Year |
Citation |
Score |
2023 |
Ali BA, Judy RM, Chowdhury S, Jacobsen NK, Castanzo DT, Carr KL, Richardson CD, Lander GC, Martin A, Gardner BM. The N1 domain of the peroxisomal AAA-ATPase Pex6 is required for Pex15 binding and proper assembly with Pex1. The Journal of Biological Chemistry. 105504. PMID 38036174 DOI: 10.1016/j.jbc.2023.105504 |
0.614 |
|
2023 |
Ali BA, Judy RM, Chowdhury S, Jacobsen NK, Castanzo DT, Carr KL, Richardson CD, Lander GC, Martin A, Gardner BM. The Pex6 N1 domain is required for Pex15 binding and proper assembly with Pex1. Biorxiv : the Preprint Server For Biology. PMID 37745580 DOI: 10.1101/2023.09.15.557798 |
0.612 |
|
2022 |
Yang S, Tang Y, Liu Y, Brown AJ, Schaks M, Ding B, Kramer DA, Mietkowska M, Ding L, Alekhina O, Billadeau DD, Chowdhury S, Wang J, Rottner K, Chen B. Arf GTPase activates the WAVE regulatory complex through a distinct binding site. Science Advances. 8: eadd1412. PMID 36516255 DOI: 10.1126/sciadv.add1412 |
0.787 |
|
2022 |
Ding B, Yang S, Schaks M, Liu Y, Brown AJ, Rottner K, Chowdhury S, Chen B. Structures reveal a key mechanism of WAVE regulatory complex activation by Rac1 GTPase. Nature Communications. 13: 5444. PMID 36114192 DOI: 10.1038/s41467-022-33174-3 |
0.802 |
|
2022 |
Ding B, Narvaez-Ortiz HY, Singh Y, Hocky GM, Chowdhury S, Nolen BJ. Structure of Arp2/3 complex at a branched actin filament junction resolved by single-particle cryo-electron microscopy. Proceedings of the National Academy of Sciences of the United States of America. 119: e2202723119. PMID 35622886 DOI: 10.1073/pnas.2202723119 |
0.804 |
|
2021 |
Anzelon TA, Chowdhury S, Hughes SM, Xiao Y, Lander GC, MacRae IJ. Structural basis for piRNA targeting. Nature. PMID 34471284 DOI: 10.1038/s41586-021-03856-x |
0.569 |
|
2020 |
Basanta B, Chowdhury S, Lander GC, Grotjahn DA. A guided approach for subtomogram averaging of challenging macromolecular assemblies. Journal of Structural Biology: X. 4: 100041. PMID 33319208 DOI: 10.1016/j.yjsbx.2020.100041 |
0.552 |
|
2020 |
Shaaban M, Chowdhury S, Nolen BJ. Cryo-EM reveals the transition of Arp2/3 complex from inactive to nucleation-competent state. Nature Structural & Molecular Biology. PMID 32839613 DOI: 10.1038/S41594-020-0481-X |
0.758 |
|
2020 |
Chowdhury S, Shaaban MH, Nolen B. Cryo-EM Reveals Actin Filament Nucleation by Activated Arp2/3 Complex Biophysical Journal. 118. DOI: 10.1016/J.Bpj.2019.11.1667 |
0.55 |
|
2019 |
Rollins MF, Chowdhury S, Carter J, Golden SM, Miettinen HM, Santiago-Frangos A, Faith D, Lawrence CM, Lander GC, Wiedenheft B. Structure Reveals a Mechanism of CRISPR-RNA-Guided Nuclease Recruitment and Anti-CRISPR Viral Mimicry. Molecular Cell. PMID 30872121 DOI: 10.1016/J.Molcel.2019.02.001 |
0.691 |
|
2018 |
Otomo T, Chowdhury S, Lander GC. The rod-shaped ATG2A-WIPI4 complex tethers membranes in vitro. Contact (Thousand Oaks (Ventura County, Calif.)). 1. PMID 30766969 DOI: 10.1177/2515256418819936 |
0.611 |
|
2018 |
Chowdhury S, Otomo C, Leitner A, Ohashi K, Aebersold R, Lander GC, Otomo T. Insights into autophagosome biogenesis from structural and biochemical analyses of the ATG2A-WIPI4 complex. Proceedings of the National Academy of Sciences of the United States of America. PMID 30185561 DOI: 10.1073/Pnas.1811874115 |
0.664 |
|
2018 |
Grotjahn DA, Chowdhury S, Xu Y, McKenney RJ, Schroer TA, Lander GC. Author Correction: Cryo-electron tomography reveals that dynactin recruits a team of dyneins for processive motility. Nature Structural & Molecular Biology. PMID 29476122 DOI: 10.1038/S41594-018-0043-7 |
0.58 |
|
2018 |
Grotjahn DA, Chowdhury S, Xu Y, McKenney RJ, Schroer TA, Lander GC. Cryo-electron tomography reveals that dynactin recruits a team of dyneins for processive motility. Nature Structural & Molecular Biology. PMID 29416113 DOI: 10.1038/S41594-018-0027-7 |
0.718 |
|
2018 |
Gardner BM, Castanzo DT, Chowdhury S, Stjepanovic G, Stefely MS, Hurley JH, Lander GC, Martin A. The peroxisomal AAA-ATPase Pex1/Pex6 unfolds substrates by processive threading. Nature Communications. 9: 135. PMID 29321502 DOI: 10.1038/S41467-017-02474-4 |
