Year |
Citation |
Score |
2024 |
Xu XP, Cao W, Swift MF, Pandit NG, Huehn AE, Sindelar CV, De La Cruz EM, Hanein D, Volkmann N. High-resolution yeast actin structures indicate the molecular mechanism of actin filament stiffening by cations. Communications Chemistry. 7: 164. PMID 39079963 DOI: 10.1038/s42004-024-01243-x |
0.581 |
|
2024 |
Chavali SS, Chou SZ, Cao W, Pollard TD, De La Cruz EM, Sindelar CV. Publisher Correction: Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex. Nature Communications. 15: 2354. PMID 38491023 DOI: 10.1038/s41467-024-46804-9 |
0.545 |
|
2024 |
Chavali SS, Chou SZ, Cao W, Pollard TD, De La Cruz EM, Sindelar CV. Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex. Nature Communications. 15: 2059. PMID 38448439 DOI: 10.1038/s41467-024-46179-x |
0.553 |
|
2024 |
Singh SK, Siegler N, Pandey H, Yanir N, Popov M, Goldstein-Levitin A, Sadan M, Debs G, Zarivach R, Frank GA, Kass I, Sindelar CV, Zalk R, Gheber L. Noncanonical interaction with microtubules via the N-terminal nonmotor domain is critical for the functions of a bidirectional kinesin. Science Advances. 10: eadi1367. PMID 38324691 DOI: 10.1126/sciadv.adi1367 |
0.313 |
|
2023 |
Bibeau JP, Pandit NG, Gray S, Shatery Nejad N, Sindelar CV, Cao W, De La Cruz EM. Twist response of actin filaments. Proceedings of the National Academy of Sciences of the United States of America. 120: e2208536120. PMID 36656858 DOI: 10.1073/pnas.2208536120 |
0.447 |
|
2022 |
Grushin K, Kalyana Sundaram RV, Sindelar CV, Rothman JE. 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. PMID 35135883 DOI: 10.1073/pnas.2121259119 |
0.437 |
|
2021 |
Hocky GM, Sindelar CV, Cao W, Voth GA, De La Cruz EM. Structural basis of fast- and slow-severing actin-cofilactin boundaries. The Journal of Biological Chemistry. 100337. PMID 33508320 DOI: 10.1016/j.jbc.2021.100337 |
0.393 |
|
2020 |
Debs GE, Cha M, Liu X, Huehn AR, Sindelar CV. 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. PMID 32636254 DOI: 10.1073/pnas.2001546117 |
0.432 |
|
2020 |
Gibson KH, Trajtenberg F, Wunder EA, Brady MR, San Martin F, Mechaly A, Shang Z, Liu J, Picardeau M, Ko A, Buschiazzo A, Sindelar CV. An asymmetric sheath controls flagellar supercoiling and motility in the leptospira spirochete. Elife. 9. PMID 32157997 DOI: 10.7554/eLife.53672 |
0.365 |
|
2020 |
Huehn AR, Bibeau JP, Schramm AC, Cao W, De La Cruz EM, Sindelar CV. 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. PMID 31900364 DOI: 10.1073/pnas.1915987117 |
0.53 |
|
2018 |
Iwamoto DV, Huehn A, Simon B, Huet-Calderwood C, Baldassarre M, Sindelar CV, Calderwood DA. Structural basis of the filamin A actin-binding domain interaction with F-actin. Nature Structural & Molecular Biology. PMID 30224736 DOI: 10.1038/S41594-018-0128-3 |
0.428 |
|
2018 |
Wunder EA, Slamti L, Suwondo DN, Gibson KH, Shang Z, Sindelar CV, Trajtenberg F, Buschiazzo A, Ko AI, Picardeau M. FcpB Is a Surface Filament Protein of the Endoflagellum Required for the Motility of the Spirochete . Frontiers in Cellular and Infection Microbiology. 8: 130. PMID 29868490 DOI: 10.3389/fcimb.2018.00130 |
0.337 |
|
2018 |
Huehn A, Cao W, Elam WA, Liu X, De La Cruz EM, Sindelar CV. The actin filament twist changes abruptly at boundaries between bare and cofilin-decorated segments. The Journal of Biological Chemistry. PMID 29463680 DOI: 10.1074/jbc.AC118.001843 |
0.477 |
|
2018 |
Mentes A, Huehn A, Liu X, Zwolak A, Dominguez R, Shuman H, Ostap EM, Sindelar CV. High-resolution cryo-EM structures of actin-bound myosin states reveal the mechanism of myosin force sensing. Proceedings of the National Academy of Sciences of the United States of America. PMID 29358376 DOI: 10.1016/J.Bpj.2017.11.1796 |
0.596 |
|
2017 |
Elam WA, Cao W, Kang H, Huehn A, Hocky GM, Prochniewicz E, Schramm AC, Negrón K, Garcia J, Bonello TT, Gunning PW, Thomas DD, Voth GA, Sindelar CV, De La Cruz EM. Phosphomimetic S3D-Cofilin Binds But Only Weakly Severs Actin Filaments. The Journal of Biological Chemistry. PMID 28939776 DOI: 10.1074/Jbc.M117.808378 |
