKHG3 to focal adhesions and restrain protrusion dynamics
- DAAM1 formin and Ena/VASP proteins assemble functionally distinct actin filaments for focal adhesions
- VASP cooperates with zyxin to organize mechanically competent adhesions
- Tall adhesions overcome cell surface steric interference and rescue antibody-dependent phagocytosis in macrophages.
BibTeX
@article{lee2026curved,
title = {{Curved adhesions resist disruption by high-affinity αv integrin inhibitors}},
author = {Christina E. Lee and Judith Martinez and Anna Amine and Wei Zhang and Chih-Hao Lu and Xingyuan Zhang and He You and Ching-Ting Tsai and Melissa L. Nakamoto and Bianxiao Cui},
journal = {Cell chemical biology},
year = {2026},
month = sep,
doi = {10.1016/j.chembiol.2026.08.017},
url = {https://doi.org/10.1016/j.chembiol.2026.08.017},
}
RIS
TY - JOUR
TI - Curved adhesions resist disruption by high-affinity αv integrin inhibitors
AU - Christina E. Lee
AU - Judith Martinez
AU - Anna Amine
AU - Wei Zhang
AU - Chih-Hao Lu
AU - Xingyuan Zhang
AU - He You
AU - Ching-Ting Tsai
AU - Melissa L. Nakamoto
AU - Bianxiao Cui
PY - 2026
DA - 2026/09/28
JO - Cell chemical biology
DO - 10.1016/j.chembiol.2026.08.017
UR - https://doi.org/10.1016/j.chembiol.2026.08.017
SN - 2451-9456
SN - 2451-9448
ER -