Evidence map›Paper›PMID 37461710›Full record

ArticlebioRxiv : the preprint server for biology2023

Double and triple thermodynamic mutant cycles reveal the basis for specific MsbA-lipid interactions.

Jixing Lyu, Tianqi Zhang, Michael T Marty, David Clemmer, David H Russell, Arthur Laganowsky

Open access · greenAbstract readPreprint
PubMed Full text at PMC Publisher
In one paragraph

Article in bioRxiv : the preprint server for biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 1 country.

Jixing LyuDepartment of Chemistry, Texas A&M University, College Station, TX 77843.
Tianqi ZhangDepartment of Chemistry, Texas A&M University, College Station, TX 77843.
Michael T MartyDepartment of Chemistry and Biochemistry and Bio5 Institute, The University of Arizona, Tucson, AZ 85721.ORCID 0000-0001-8115-1772
David ClemmerDepartment of Chemistry, Indiana University, Bloomington, IN 47405.ORCID 0000-0003-4039-1360
David H RussellDepartment of Chemistry, Texas A&M University, College Station, TX 77843.ORCID 0000-0003-0830-3914
Arthur LaganowskyDepartment of Chemistry, Texas A&M University, College Station, TX 77843.ORCID 0000-0001-5012-5547
Texas A&M University · USIndiana University Bloomington · USUniversity of Arizona · US

Funding

Waters Select Series Cyclic IMS for P41 Native MS Resource Application to Alzheimer's DiseaseP41GM128577 · NIGMS · OHIO STATE UNIVERSITY · PI SOMOGYI, ARPAD · 2018 to 2022
$7.6M
Understanding the role of lipids in structure and function of membrane proteinsRM1GM145416 · NIGMS · TEXAS A&M UNIVERSITY · PI Erin S Baker, Arthur D Laganowsky · 2022 to 2026
$7.4M
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
Native ion mobility mass spectrometry studies of potassium inward rectifier channels: insight into gating and lipid bindingDP2GM123486 · NIGMS · TEXAS A&M UNIVERSITY HEALTH SCIENCE CTR · PI LAGANOWSKY, ARTHUR D · 2016 to 2016
$2.2M
Development of high resolution mobility measurements for structural biologyR01GM121751 · NIGMS · TRUSTEES OF INDIANA UNIVERSITY · PI CLEMMER, DAVID E., LAGANOWSKY, ARTHUR D · 2017 to 2020
$1.7M
Innovative Native Ion Mobility Approaches for Transformational Measurements in Structural BiologyR01GM138863 · NIGMS · TEXAS A&M UNIVERSITY · PI CLOWERS, BRIAN, LAGANOWSKY, ARTHUR D · 2020 to 2023
$1.2M
Developing new tools to probe membrane protein-lipid interactions for biomedical applicationsR01GM139876 · NIGMS · TEXAS A&M UNIVERSITY · PI LAGANOWSKY, ARTHUR D · 2021 to 2024
$1.2M
NIGMS NIH HHS DP2 GM123486NIGMS NIH HHS P41 GM128577NIGMS NIH HHS R01 GM121751NIGMS NIH HHS R01 GM138863NIGMS NIH HHS R01 GM139876NIGMS NIH HHS R35 GM128624NIGMS NIH HHS RM1 GM145416
6 · The paper itself

Abstract

Structural and functional studies of the ATP-binding cassette transporter MsbA have revealed two distinct lipopolysaccharide (LPS) binding sites: one located in the central cavity and the other at a membrane-facing, exterior site. Although these binding sites are known to be important for MsbA function, the thermodynamic basis for these specific MsbA-LPS interactions is not well understood. Here, we use native mass spectrometry to determine the thermodynamics of MsbA interacting with the LPS-precursor 3-deoxy-D-

Identifiers

PMID37461710
PMCPMC10350010
OpenAlexW4382936592

What OpenQuestion holds

Textmetadata
LicenceCC BY-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.