Article in Structure (London, England : 1993), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
0numbers the graph read from it
0cells of the map it votes in
1citing 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.
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
5 · Who and what money
Authors and funding
6 authors.
Claire Overly CottomDepartment of Biological Sciences, Purdue University, West Lafayette, IN, USA.
Robert StephensonDepartment of Biological Sciences, Purdue University, West Lafayette, IN, USA.
Dante RicciAchaogen, Inc., South San Francisco, CA, USA.
Lixinhao YangSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA, USA.
James C GumbartSchool of Chemistry and Biochemistry, Georgia Institute of Technology, Atlanta, GA, USA; School of Physics, Georgia Institute of Technology, Atlanta, GA, USA.
Nicholas NoinajDepartment of Biological Sciences, Purdue University, West Lafayette, IN, USA; Markey Center for Structural Biology, Purdue University, West Lafayette, IN, USA; Purdue Institute of Inflammation, Immunology and Infectious Disease, Purdue University, West Lafayette, IN, USA. Electronic address: nnoinaj@purdue.edu.
Funding
User Training & OutreachP30GM138396 · NIGMS · UCHICAGO ARGONNE, LLC · PI JANET L. SMITH · 2020 to 2026
$34.3M
The Biophysics Collaborative Access Team (User Training and Outreach)P30GM138395 · NIGMS · ILLINOIS INSTITUTE OF TECHNOLOGY · PI THOMAS C IRVING · 2021 to 2026
$16.5M
High-Speed High-Sensitivity Detector for X-ray Micro-Crystallography at GM/CA@APSS10OD012289 · OD · UNIVERSITY OF CHICAGO · PI FISCHETTI, ROBERT F. · 2014 to 2014
$2.0M
Structural Characterization of the TOC Protein Translocon MachineryR01GM127896 · NIGMS · PURDUE UNIVERSITY · PI NOINAJ, NICHOLAS · 2018 to 2022
$1.5M
Dynamic characterization of outer-membrane-protein biogenesis by the BAM and TAM complexesR01GM123169 · NIGMS · GEORGIA INSTITUTE OF TECHNOLOGY · PI GUMBART, JAMES C. · 2017 to 2021
$1.4M
Unraveling the mechanism by which the BAM complex mediates OMP biogenesisR01GM127884 · NIGMS · PURDUE UNIVERSITY · PI NOINAJ, NICHOLAS · 2019 to 2022
$1.2M
Drug Discovery in Infectious Disease TrainingT32AI148103 · NIAID · PURDUE UNIVERSITY · PI STAHELIN, ROBERT VIRGIL, YEO, YOON · 2020 to 2024
$949k
Advanced Pixel Array Detector for Time-Resolved SAXS and Fiber DiffractionS10OD018090 · OD · ILLINOIS INSTITUTE OF TECHNOLOGY · PI IRVING, THOMAS C · 2014 to 2014
Recent studies have demonstrated BamA, the central component of the β-barrel assembly machinery (BAM), as an important therapeutic target to combat infections caused by Acinetobacter baumannii and other Gram-negative pathogens. Homology modeling indicates BamA in A. baumannii consists of five polypeptide transport-associated (POTRA) domains and a β-barrel membrane domain. We characterized the POTRA domains of BamA from A. baumannii in solution using size-exclusion chromatography small angle X-ray scattering (SEC-SAXS) analysis and determined crystal structures in two conformational states that are drastically different than those previously observed in BamA from other bacteria, indicating that the POTRA domains are even more conformationally dynamic than has been observed previously. Molecular dynamics simulations of the POTRA domains from A. baumannii and Escherichia coli allowed us to identify key structural features that contribute to the observed novel states. Together, these studies expand on our current understanding of the conformational plasticity within BamA across differing bacterial species.
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.
Structural characterization of the POTRA domains from A. baumannii reveals new conformations in BamA. · full record | OpenQuestion