0.685 |
|
2017 |
Chen KC, Qu S, Chowdhury S, Noxon IC, Schonhoft JD, Plate L, Powers ET, Kelly JW, Lander GC, Wiseman RL. The endoplasmic reticulum HSP40 co-chaperone ERdj3/DNAJB11 assembles and functions as a tetramer. The Embo Journal. PMID 28655754 DOI: 10.15252/Embj.201695616 |
0.657 |
|
2017 |
Rollins MF, Chowdhury S, Carter J, Golden SM, Wilkinson RA, Bondy-Denomy J, Lander GC, Wiedenheft B. Cas1 and the Csy complex are opposing regulators of Cas2/3 nuclease activity. Proceedings of the National Academy of Sciences of the United States of America. PMID 28438998 DOI: 10.1073/Pnas.1616395114 |
0.708 |
|
2017 |
Chowdhury S, Carter J, Rollins MF, Golden SM, Jackson RN, Hoffmann C, Nosaka L, Bondy-Denomy J, Maxwell KL, Davidson AR, Fischer ER, Lander GC, Wiedenheft B. Structure Reveals Mechanisms of Viral Suppressors that Intercept a CRISPR RNA-Guided Surveillance Complex. Cell. 169: 47-57.e11. PMID 28340349 DOI: 10.1016/J.Cell.2017.03.012 |
0.677 |
|
2017 |
Chowdhury S, Rollins MF, Carter J, Jackson R, Nosaka L, Wiedenheft B, Lander GC. Using Cryoem to Understand How Phages Evade Bacterial CRISPR Defense System Biophysical Journal. 112: 334a-335a. DOI: 10.1016/J.Bpj.2016.11.1811 |
0.673 |
|
2017 |
Grotjahn D, Chowdhury S, Xu Y, Lander G. Three-Dimensional Snapshots of the Microtubule-Bound Dynein-Dynactin Complex Biophysical Journal. 112. DOI: 10.1016/J.Bpj.2016.11.1417 |
0.671 |
|
2015 |
Chowdhury S, Ketcham SA, Schroer TA, Lander GC. Structural organization of the dynein-dynactin complex bound to microtubules. Nature Structural & Molecular Biology. 22: 345-7. PMID 25751425 DOI: 10.1038/Nsmb.2996 |
0.674 |
|
2015 |
Gardner BM, Chowdhury S, Lander GC, Martin A. The Pex1/Pex6 complex is a heterohexameric AAA+ motor with alternating and highly coordinated subunits. Journal of Molecular Biology. 427: 1375-88. PMID 25659908 DOI: 10.1016/J.Jmb.2015.01.019 |
0.714 |
|
2015 |
Chowdhury S, Ketcham SA, Schroer TA, Lander GC. Ultrastructure of Dynactin Complex: A Mediator of Cytoplasmic Dynein Biophysical Journal. 108: 22a. DOI: 10.1016/J.Bpj.2014.11.142 |
0.725 |
|
2014 |
Sysoeva TA, Chowdhury S, Nixon BT. Breaking symmetry in multimeric ATPase motors. Cell Cycle (Georgetown, Tex.). 13: 1509-10. PMID 24755939 DOI: 10.4161/Cc.28957 |
0.825 |
|
2013 |
Sysoeva TA, Chowdhury S, Guo L, Nixon BT. Nucleotide-induced asymmetry within ATPase activator ring drives σ54-RNAP interaction and ATP hydrolysis. Genes & Development. 27: 2500-11. PMID 24240239 DOI: 10.1101/Gad.229385.113 |
0.813 |
|
2012 |
Chakraborty A, Wang D, Ebright YW, Korlann Y, Kortkhonjia E, Kim T, Chowdhury S, Wigneshweraraj S, Irschik H, Jansen R, Nixon BT, Knight J, Weiss S, Ebright RH. Opening and closing of the bacterial RNA polymerase clamp. Science (New York, N.Y.). 337: 591-5. PMID 22859489 DOI: 10.1126/Science.1218716 |
0.716 |
|
2011 |
Nixon BT, Sysoeva TA, Chen B, Chowdhury S, Guo L, De Carlo S, Hanson J, Yang H. AAA+ ATPase Mechanism Biophysical Journal. 100: 38a. DOI: 10.1016/J.Bpj.2010.12.412 |
0.796 |
|
2010 |
Chen B, Sysoeva TA, Chowdhury S, Guo L, De Carlo S, Hanson JA, Yang H, Nixon BT. Engagement of arginine finger to ATP triggers large conformational changes in NtrC1 AAA+ ATPase for remodeling bacterial RNA polymerase. Structure (London, England : 1993). 18: 1420-30. PMID 21070941 DOI: 10.1016/J.Str.2010.08.018 |
0.796 |
|
2009 |
Chen B, Sysoeva TA, Chowdhury S, Guo L, Nixon BT. ADPase activity of recombinantly expressed thermotolerant ATPases may be caused by copurification of adenylate kinase of Escherichia coli. The Febs Journal. 276: 807-15. PMID 19143839 DOI: 10.1111/J.1742-4658.2008.06825.X |
0.769 |
|
2008 |
Chen B, Sysoeva TA, Chowdhury S, Nixon BT. Regulation and action of the bacterial enhancer-binding protein AAA+ domains. Biochemical Society Transactions. 36: 89-93. PMID 18208392 DOI: 10.1042/Bst0360089 |
0.792 |
|
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