ArticleProceedings of the National Academy of Sciences of the United States of America2020
Structure of the cell-binding component of the
Erratum issuedOpen access · greenAbstract read
In one paragraph
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 29 papers.
0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
0.6field-weighted citation impact, top 20% of its field
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
29 citing papers in PubMed, 36 citations in OpenAlex.
- Step-by-step maturation mechanism of the binary toxin pore revealed by cryo-EM analysis.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Structural basis for independent pore function of Vpb4 from Bacillus thuringiensis.Nature communications · 2026Article
- Nanobodies against Clostridioides difficile CDTb provide a toolkit for potent toxin neutralization and highly sensitive quantitation.The Journal of biological chemistry · 2026Article
- Identification of amino acids essential for angulin-1/3 binding of the tricellular tight junction binder, angubindin-1.FEBS open bio · 2026Article
- Oligomerization of the Clostridioides difficile transferase B component proceeds through a stepwise mechanism.PLoS pathogens · 2025Article
- Pore formation by the CDTb component of the Clostridioides difficile binary toxin is CaCommunications biology · 2025Article
- The N-terminus of themBio · 2025Article
- High-Resolution Melting PCR as a Fast and Simple Molecular Biology-Based Method for the Identification of HypervirulentMicroorganisms · 2024Article
- Origin, Evolution and Diversity of φ29-like Phages-Review and Bioinformatic Analysis.International journal of molecular sciences · 2024Review
- Review
- Exploring the Toxin-Mediated Mechanisms inMicroorganisms · 2024Review
- An Updated View on the Cellular Uptake and Mode-of-Action of Clostridioides difficile Toxins.Advances in experimental medicine and biology · 2024Article
- Pathogenicity and virulence ofVirulence · 2023Review
- Structural Basis for Binding of Neutralizing Antibodies toJournal of bacteriology · 2023Article
- Review
- The Hospital Environment as a Potential Source forInternational journal of environmental research and public health · 2023Article
- Computer-Aided Drug Design: An Update.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Binding and Functional Folding (BFF): A Physiological Framework for Studying Biomolecular Interactions and Allostery.Journal of molecular biology · 2022Review
- Cryo-EM structures of the translocational binary toxin complex CDTa-bound CDTb-pore from Clostridioides difficile.Nature communications · 2022Article
- Influence of Binary Toxin Gene Detection and Decreased Susceptibility to Antibiotics among Clostridioides difficile Strains on Disease Severity: a Single-Center Study.Antimicrobial agents and chemotherapy · 2022Article
Corrections and comments
- Erratum issued
Authors and funding
25 authors at 5 institutions in 1 country.
Xingjian XuCity University of New York Advanced Science Research Center, City University of New York, New York, NY 10017.
Raquel Godoy-RuizDepartment of Biochemistry & Molecular Biology, University of Maryland School of Medicine, University of Maryland, Baltimore, MD 21201.
Kaylin A AdipietroDepartment of Biochemistry & Molecular Biology, University of Maryland School of Medicine, University of Maryland, Baltimore, MD 21201.
Christopher PeraltaCity University of New York Advanced Science Research Center, City University of New York, New York, NY 10017.
Danya Ben-HailCity University of New York Advanced Science Research Center, City University of New York, New York, NY 10017.
Kristen M VarneyDepartment of Biochemistry & Molecular Biology, University of Maryland School of Medicine, University of Maryland, Baltimore, MD 21201.
Mary E CookDepartment of Biochemistry & Molecular Biology, University of Maryland School of Medicine, University of Maryland, Baltimore, MD 21201.
Braden M RothDepartment of Biochemistry & Molecular Biology, University of Maryland School of Medicine, University of Maryland, Baltimore, MD 21201.
Paul T WilderDepartment of Biochemistry & Molecular Biology, University of Maryland School of Medicine, University of Maryland, Baltimore, MD 21201.
Thomas ClevelandNational Institute of Standards, Rockville, MD 20899.
Alexander GrishaevNational Institute of Standards, Rockville, MD 20899.
Heather M NeuUniversity of Maryland School of Pharmacy, University of Maryland, Baltimore, MD 21201.
