LBMS Publications

Publications are an important way to disseminate the breadth and depth of research performed at the Laboratory for BioMolecular Structure (LBMS). The LBMS Publications Database is the official source for listing all journal articles, conference proceedings, dissertations, books, technical reports, patents, and any other published work that used LBMS and/or LBMS resources. Users are expected to report their publications to the facility and this information is carefully considered during the proposal review process.

Facility Acknowledgement

All users are obligated to inform the Brookhaven National Laboratory of their publications or Ph.D. thesis based on research carried out, in whole or in part, at LBMS.

Use the following acknowledgment when referencing work done at LBMS.

If you have a question about the publications database, or need assistance with a database related matter, please email lbmsuser@bnl.gov.

Publications

*High-impact papers are published in journals with an impact factor greater than 7. Citation counts are provided by Web of Science.

High ImpactSwapnil C Devarkar, Christina R Budding, Chathuri Pathirage, Arundhati Kavoor, Cassandra Herbert, Patrick A Limbach, Karin Musier-Forsyth, Yong Xiong, Structural basis for aminoacylation of cellular modified tRNALys3 by human lysyl-tRNA synthetase. Nucleic Acids Res., 53(5) (2025). [doi: 10.1093/nar/gkaf114]

High ImpactMatthew Cook, Christian Freniere, Chunxiang Wu, Faith Lozano, Yong Xiong, Structural insights into HIV-2 CA lattice formation and FG-pocket binding revealed by single-particle cryo-EM. Cell Rep., 44(2), 115245 (2025). [doi: 10.1016/j.celrep.2025.115245]

Cited 1 timeBradyn Quintard, Xi Yang, Liguo Wang, Quantitative Modeling of High-Energy Electron Scattering in Thick Samples Using Monte Carlo Techniques. Applied Sciences, 15(2), 565 (2025). [doi: 10.3390/app15020565]

High ImpactCited 1 timeYingxia Hu, Krista A. Delviks-Frankenberry, Chunxiang Wu, Fidel Arizaga, Vinay K. Pathak, Yong Xiong, Structural insights into PPP2R5A degradation by HIV-1 Vif. Nat Struct Mol Biol, 31(10), 1492-1501 (2024). [doi: 10.1038/s41594-024-01314-6]

Judy Z Hu, Lijun Qiao, Xianhai Zhao, Chang-Jun Liu, Guo-Bin Hu, Continuity of Mitochondrial Budding: Insights from BS-C-1 Cells by In Situ Cryo-electron Tomography. Microsc. Microanal. (2025). [doi: 10.1093/mam/ozae122]

High ImpactCited 2 timesRan Yang, Olivia Hunker, Marleigh Wise, Franziska Bleichert, Multiple mechanisms for licensing human replication origins. Nature, 636(8042), 488-498 (2024). [doi: 10.1038/s41586-024-08237-8]

High ImpactCited 2 timesErik Henze, Jacqueline J. Ehrlich, Janice L. Robertson, Eric Gelsleichter, Toshimitsu Kawate, The C-terminal activating domain promotes pannexin 1 channel opening. Proc Natl Acad Sci USA, 121(51) (2024). [doi: 10.1073/pnas.2411898121]

High ImpactJian-Shu Lou, Minfei Su, Jinan Wang, Hung Nguyen Do, Yinglong Miao, Xin-Yun Huang, Distinct binding conformations of epinephrine with α- and β-adrenergic receptors. Exp Mol Med, 56(9), 1952-1966 (2024). [doi: 10.1038/s12276-024-01296-x]

High ImpactYueyue Wang, Yalan Zhang, Wenxue Li, Barbora Salovska, Jianan Zhang, Tongqing Li, Hengyi Li, Yansheng Liu, Leonard K. Kaczmarek, Lajos Pusztai, Daryl E. Klein, GABAA receptor π forms channels that stimulate ERK through a G-protein-dependent pathway. Mol. Cell, 85(1), 166-176.e5 (2025). [doi: 10.1016/j.molcel.2024.11.016]

High ImpactCited 3 timesLinlin You, Chengyuan Wang, Vadim Molodtsov, Konstantin Kuznedelov, Xinyi Miao, Breanna R. Wenck, Paul Ulisse, Travis J. Sanders, Craig J. Marshall, Emre Firlar, Jason T. Kaelber, Thomas J. Santangelo, Richard H. Ebright, Structural basis of archaeal FttA-dependent transcription termination. Nature, 635(8037), 229-236 (2024). [doi: 10.1038/s41586-024-07979-9]

