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- protein structure prediction 1,103
- human 601
- protein folding & dynamics 533
- cell signaling & trafficking 340
- cell type annotation 334
- host-pathogen & immune response 314
- microscopy & imaging analysis 279
- chromatin & epigenetic regulation 260
- bacteria (other) 212
- drug response / drug discovery 102
- statistical model 98
- E. coli 89
1,000+ papers
- BiochemistrybioRxivPreprint
EngA adopts multiple distinct conformational states during ribosome assembly
Ankita Arora, Jhalak Aggarwal, Nisheeth Agarwal, Prem S. Kaushal
This study reports cryo-EM structures of the 50S ribosome with EngA-bound GTPγS or GDP, revealing conformational changes in EngA and a novel SLJ motif during ribosome assembly.
DOI 10.64898/2026.11.04.764183 - MicrobiologybioRxivPreprint
Structural basis of virion assembly in the Mycobacterium tuberculosis-infecting mycobacteriophage SWU1
Qucheng Bian, Yu Huang, Tingting Feng…·Yan Gao
This study determines the atomic structure of mycobacteriophage SWU1 using cryo-EM, revealing key architectural features critical for virion assembly and infection.
DOI 10.64898/2026.11.08.765204 - BiochemistrybioRxivPreprint
Bacterial major vault protein homologs form divergent vault structures
Jake C Lachowicz, Mohammed Hoque, Anbo Zhou…·Andrew D Baik
The paper identifies bacterial MVP homologs and reports cryoEM structures of vaults from Corallococcus praedator and a Deltaproteobacteria bacterium, revealing novel symmetries.
DOI 10.64898/2026.11.06.764734 - MicrobiologybioRxivPreprint
Cryo-EM structures of an Acinetobacter baumannii podovirus reveal a canonical capsid maturation
Heng Xue, Guibo Rao, Xinfeng Li…·Hang Yang
The paper reports the cryo-EM structures of an Acinetobacter baumannii podovirus, revealing its capsid maturation mechanism and providing a reference for phage engineering.
DOI 10.64898/2026.11.06.765006 - Molecular BiologybioRxivPreprint
Stepwise assembly and mechanical stability of nsP3 Helical Scaffolds in Chikungunya Virus
Natalia Martin Gonzalez, Andrei Karpov, Juan Reguera, Ignacio Casuso
This study investigates the stepwise assembly and mechanical stability of nsP3 helical scaffolds in Chikungunya Virus using HS-AFM and EM, revealing domain-specific contributions to scaffold formation and function.
DOI 10.64898/2026.11.05.764274 - BiochemistrybioRxivPreprint
Structural basis for inefficient G protein coupling by Frizzled receptors
Wessel A. C. Burger, Susovan Das, Hariprasad Venugopal…·Alisa Glukhova
The paper identifies detergent LMNG as stabilizing a weak FZD-G protein interface, revealing that FZDs inherently weakly couple to G proteins and preferentially signal through DVL.
DOI 10.64898/2026.11.03.763784 - BiophysicsbioRxivPreprint
The Molecular Interplay of Tau and Motor Proteins on Microtubules
Yifei He, Julia Peukes, Mert Golcuk…·Ahmet Yildiz
This study investigates how tau protein regulates motor proteins on microtubules using single-molecule imaging, cryo-EM, and MD simulations, revealing distinct mechanisms for inhibiting kinesin-1 and dynein.
- Cell BiologybioRxivPreprint
The mechanism of cysteine sensing by LRRC58
Emma C. Fink, Hilina B. Woldemichael, Nikhit Kambdur…·Edward T. Chouchani
This study identifies how LRRC58 senses cysteine through structural changes that regulate CDO1 binding and cysteine homeostasis.
DOI 10.64898/2026.11.03.763985 - ImmunologybioRxivPreprint
Structural and evolutionary insights into FcαμR recognition of polymeric immunoglobulins
Mai Zhang, Ruixue Zhang, Yuxin Wang, Junyu Xiao
This study determines cryo-EM structures of FcR bound to IgM and IgA, revealing its binding mechanism and evolutionary insights into pIg receptor recognition.
- NeurosciencebioRxivPreprint
Oligodendrocytes may provide the extra density of α-synuclein filaments from multiple system atrophy
Dongqi Zhang, Magdalena Matic, Airi Tarutani…·Sjors Scheres
The paper investigates how oligodendrocytes contribute to the formation of α-synuclein filaments in multiple system atrophy by comparing seeded aggregation in different cell types.
- BiochemistrybioRxivPreprint
Cryo-EM structures of Cereibacter sphaeroides ferrochelatase reveal an oligomeric state that occludes the substrate-binding site
Jack H Salisbury, Pu Qian, Yibo Jin…·Andrew Hitchcock
This study determines the cryo-EM structures of Cereibacter sphaeroides ferrochelatase, revealing oligomeric states that occlude the substrate-binding site.
DOI 10.64898/2026.11.02.762883 - MicrobiologyNature CommunicationsPeer-reviewed
Structural basis for curvature generation and functional specialization in spirochete flagella
Luca A Troman, Bindusmita Paul, Jack Kim…·Debnath Ghosal
The paper determines the near-atomic structures of spirochete flagellar filaments, revealing how sheath proteins generate curvature and enable functional specialization.