Sarah L J MichelUniversity of Maryland School of Pharmacy, University of Maryland, Baltimore, MD 21201.ORCID 0000-0002-6366-2453
Wenbo YuInstitute for Bioscience and Biotechnology Research, University of Maryland, Rockville, MD 20850.
Dorothy BeckettDepartment of Chemistry & Biochemistry, University of Maryland, College Park, MD 20742.
Richard R RustandiMerck & Co., Inc., Kenilworth, NJ 07033.
Catherine LancasterMerck & Co., Inc., Kenilworth, NJ 07033.
John W LoughneyMerck & Co., Inc., Kenilworth, NJ 07033.
Adam KristopeitMerck & Co., Inc., Kenilworth, NJ 07033.
Sianny ChristantiMerck & Co., Inc., Kenilworth, NJ 07033.
Jessica W OlsonMerck & Co., Inc., Kenilworth, NJ 07033.
Alexander D MacKerellInstitute for Bioscience and Biotechnology Research, University of Maryland, Rockville, MD 20850.
Amedee des GeorgesCity University of New York Advanced Science Research Center, City University of New York, New York, NY 10017; adesgeorges@gc.cuny.edu EPozharskiy@som.umaryland.edu dweber@som.umaryland.edu.
Edwin PozharskiDepartment of Biochemistry & Molecular Biology, University of Maryland School of Medicine, University of Maryland, Baltimore, MD 21201; adesgeorges@gc.cuny.edu EPozharskiy@som.umaryland.edu dweber@som.umaryland.edu.
David J WeberDepartment of Biochemistry & Molecular Biology, University of Maryland School of Medicine, University of Maryland, Baltimore, MD 21201; adesgeorges@gc.cuny.edu EPozharskiy@som.umaryland.edu dweber@som.umaryland.edu.ORCID 0000-0002-8824-1110
University of Maryland, Baltimore · USMerck & Co., Inc., Rahway, NJ, USA (United States) · USThe Graduate Center, CUNY · USNational Institute of Standards and Technology · USUniversity of Maryland, College Park · US
Funding
ZWITTERION SURFACTANT DDMAB FOR IMPROV STABIL OF PROTEINP41RR001209 · NCRR · STANFORD UNIVERSITY · PI SCOTT, EMILY E · 1985 to 2011
$38.9MX-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6MTRD #3: An automated and streamlined pipeline for in-situ molecular microscopyP41GM103310 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI DE MARCO, ALEX, KIEFT, JEFFREY S · 2012 to 2021
$14.7MInterdisciplinary Training Program Muscle BiologyT32AR007592 · NIAMS · UNIVERSITY OF MARYLAND BALTIMORE · PI Aikaterini Kontrogianni-Konstantopoulos · 1996 to 2026
$11.7MUnderstanding membrane proteins’ allosteric modulation with cryo-EMR35GM133598 · NIGMS · NEW YORK UNIVERSITY · PI Amedee des Georges · 2019 to 2026
$3.4MStructure-based targeting of the C. difficile toxin (CDT) from hypervirulent bacterial strainsR56AI152397 · NIAID · UNIVERSITY OF MARYLAND BALTIMORE · PI DES GEORGES, AMEDEE, WEBER, DAVID JOSEPH · 2021 to 2021
$522kNCRR NIH HHS P41 RR001209NIAID NIH HHS R56 AI152397NIAMS NIH HHS T32 AR007592NIGMS NIH HHS P41 GM103310NIGMS NIH HHS P41 GM103393NIGMS NIH HHS R35 GM133598
Abstract
Targeting
Indexed as
ADP Ribose TransferasesAnimalsBacterial ProteinsBacterial ToxinsBinding SitesBiophysical PhenomenaChlorocebus aethiopsClostridioides difficileCryoelectron MicroscopyCrystallography, X-RayEnterotoxinsModels, MolecularNuclear Magnetic Resonance, BiomolecularProtein ConformationProtein DomainsVero Cellsactin-specific ADP-ribosyltransferase, ClostridiumADP Ribose TransferasesBacterial ProteinsBacterial ToxinsEnterotoxinsClostridium difficilecryo-EMNMRstructural biologyX-ray crystallography
Identifiers
What OpenQuestion holds
Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390
Registered trials
None linked
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.