High ImpactChristopher J. Gisriel, Tirupathi Malavath, Tianyin Qiu, Jan Paul Menzel, Victor S. Batista, Gary W. Brudvig, Lisa M. Utschig, Structure of a biohybrid photosystem I-platinum nanoparticle solar fuel catalyst. Nat. Comm., 15(1), 9519 (2024). [doi: 10.1038/s41467-024-53476-y]

Vladyslava Sokolova, Jacob Miratsky, Vladimir Svetlov, Michael Brenowitz, John Vant, Tyler S. Lewis, Kelly Dryden, Gahyun Lee, Shayan Sarkar, Evgeny Nudler, Abhishek Singharoy, Dongyan Tan, Structural mechanism of HP1⍺-dependent transcriptional repression and chromatin compaction. Structure, 32(11), 2094-2106.e6 (2024). [doi: 10.1016/j.str.2024.09.013]

High ImpactRuoxi Wu, Shakti Ingle, Sarah A Barnes, Heather R Dahlin, Susmita Khamrui, Yufei Xiang, Yi Shi, David H Bechhofer, Michael B Lazarus, Structural insights into RNA cleavage by a novel family of bacterial RNases. Nucleic Acids Res. (2024). [doi: 10.1093/nar/gkae717]

David A. Flesher, Jinchan Liu, Jimin Wang, Christopher J. Gisriel, Ke R. Yang, Victor S. Batista, Richard J. Debus, Gary W. Brudvig, Mutation-induced shift of the photosystem II active site reveals insight into conserved water channels. J. Biol. Chem., 300(7), 107475 (2024). [doi: 10.1016/j.jbc.2024.107475]

Cited 2 timesZihan Lin, Xiao Zhang, Purbasha Nandi, Yuewei Lin, Liguo Wang, Yong S. Chu, Timothy Paape, Yang Yang, Xianghui Xiao, Qun Liu, Correlative single-cell hard X-ray computed tomography and X-ray fluorescence imaging. Commun Biol, 7(1), 280 (2024). [doi: 10.1038/s42003-024-05950-y]

High ImpactCited 6 timesStefan G. Krimmer, Nicole Bertoletti, Yoshihisa Suzuki, Luka Katic, Jyotidarsini Mohanty, Sheng Shu, Sangwon Lee, Irit Lax, Wei Mi, Joseph Schlessinger, Cryo-EM analyses of KIT and oncogenic mutants reveal structural oncogenic plasticity and a target for therapeutic intervention. Proc Natl Acad Sci USA, 120(13) (2023). [doi: 10.1073/pnas.2300054120]

High ImpactCited 15 timesAudrey L. Warren, David Lankri, Michael J. Cunningham, Inis C. Serrano, Lyonna F. Parise, Andrew C. Kruegel, Priscilla Duggan, Gregory Zilberg, Michael J. Capper, Vaclav Havel, Scott J. Russo, Dalibor Sames, Daniel Wacker, Structural pharmacology and therapeutic potential of 5-methoxytryptamines. Nature, 630(8015), 237-246 (2024). [doi: 10.1038/s41586-024-07403-2]

High ImpactCited 20 timesWan Zheng, Pengxin Chai, Jiapeng Zhu, Kai Zhang, High-resolution in situ structures of mammalian respiratory supercomplexes. Nature, 631(8019), 232-239 (2024). [doi: 10.1038/s41586-024-07488-9]

High ImpactCited 5 timesHao Zuo, Jinseo Park, Aurel Frangaj, Jianxiang Ye, Guanqi Lu, Jamie J. Manning, Wesley B. Asher, Zhengyuan Lu, Guo-bin Hu, Liguo Wang, Joshua Mendez, Edward Eng, Zhening Zhang, Xin Lin, Robert Grassucci, Wayne A. Hendrickson, Oliver B. Clarke, Jonathan A. Javitch, Arthur D. Conigrave, Qing R. Fan, Promiscuous G-protein activation by the calcium-sensing receptor. Nature, 629(8011), 481-488 (2024). [doi: 10.1038/s41586-024-07331-1]

High ImpactGregory Zilberg, Alexandra K. Parpounas, Audrey L. Warren, Bianca Fiorillo, Davide Provasi, Marta Filizola, Daniel Wacker, Structural insights into the unexpected agonism of tetracyclic antidepressants at serotonin receptors 5-HT _1e R and 5-HT _1F R. Sci. Adv., 10(16) (2024). [doi: 10.1126/sciadv.adk4855]

