ArticleNature2023
Structural basis of BAM-mediated outer membrane β-barrel protein assembly.
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In one paragraph
Article in Nature, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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57citing papers in PubMed
–field-weighted citation impact
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
57 citing papers in PubMed.
- BamA as a next-generation antibacterial target: mechanistic insights, inhibitor landscape, and rational drug design strategies.RSC advances · 2026Review
- In vitro reconstitution implicates multiple OMP assembly factors in CdiAThe Journal of biological chemistry · 2026Article
- Stress-induced membrane insertion at the β-barrel assembly machinery complex regulates BepA metalloprotease activity.Nature communications · 2026Article
- Cryo-EM structures of the SurA-BAM complex reveal conformational changes in outer membrane protein assembly.Nature communications · 2026Article
- Cryo-EM structures of multiple-peptide resistance factor (MprF) from Pseudomonas aeruginosa.The FEBS journal · 2026Article
- Mechanistic basis of LolDF-mediated lipoprotein transport in Acinetobacter.Nature communications · 2026Article
- Conformational hijacking of lipoprotein transporter LolDF enables precision antimicrobial activity against Acinetobacter baumannii.Nature communications · 2026Article
- BAM-BepA complexes in outer membrane protein quality control.Nature communications · 2026Article
- L-type pyocins inhibit the BAM complex to kill without cell entry.Nature communications · 2026Article
- DeepPath: overcoming data scarcity for protein transition pathway prediction using physics-based deep learning.Chemical science · 2026Article
- Gut microbial genetic variations are associated with exploratory behavior via SNV-driven metabolic regulation in a sheep model.Science China. Life sciences · 2026Article
- A mechanism for substrate quality control in outer membrane protein assembly.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Assembly of two functionally-distinct protein import complexes in the outer membrane of plant chloroplasts.Nature communications · 2026Article
- A secreted citrus protease cleaves an outer membrane protein of the Huanglongbing pathogen.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The BaeSR two-component system activatesmBio · 2026Article
- Integration of Membrane Proteins into the Outer Membrane of Diderm Bacteria by the BAM Complex.Chemical reviews · 2026Review
- Structures of folding intermediates on BAM show diverse substrates fold by a conserved mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Mechanism of phospholipid transport to the bacterial outer membrane by TAM.bioRxiv : the preprint server for biology · 2026Article
- Targeting of the Gram-Negative Outer Membrane for Antibiotic Discovery and Potentiation.ACS infectious diseases · 2026Review
- Review
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Authors and funding
15 authors.
Chongrong Shen *State Key Laboratory of Biotherapy and Cancer Center, National Clinical Research Center for Geriatrics, West China Hospital, Sichuan University and Collaborative Innovation Center of Biotherapy, Chengdu, China.
Shenghai Chang *Department of Biophysics of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, China.
Qinghua Luo *State Key Laboratory of Biotherapy and Cancer Center, National Clinical Research Center for Geriatrics, West China Hospital, Sichuan University and Collaborative Innovation Center of Biotherapy, Chengdu, China.
Kevin Chun Chan *Institute of Quantitative Biology, College of Life Sciences, Cancer Center, The First Affiliated Hospital, School of Medicine, Zhejiang University, Hangzhou, China.ORCID http://orcid.org/0000-0002-3705-1835
Zhibo ZhangState Key Laboratory of Biotherapy and Cancer Center, National Clinical Research Center for Geriatrics, West China Hospital, Sichuan University and Collaborative Innovation Center of Biotherapy, Chengdu, China.
Bingnan LuoState Key Laboratory of Biotherapy and Cancer Center, National Clinical Research Center for Geriatrics, West China Hospital, Sichuan University and Collaborative Innovation Center of Biotherapy, Chengdu, China.
Teng XieInstitute of Quantitative Biology, College of Life Sciences, Cancer Center, The First Affiliated Hospital, School of Medicine, Zhejiang University, Hangzhou, China.
Guangwen LuState Key Laboratory of Biotherapy and Cancer Center, National Clinical Research Center for Geriatrics, West China Hospital, Sichuan University and Collaborative Innovation Center of Biotherapy, Chengdu, China.ORCID http://orcid.org/0000-0001-7568-592X
Xiaofeng ZhuCollege of Life Science, Sichuan University, Chengdu, China.
Xiawei WeiState Key Laboratory of Biotherapy and Cancer Center, National Clinical Research Center for Geriatrics, West China Hospital, Sichuan University and Collaborative Innovation Center of Biotherapy, Chengdu, China.ORCID http://orcid.org/0000-0002-6513-6422
Changjiang DongSchool of Pharmaceutical Sciences, Wuhan University, Wuhan, China.
Ruhong ZhouInstitute of Quantitative Biology, College of Life Sciences, Cancer Center, The First Affiliated Hospital, School of Medicine, Zhejiang University, Hangzhou, China. rhzhou@zju.edu.cn.ORCID http://orcid.org/0000-0001-8624-5591
Xing ZhangDepartment of Biophysics of Sir Run Run Shaw Hospital, Zhejiang University School of Medicine, Hangzhou, China. xzhang1999@zju.edu.cn.ORCID http://orcid.org/0000-0002-6776-326X
Xiaodi TangState Key Laboratory of Biotherapy and Cancer Center, National Clinical Research Center for Geriatrics, West China Hospital, Sichuan University and Collaborative Innovation Center of Biotherapy, Chengdu, China. tangxiaodi@scu.edu.cn.ORCID http://orcid.org/0000-0001-7452-5211
Haohao DongState Key Laboratory of Biotherapy and Cancer Center, National Clinical Research Center for Geriatrics, West China Hospital, Sichuan University and Collaborative Innovation Center of Biotherapy, Chengdu, China. haohaodong@scu.edu.cn.ORCID http://orcid.org/0000-0002-5022-3494
Funding
No grant is acknowledged in the PubMed record.
Abstract
The outer membrane structure is common in Gram-negative bacteria, mitochondria and chloroplasts, and contains outer membrane β-barrel proteins (OMPs) that are essential interchange portals of materials
Indexed as
Bacterial Outer Membrane ProteinsEscherichia coliEscherichia coli ProteinsMolecular Dynamics SimulationProtein FoldingSerine EndopeptidasesSubstrate SpecificityBacterial Outer Membrane ProteinsBamA protein, E coliEscherichia coli ProteinsEspP protein, E coliSerine Endopeptidases
Identifiers
PMID
37100902What OpenQuestion holds
Textmetadata
Read underepoch 390
Registered trials
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.