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

(2023)10.7554/elife.91094.1Source: DataRank Database

Double and triple thermodynamic mutant cycles reveal the basis for specific MsbA-lipid interactions is a research paper (2023). On theSindex it has a DataRank of 0.

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datarank_citation_only_1hop_v6· scope data_onlyMethodology

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Enrichment:Funding (16 grants)OA: goldTopics (30)Linked Datasets (2)DataCite Reuse (2)IDs (PubMed, OpenAlex)

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Authors (6)

Tianqi Zhang ORCID,Michael T. Marty ORCID,David E. Clemmer ORCID,David H. Russell ORCID,Arthur Laganowsky ORCID

Live enrichment

PubMed:19767382 OpenAlex:https://openalex.org/W4387096240

National Institute of General Medical Sciences

Grant: R01GM139876

National Institute of General Medical Sciences

Grant: R01GM138863

National Institute of General Medical Sciences

Grant: RM1GM149374

National Institute of General Medical Sciences

Grant: R35GM128624

National Institute of General Medical Sciences

Grant: RM1GM145416

National Institutes of Health

Grant: DP2GM123486

National Institutes of Health

Grant: R01GM121751

National Institutes of Health

Grant: P41GM128577

National Institutes of Health

Grant: 5R01GM138863-04

Innovative Native Ion Mobility Approaches for Transformational Measurements in Structural Biology

National Institutes of Health

Grant: 5RM1GM149374-02

Native Mass Spectrometry Guided Structural Biology Center

National Institutes of Health

Grant: 1R01GM139876-01

Developing new tools to probe membrane protein-lipid interactions for biomedical applications

National Institutes of Health

Grant: 3P41GM128577-02S1

Resource for Native Mass Spectrometry Guided Structural Biology

National Institutes of Health

Grant: 5R35GM128624-07

Unravelling Membrane Protein-Lipid Interactions using Nanodiscs and Mass Spectrometry

National Institutes of Health

Grant: 5RM1GM145416-03

Understanding the role of lipids in structure and function of membrane proteins

National Institutes of Health

Grant: 1DP2GM123486-01

Native ion mobility mass spectrometry studies of potassium inward rectifier channels: insight into gating and lipid binding

National Institutes of Health

Grant: 5R01GM121751-03

Development of high resolution mobility measurements for structural biology

goldLicense: cc-by

journalhttps://github.com/elifesciences/enhanced-preprints-data/raw/master/data/91094/v1/91094-v1.pdf

publisherhttps://github.com/elifesciences/enhanced-preprints-data/raw/master/data/91094/v1/91094-v1.pdf

publisherhttps://cdn.elifesciences.org/preprints/91094/elife-preprint-91094-v1.pdf

publisherhttps://cdn.elifesciences.org/preprints/91094/elife-preprint-91094-v1.xml

publisherhttps://elifesciences.org/reviewed-preprints/91094v1/pdf

Fields of Study

Protein Structure and DynamicsLipid Membrane Structure and BehaviorMetabolomics and Mass Spectrometry Studies0301 basic medicine03 medical and health sciences

Keywords

MutantBasis (linear algebra)ChemistryProcess (computing)ThermodynamicsPhysicsComputer scienceBiochemistryMathematicsGeneLipopolysaccharidesBinding Sitesnative mass spectrometryQH301-705.5ScienceEntropyQRArticleprotein-lipid interactionsBiochemistry and Chemical BiologyMedicineATP-Binding Cassette TransportersABC transporterBiology (General)

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

10.5281/zenodo.10403301Zenodo

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

10.5281/zenodo.10403300Zenodo