Liguo Wang, Christina M. Zimanyi, Cryo-EM sample preparation for high-resolution structure studies. Acta Cryst Sect F, 80(4), 74-81 (2024). [doi: 10.1107/S2053230X24002553]

Cited 4 timesPing Ren, Yingxia Hu, Lei Peng, Luojia Yang, Kazushi Suzuki, Zhenhao Fang, Meizhu Bai, Liqun Zhou, Yanzhi Feng, Yongji Zou, Yong Xiong, Sidi Chen, Function and Cryo-EM structures of broadly potent bispecific antibodies against multiple SARS-CoV-2 Omicron sublineages. Sig Transduct Target Ther, 8(1), 281 (2023). [doi: 10.1038/s41392-023-01509-1]

High ImpactCited 5 timesMohammad Afsar, GuanQun Liu, Lijia Jia, Eliza A. Ruben, Digant Nayak, Zuberwasim Sayyad, Priscila dos Santos Bury, Kristin E. Cano, Anindita Nayak, Xiang Ru Zhao, Ankita Shukla, Patrick Sung, Elizabeth V. Wasmuth, Michaela U. Gack, Shaun K. Olsen, Cryo-EM structures of Uba7 reveal the molecular basis for ISG15 activation and E1-E2 thioester transfer. Nat. Comm., 14(1), 4786 (2023). [doi: 10.1038/s41467-023-39780-z]

Cited 5 timesPreeti Verma, Albert L. Kwansa, Ruoya Ho, Yaroslava G. Yingling, Jochen Zimmer, Insights into substrate coordination and glycosyl transfer of poplar cellulose synthase-8. Structure, 31(10), 1166-1173.e6 (2023). [doi: 10.1016/j.str.2023.07.010]

High ImpactCited 8 timesJacob W. Weaver, Sergey Proshkin, Wenqian Duan, Vitaly Epshtein, Manjunath Gowder, Binod K. Bharati, Elena Afanaseva, Alexander Mironov, Alexander Serganov, Evgeny Nudler, Control of transcription elongation and DNA repair by alarmone ppGpp. Nat Struct Mol Biol, 30(5), 600-607 (2023). [doi: 10.1038/s41594-023-00948-2]

High ImpactCited 4 timesLie Wang, Anthony Hoang, Eva Gil-Iturbe, Arthur Laganowsky, Matthias Quick, Ming Zhou, Mechanism of anion exchange and small-molecule inhibition of pendrin. Nat. Comm., 15(1), 346 (2024). [doi: 10.1038/s41467-023-44612-1]

Cited 5 timesLiguo Wang, Xi Yang, Monte Carlo Simulation of Electron Interactions in an MeV-STEM for Thick Frozen Biological Sample Imaging. Applied Sciences, 14(5), 1888 (2024). [doi: 10.3390/app14051888]

High ImpactCited 8 timesChunyi Hu, Mason T. Myers, Xufei Zhou, Zhonggang Hou, Macy L. Lozen, Ki Hyun Nam, Yan Zhang, Ailong Ke, Exploiting activation and inactivation mechanisms in type I-C CRISPR-Cas3 for genome-editing applications. Mol. Cell, 84(3), 463-475.e5 (2024). [doi: 10.1016/j.molcel.2023.12.034]

Cited 4 timesGaya P. Yadav, Haiyuan Wang, Joke Ouwendijk, Stephen Cross, Qiaochu Wang, Feng Qin, Paul Verkade, Michael X. Zhu, Qiu-Xing Jiang, Chromogranin B (CHGB) is dimorphic and responsible for dominant anion channels delivered to cell surface via regulated secretion. Front. Mol. Neurosci., 16 (2023). [doi: 10.3389/fnmol.2023.1205516]

High ImpactCited 8 timesMinfei Su, Jinan Wang, Guoqing Xiang, Hung Nguyen Do, Joshua Levitz, Yinglong Miao, Xin-Yun Huang, Structural basis of agonist specificity of α1A-adrenergic receptor. Nat. Comm., 14(1), 4819 (2023). [doi: 10.1038/s41467-023-40524-2]

High ImpactCited 5 timesSwapnil C. Devarkar, Michael Vetick, Shravani Balaji, Ivan B. Lomakin, Luojia Yang, Danni Jin, Wendy V. Gilbert, Sidi Chen, Yong Xiong, Structural basis for translation inhibition by MERS-CoV Nsp1 reveals a conserved mechanism for betacoronaviruses. Cell Rep., 42(10), 113156 (2023). [doi: 10.1016/j.celrep.2023.113156]