0.482 |
|
2017 |
Bell KM, Cha HK, Sindelar CV, Cochran JC. The yeast kinesin-5 Cin8 interacts with the microtubule in a noncanonical manner. The Journal of Biological Chemistry. PMID 28701465 DOI: 10.1074/jbc.M117.797662 |
0.334 |
|
2017 |
Liu D, Liu X, Shang Z, Sindelar CV. Structural basis of cooperativity in kinesin revealed by 3D reconstruction of a two-head-bound state on microtubules. Elife. 6. PMID 28504639 DOI: 10.7554/eLife.24490 |
0.485 |
|
2016 |
Ropars V, Yang Z, Isabet T, Blanc F, Zhou K, Lin T, Liu X, Hissier P, Samazan F, Amigues B, Yang ED, Park H, Pylypenko O, Cecchini M, Sindelar CV, et al. The myosin X motor is optimized for movement on actin bundles. Nature Communications. 7: 12456. PMID 27580874 DOI: 10.1038/Ncomms12456 |
0.465 |
|
2014 |
Kang H, Bradley MJ, Cao W, Zhou K, Grintsevich EE, Michelot A, Sindelar CV, Hochstrasser M, De La Cruz EM. Site-specific cation release drives actin filament severing by vertebrate cofilin. Proceedings of the National Academy of Sciences of the United States of America. 111: 17821-6. PMID 25468977 DOI: 10.1073/Pnas.1413397111 |
0.55 |
|
2014 |
Shang Z, Zhou K, Xu C, Csencsits R, Cochran JC, Sindelar CV. High-resolution structures of kinesin on microtubules provide a basis for nucleotide-gated force-generation. Elife. 3: e04686. PMID 25415053 DOI: 10.7554/Elife.04686 |
0.476 |
|
2014 |
Shuman H, Greenberg MJ, Zwolak A, Lin T, Sindelar CV, Dominguez R, Ostap EM. A vertebrate myosin-I structure reveals unique insights into myosin mechanochemical tuning. Proceedings of the National Academy of Sciences of the United States of America. 111: 2116-21. PMID 24469830 DOI: 10.1073/Pnas.1321022111 |
0.346 |
|
2012 |
Goulet A, Behnke-Parks WM, Sindelar CV, Major J, Rosenfeld SS, Moores CA. The structural basis of force generation by the mitotic motor kinesin-5. The Journal of Biological Chemistry. 287: 44654-66. PMID 23135273 DOI: 10.1016/J.Bpj.2012.11.2129 |
0.376 |
|
2012 |
Shen QT, Hsiue PP, Sindelar CV, Welch MD, Campellone KG, Wang HW. Structural insights into WHAMM-mediated cytoskeletal coordination during membrane remodeling. The Journal of Cell Biology. 199: 111-24. PMID 23027905 DOI: 10.1083/Jcb.201204010 |
0.438 |
|
2010 |
Fourniol FJ, Sindelar CV, Amigues B, Clare DK, Thomas G, Perderiset M, Francis F, Houdusse A, Moores CA. Template-free 13-protofilament microtubule-MAP assembly visualized at 8 A resolution. The Journal of Cell Biology. 191: 463-70. PMID 20974813 DOI: 10.1083/Jcb.201007081 |
0.392 |
|
2010 |
Sindelar CV, Downing KH. An atomic-level mechanism for activation of the kinesin molecular motors. Proceedings of the National Academy of Sciences of the United States of America. 107: 4111-6. PMID 20160108 DOI: 10.1073/pnas.0911208107 |
0.357 |
|
2009 |
Cochran JC, Sindelar CV, Mulko NK, Collins KA, Kong SE, Hawley RS, Kull FJ. ATPase cycle of the nonmotile kinesin NOD allows microtubule end tracking and drives chromosome movement. Cell. 136: 110-22. PMID 19135893 DOI: 10.1016/J.Cell.2008.11.048 |
0.632 |
|
2008 |
Dietrich KA, Sindelar CV, Brewer PD, Downing KH, Cremo CR, Rice SE. The kinesin-1 motor protein is regulated by a direct interaction of its head and tail. Proceedings of the National Academy of Sciences of the United States of America. 105: 8938-43. PMID 18579780 DOI: 10.1073/Pnas.0803575105 |
0.391 |
|
2007 |
Sindelar CV, Downing KH. The beginning of kinesin's force-generating cycle visualized at 9-A resolution. The Journal of Cell Biology. 177: 377-85. PMID 17470637 DOI: 10.1083/Jcb.200612090 |
0.401 |
|
2002 |
Sindelar CV, Budny MJ, Rice S, Naber N, Fletterick R, Cooke R. Two conformations in the human kinesin power stroke defined by X-ray crystallography and EPR spectroscopy. Nature Structural Biology. 9: 844-8. PMID 12368902 DOI: 10.1038/Nsb852 |
0.592 |
|
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