Charles V. Sindelar
Affiliations: | Molecular Biophysics and Biochemistry | Yale University, New Haven, CT |
Area:
Structural BiologyWebsite:
http://medicine.yale.edu/mbb/faculty/charles_sindelar.profileGoogle:
"Charles V. Sindelar"Mean distance: 8.41 | S | N | B | C | P |
Parents
Sign in to add mentorRobert J. Fletterick | grad student | 2002 | UCSF | |
(New conformations in the force-delivering element of a walking molecular motor and a computable analytic expression for the partition function of the first solvation shell.) |
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Publications
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Chavali SS, Chou SZ, Cao W, et al. (2024) Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex. Nature Communications. 15: 2059 |
Singh SK, Siegler N, Pandey H, et al. (2024) Noncanonical interaction with microtubules via the N-terminal nonmotor domain is critical for the functions of a bidirectional kinesin. Science Advances. 10: eadi1367 |
Grushin K, Kalyana Sundaram RV, Sindelar CV, et al. (2022) Munc13 structural transitions and oligomers that may choreograph successive stages in vesicle priming for neurotransmitter release. Proceedings of the National Academy of Sciences of the United States of America. 119 |
Hocky GM, Sindelar CV, Cao W, et al. (2021) Structural basis of fast- and slow-severing actin-cofilactin boundaries. The Journal of Biological Chemistry. 100337 |
Debs GE, Cha M, Liu X, et al. (2020) Dynamic and asymmetric fluctuations in the microtubule wall captured by high-resolution cryoelectron microscopy. Proceedings of the National Academy of Sciences of the United States of America |
Gibson KH, Trajtenberg F, Wunder EA, et al. (2020) An asymmetric sheath controls flagellar supercoiling and motility in the leptospira spirochete. Elife. 9 |
Bodrug T, Wilson-Kubalek EM, Nithianantham S, et al. (2020) The kinesin-5 tail domain directly modulates the mechanochemical cycle of the motor domain for anti-parallel microtubule sliding. Elife. 9 |
Huehn AR, Bibeau JP, Schramm AC, et al. (2020) Structures of cofilin-induced structural changes reveal local and asymmetric perturbations of actin filaments. Proceedings of the National Academy of Sciences of the United States of America |
Iwamoto DV, Huehn A, Simon B, et al. (2018) Structural basis of the filamin A actin-binding domain interaction with F-actin. Nature Structural & Molecular Biology |
Huehn A, Cao W, Elam WA, et al. (2018) The actin filament twist changes abruptly at boundaries between bare and cofilin-decorated segments. The Journal of Biological Chemistry |