Cited 4 timesChristopher J. Gisriel, Gaozhong Shen, Gary W. Brudvig, Donald A. Bryant, Structure of the antenna complex expressed during far-red light photoacclimation in Synechococcus sp. PCC 7335. J. Biol. Chem., 300(2), 105590 (2024). [doi: 10.1016/j.jbc.2023.105590]

Cited 8 timesTimothy Chaya, Aparajita Banerjee, Brian D Rutter, Deji Adekanye, Jean Ross, Guobin Hu, Roger W Innes, Jeffrey L Caplan, The extracellular vesicle proteomes of <em>Sorghum bicolor</em> and <em>Arabidopsis thaliana</em> are partially conserved. Plant Physiol. (2024). [doi: 10.1093/plphys/kiad644]

High ImpactCited 8 timesAnuska Das, Jay Rai, Mitchell O. Roth, Yuerong Shu, Megan L. Medina, Mackenzie R. Barakat, Hong Li, Coupled catalytic states and the role of metal coordination in Cas9. Nat. Catal., 6(10), 969-977 (2023). [doi: 10.1038/s41929-023-01031-1]

High ImpactCited 7 timesYu Zhao, Jay Rai, Hong Li, Regulation of translation by ribosomal RNA pseudouridylation. Sci. Adv., 9(33) (2023). [doi: 10.1126/sciadv.adg8190]

High ImpactCited 6 timesMichael J. Capper, Shifan Yang, Alexander C. Stone, Sezen Vatansever, Gregory Zilberg, Yamuna Kalyani Mathiharan, Raul Habib, Keino Hutchinson, Yihan Zhao, Avner Schlessinger, Mihaly Mezei, Roman Osman, Bin Zhang, Daniel Wacker, Substrate binding and inhibition of the anion exchanger 1 transporter. Nat Struct Mol Biol, 30(10), 1495-1504 (2023). [doi: 10.1038/s41594-023-01085-6]

High ImpactCited 11 timesLie Wang, Ming Zhou, Structure of a eukaryotic cholinephosphotransferase-1 reveals mechanisms of substrate recognition and catalysis. Nat. Comm., 14(1), 2753 (2023). [doi: 10.1038/s41467-023-38003-9]

High ImpactCited 5 timesWilliam D. Ton, Yue Wang, Pengxin Chai, Cisloynny Beauchamp-Perez, Nicholas T. Flint, Lindsay G. Lammers, Hao Xiong, Kai Zhang, Steven M. Markus, Microtubule-binding-induced allostery triggers LIS1 dissociation from dynein prior to cargo transport. Nat Struct Mol Biol, 30(9), 1365-1379 (2023). [doi: 10.1038/s41594-023-01010-x]

High ImpactCited 13 timesChangxu Pang, Jin Chai, Ping Zhu, John Shanklin, Qun Liu, Structural mechanism of intracellular autoregulation of zinc uptake in ZIP transporters. Nat. Comm., 14(1), 3404 (2023). [doi: 10.1038/s41467-023-39010-6]

High ImpactCited 38 timesArthur Neuberger, Mai Oda, Yury A. Nikolaev, Kirill D. Nadezhdin, Elena O. Gracheva, Sviatoslav N. Bagriantsev, Alexander I. Sobolevsky, Human TRPV1 structure and inhibition by the analgesic SB-366791. Nat. Comm., 14(1), 2451 (2023). [doi: 10.1038/s41467-023-38162-9]

High ImpactCited 10 timesJin Chai, Gongrui Guo, Sean M. McSweeney, John Shanklin, Qun Liu, Structural basis for enzymatic terminal C–H bond functionalization of alkanes. Nat Struct Mol Biol, 30(4), 521-526 (2023). [doi: 10.1038/s41594-023-00958-0]

High ImpactCited 86 timesMichal Pyzik, Lisa K. Kozicky, Amit K. Gandhi, Richard S. Blumberg, The therapeutic age of the neonatal Fc receptor. Nat Rev Immunol, 23(7), 415-432 (2023). [doi: 10.1038/s41577-022-00821-1]

Cited 17 timesChristopher J. Gisriel, Gaozhong Shen, David A. Flesher, Vasily Kurashov, John H. Golbeck, Gary W. Brudvig, Muhamed Amin, Donald A. Bryant, Structure of a dimeric photosystem II complex from a cyanobacterium acclimated to far-red light. J. Biol. Chem., 299(1), 102815 (2023). [doi: 10.1016/j.jbc.2022.102815]