2 citations - BiophysicsbioRxivPreprint
CryoSHIELDs: tunable amphipathic peptide additives for cryo-EM
Caleigh M. Azumaya, Przemysław Dutka, Matthew Camp Johnson…·Stanislau Yatskevich
This paper introduces cryoSHIELDs, tunable peptides that improve cryo-EM sample preparation by modulating the air-water interface, enhancing particle distribution and complex integrity across multiple protein systems.
DOI 10.64898/2026.10.01.755993 - BiochemistryNaturePeer-reviewed
Cryo-EM structure of a methanogen nitrogenase-PII protein supercomplex
R. P. KASHYAP, Thomas M. Deere, Ahmed E. Dhamad…·Edwin Antony
The paper reports a cryo-EM structure of a nitrogenase-PII supercomplex in methanogens, revealing a metabolite-gated assembly mechanism for nitrogenase inhibition.
3 citations - BiochemistryThe EMBO JournalPeer-reviewed
A conserved archaeal ribosome-associated factor linking bacterial hibernation and eukaryotic energy sensing
Diorge Paulo de Souza, Mira B. May, Jackson Carrion…·Joseph H. Davis
This study identifies AHA, a conserved archaeal ribosome-associated factor involved in hibernation and energy sensing, linking prokaryotic translational silencing to eukaryotic energy sensing.
DOI 10.1038/s44318-026-00918-6 - BiochemistryStructurePeer-reviewed
Cryo-EM structure of the Arabidopsis thaliana V-type ATPase
Mariia Khamina, Nadja Wunsch, Upendo Lupanga…·John L. Rubinstein
The paper determines the Cryo-EM structure of the Arabidopsis thaliana V-type ATPase, revealing its catalytic cycle and organelle-specific interactions with TLDc proteins.
DOI 10.1016/j.str.2026.10.002 - MicrobiologyCell ReportsPeer-reviewed
The archaic CUP pilus SMF-1 uses an antiparallel bundling mechanism to initiate biofilm formation
Jessie Lynda Fields, Caitlyn C. Sebastian, Hua Zhang…·Fengbin Wang
This study reveals the structure and bundling mechanism of SMF-1, a CUP pilus in Stenotrophomonas maltophilia, showing it forms antiparallel bundles that initiate biofilm formation.
DOI 10.1016/j.celrep.2026.118075 - BiochemistryJournal of Biological ChemistryPeer-reviewed
Cryo-EM Structures Reveal Upstream DNA Interactions within the Mitochondrial Transcription Initiation Complex
Rory E. Sharkey, Caitlin Schroeder, Xiangyu Deng…·Yang Gao
The paper presents cryo-EM structures of mitochondrial transcription initiation complexes, showing how TFAM and PolRMT interact with upstream DNA to regulate transcription initiation and specificity.
DOI 10.1016/j.jbc.2026.113611 - MicrobiologybioRxivPreprint
Structural characterization of a pseudaminic acid-modified lateral flagellar filament from Vibrio alginolyticus
Miki Kinoshita, Tohru Minamino, Hajime Nakatani…·Michio Homma
The paper characterizes pseudaminic acid modifications on the lateral flagellar filament of Vibrio alginolyticus and shows Maf is required for filament formation.
- BiochemistryBioscience ReportsPeer-reviewed
High-resolution cryoEM of nucleosomes in nuclear extracts of mammalian cells
De‐Sheng Ker, Hedaya Aboalnaga, Luca Pellegrini
The paper presents a method for high-resolution cryoEM of nucleosomes in mammalian cell nuclear extracts without requiring thin sectioning.
- BiochemistryCommunications BiologyPeer-reviewed
Structural characterization of hibernating ribosomes in four Gram-negative pathogenic bacteria
Radhakrishnan B. Vasanthakrishnan, Olivier Delalande, Yann Lefrancois Copy…·Reynald Gillet
This study reports cryo-EM structures of hibernating ribosomes from four Gram-negative bacteria, revealing how hibernation factors inhibit translation.
DOI 10.1038/s42003-026-11002-4 - BiophysicsScience AdvancesPeer-reviewed
Structural Mechanisms of SAMD9 Autoinhibition and Pathogenic Dysregulation
Zongjun Mou, Fushun Zhang, Marisol Morales…·Yan Xiang
This study determines the structural basis of SAMD9 autoinhibition and explains how pathogenic mutations disrupt this mechanism to cause disease.
- BiochemistryCommunications BiologyPeer-reviewed
Substrate-enhanced filamentation of 3-methylcrotonyl-CoA carboxylase in Legionella pneumophila
Radha P. Somarathne, Riti Shrestha, Mishghan Zehra…·Clarissa L. Durie
The paper presents the cryo-EM structure of Legionella pneumophila's MCC and identifies substrate-induced filamentation, suggesting a role in bacterial life cycle differentiation.
DOI 10.1038/s42003-026-10960-z - MicrobiologyNature CommunicationsPeer-reviewed
Structural basis of lenacapavir-induced HIV-1 capsid disruption during virion maturation
Hiroki Tanaka, Reina Morita, Tomomasa Oka…·Shinichi Machida
This study determines the cryo-EM structure of HIV-1 capsid lattice with lenacapavir, showing how it disrupts capsid formation and function during virion maturation.
- BiochemistryNature CommunicationsPeer-reviewed
Structure of Blm10:13S proteasome intermediate reveals parallel assembly pathways for the proteasome core particle
Mandeep Kaur, Xiang Chen, Stella Y. Lee…·Jeroen Roelofs
The paper presents cryo-EM structures of a Blm10:13S proteasome intermediate, revealing parallel assembly pathways for the proteasome core particle involving Blm10 and Pba1/Pba2.
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