Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it
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.
2 · The registry
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.
Khuram U AshrafDepartment of Physiology and Cellular Biophysics, Columbia University Irving Medical Center, New York, NY, USA.ORCID http://orcid.org/0000-0002-0799-4947
Kamil NosolDepartment of Biochemistry and Molecular Biology, University of Chicago, Chicago, IL, USA.
Guozhi ZhangDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, AZ, USA.
Rosemary J CaterDepartment of Physiology and Cellular Biophysics, Columbia University Irving Medical Center, New York, NY, USA.
Michael T MartyDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, AZ, USA.
M Stephen TrentDepartment of Infectious Diseases, College of Veterinary Medicine, University of Georgia, Athens, GA, USA. strent@uga.edu.ORCID http://orcid.org/0000-0001-6134-1800
Rie NygaardDepartment of Physiology and Cellular Biophysics, Columbia University Irving Medical Center, New York, NY, USA. rin7007@med.cornell.edu.ORCID http://orcid.org/0000-0002-0425-234X
Phillip J StansfeldSchool of Life Sciences and Department of Chemistry, University of Warwick, Coventry, UK. Phillip.Stansfeld@warwick.ac.uk.ORCID http://orcid.org/0000-0001-8800-7669
Filippo ManciaDepartment of Physiology and Cellular Biophysics, Columbia University Irving Medical Center, New York, NY, USA. fm123@cumc.columbia.edu.ORCID http://orcid.org/0000-0003-3293-2200
Funding
Chaperone-Assisted Structure Determination of Membrane ProteinsR01GM117372 · NIGMS · UNIVERSITY OF CHICAGO · PI ANTHONY A KOSSIAKOFF · 2016 to 2026
$4.0M
The Cell Envelope of the Multi-Drug Resistant Pathogen Acinetobacter baumanniiR01AI150098 · NIAID · UNIVERSITY OF GEORGIA · PI Michael Stephen Trent · 2020 to 2026
$3.9M
Structural basis of integral membrane enzyme functionR35GM132120 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI Filippo Mancia · 2019 to 2026
$3.7M
Unravelling Membrane Protein-Lipid Interactions using Nanodiscs and Mass SpectrometryR35GM128624 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI Michael T Marty · 2018 to 2026
$3.6M
Synthesis and transport of outer membrane components across the Gram-negative cell envelopeR01AI176776 · NIAID · UNIVERSITY OF GEORGIA · PI Michael Stephen Trent · 2023 to 2026
$2.5M
The role of cardiolipin in the biogenesis of the Gram-negative bacterial cell envelopeR01AI174416 · NIAID · UNIVERSITY OF GEORGIA · PI Michael Stephen Trent · 2023 to 2026
$2.4M
Mechanistic insights into lipid A modification by the phosphoethanolamine transferase MCR-1F31AI181556 · NIAID · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI ZINKLE, ALLEN PETER · 2024 to 2024
$49k
NIAID NIH HHS F31 AI181556NIAID NIH HHS R01 AI150098NIAID NIH HHS R01 AI174416NIAID NIH HHS R01 AI176776NIGMS NIH HHS R01 GM117372NIGMS NIH HHS R35 GM128624NIGMS NIH HHS R35 GM132120U.S. Department of Health & Human Services | NIH | National Institute of Allergy and Infectious Diseases (NIAID) AI150098U.S. Department of Health & Human Services | NIH | National Institute of Allergy and Infectious Diseases (NIAID) AI176776U.S. Department of Health & Human Services | NIH | National Institute of Allergy and Infectious Diseases (NIAID) AI181556U.S. Department of Health & Human Services | NIH | National Institute of Allergy and Infectious Diseases (NIAID) AI74416U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) GM132120Wellcome TrustWellcome Trust (Wellcome) 208361/Z/17/Z
6 · The paper itself
Abstract
Polymyxins are used to treat infections caused by multidrug-resistant Gram-negative bacteria. They are cationic peptides that target the negatively charged lipid A component of lipopolysaccharides, disrupting the outer membrane and lysing the cell. Polymyxin resistance is conferred by inner-membrane enzymes, such as phosphoethanolamine transferases, which add positively charged phosphoethanolamine to lipid A. Here, we present the structure of MCR-1, a plasmid-encoded phosphoethanolamine transferase, in its liganded form. The phosphatidylethanolamine donor substrate is bound near the active site in the periplasmic domain, and lipid A is bound over 20 Å away, within the transmembrane region. Integrating structural, biochemical, and drug-resistance data with computational analyses, we propose a two-state model in which the periplasmic domain rotates to bring the active site to lipid A, near the preferential phosphate modification site for MCR-1. This enzymatic mechanism may be generally applicable to other phosphoform transferases with large, globular soluble domains.
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.
Mechanistic basis of antimicrobial resistance mediated by the phosphoethanolamine transferase MCR-1. · full record | OpenQuestion