Cited 14 timesClara G. Altomare, Daniel C. Adelsberg, Juan Manuel Carreno, Iden A. Sapse, Fatima Amanat, Ali H. Ellebedy, Viviana Simon, Florian Krammer, Goran Bajic, Structure of a Vaccine-Induced, Germline-Encoded Human Antibody Defines a Neutralizing Epitope on the SARS-CoV-2 Spike N-Terminal Domain. mBio, 13(3) (2022). [doi: 10.1128/mbio.03580-21]

High ImpactCited 61 timesChunyi Hu, Sam P. B. van Beljouw, Ki Hyun Nam, Gabriel Schuler, Fran Ding, Yanru Cui, Alicia Rodríguez-Molina, Anna C. Haagsma, Menno Valk, Martin Pabst, Stan J. J. Brouns, Ailong Ke, Craspase is a CRISPR RNA-guided, RNA-activated protease. Science, 377(6612), 1278-1285 (2022). [doi: 10.1126/science.add5064]

Cited 11 timesSagar Sridhara, Jay Rai, Charlisa Whyms, Hemant Goswami, Huan He, Walter Woodside, Michael P. Terns, Hong Li, Structural and biochemical characterization of in vivo assembled Lactococcus lactis CRISPR-Csm complex. Commun Biol, 5(1), 279 (2022). [doi: 10.1038/s42003-022-03187-1]

Cited 13 timesHemant N Goswami, Jay Rai, Anuska Das, Hong Li, Molecular mechanism of active Cas7-11 in processing CRISPR RNA and interfering target RNA, 11 (2022). [doi: 10.7554/eLife.81678]

Cited 6 timesWu Liu, Martien Schoonen, Tong Wang, Sean McSweeney, Qun Liu, Cryo-EM structure of transmembrane AAA+ protease FtsH in the ADP state. Commun Biol, 5(1), 257 (2022). [doi: 10.1038/s42003-022-03213-2]

High ImpactCited 11 timesLei Peng, Yingxia Hu, Madeleine C. Mankowski, Ping Ren, Rita E. Chen, Jin Wei, Min Zhao, Tongqing Li, Therese Tripler, Lupeng Ye, Ryan D. Chow, Zhenhao Fang, Chunxiang Wu, Matthew B. Dong, Matthew Cook, Guilin Wang, Paul Clark, Bryce Nelson, Daryl Klein, Richard Sutton, Michael S. Diamond, Craig B. Wilen, Yong Xiong, Sidi Chen, Monospecific and bispecific monoclonal SARS-CoV-2 neutralizing antibodies that maintain potency against B.1.617. Nat. Comm., 13(1), 1638 (2022). [doi: 10.1038/s41467-022-29288-3]

High ImpactCited 47 timesGabriel Schuler, Chunyi Hu, Ailong Ke, Structural basis for RNA-guided DNA cleavage by IscB-ωRNA and mechanistic comparison with Cas9. Science, 376(6600), 1476-1481 (2022). [doi: 10.1126/science.abq7220]

Cited 13 timesYu Zhao, Jay Rai, Hongguo Yu, Hong Li, CryoEM structures of pseudouridine-free ribosome suggest impacts of chemical modifications on ribosome conformations. Structure, 30(7), 983-992.e5 (2022). [doi: 10.1016/j.str.2022.04.002]

Cited 54 timesChristopher J. Gisriel, Gaozhong Shen, Ming-Yang Ho, Vasily Kurashov, David A. Flesher, Jimin Wang, William H. Armstrong, John H. Golbeck, David J. Vinyard, Richard J. Debus, Gary W. Brudvig, Donald A. Bryant, Marilyn R. Gunner, Structure of a monomeric photosystem II core complex from a cyanobacterium acclimated to far-red light reveals the functions of chlorophylls d and f. J. Biol. Chem., 298(1), 101424 (2022). [doi: 10.1016/j.jbc.2021.101424]

Cited 36 timesChristopher J. Gisriel, David A. Flesher, Gaozhong Shen, Jimin Wang, Ming-Yang Ho, Gary W. Brudvig, Donald A. Bryant, Structure of a photosystem I-ferredoxin complex from a marine cyanobacterium provides insights into far-red light photoacclimation. J. Biol. Chem., 298(1), 101408 (2022). [doi: 10.1016/j.jbc.2021.101408]

High ImpactCited 77 timesJin Chai, Yuanheng Cai, Changxu Pang, Liguo Wang, Sean McSweeney, John Shanklin, Qun Liu, Structural basis for SARS-CoV-2 envelope protein recognition of human cell junction protein PALS1. Nat. Comm., 12(1), 3433 (2021). [doi: 10.1038/s41467-021-23533-x]