Evidence map›Paper›PMID 30802434›Full record

ReviewChemistry and physics of lipids2019

Hydrogen-deuterium exchange mass spectrometry of membrane proteins in lipid nanodiscs.

Michelle Redhair, Amanda F Clouser, William M Atkins

Open access · greenAbstract readReview
In one paragraph

Review in Chemistry and physics of lipids, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.0field-weighted citation impact, top 8% of its field
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

26 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
  2. Article
  3. The Nanodisc System for Investigating Protein-Lipid Interactions.Methods in molecular biology (Clifton, N.J.) · 2026
    Review
  4. Article
  5. Review
  6. Review
  7. Nanodiscs for the study of membrane proteins.Current opinion in structural biology · 2024
    Review
  8. MSe Collision Energy Optimization for the Analysis of Membrane Proteins Using HDX-cIMS.Journal of the American Society for Mass Spectrometry · 2024
    Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Solid-State NMR Study to Probe the Effects of Divalent Metal Ions (CaLangmuir : the ACS journal of surfaces and colloids · 2021
    Article
  16. Article
  17. Article
  18. Nanodiscs: A toolkit for membrane protein science.Protein science : a publication of the Protein Society · 2021
    Review
  19. Nanodiscs and Mass Spectrometry: Making Membranes Fly.International journal of mass spectrometry · 2020
    Article
  20. Review
4 · The record

Corrections and comments

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

3 authors at 1 institution in 1 country.

Michelle RedhairDepartment of Medicinal Chemistry, Box 357610, University of Washington, Seattle, WA 98195-7610, United States.
Amanda F ClouserDepartment of Medicinal Chemistry, Box 357610, University of Washington, Seattle, WA 98195-7610, United States.
William M AtkinsDepartment of Medicinal Chemistry, Box 357610, University of Washington, Seattle, WA 98195-7610, United States. Electronic address: winky@uw.edu.
University of Washington · US

Funding

Pharmacological Sciences SupplementT32GM007750 · NIGMS · UNIVERSITY OF WASHINGTON · PI ATKINS, WILLIAM M · 1985 to 2023
$12.6M
Functional Dynamics of Cytochrome P4503A4R01GM130810 · NIGMS · UNIVERSITY OF WASHINGTON · PI ATKINS, WILLIAM M · 2018 to 2021
$1.8M
Functional Dynamics of P-glycoproteinR01GM121603 · NIGMS · UNIVERSITY OF WASHINGTON · PI ATKINS, WILLIAM M · 2017 to 2020
$1.2M
NIGMS NIH HHS R01 GM121603NIGMS NIH HHS R01 GM130810NIGMS NIH HHS T32 GM007750
6 · The paper itself

Abstract

Hydrogen deuterium exchange mass spectrometry (H/DX MS) provides a quantitative comparison of the relative rates of exchange of amide protons for solvent deuterons. In turn, the rate of amide exchange depends on a complex combination of the stability of local secondary structure, solvent accessibility, and dynamics. H/DX MS has, therefore, been widely used to probe structure and function of soluble proteins, but its application to membrane proteins was limited previously to detergent solubilized samples. The large excess of lipids from model membranes, or from membrane fractions derived from in vivo samples, presents challenges with mass spectrometry. The lipid nanodisc platform, consisting of apolipoprotein A-derived membrane scaffold proteins, provides a native like membrane environment in which to capture analyte membrane proteins with a well defined, and low, ratio of lipid to protein. Membrane proteins in lipid nanodiscs are amenable to H/DX MS, and this is expected to lead to a rapid increase in the number of membrane proteins subjected to this analysis. Here we review the few literature examples of the application of H/DX MS to membrane proteins in nanodiscs. The incremental improvements in the experimental workflow of the H/DX MS are described and potential applications of this approach to study membrane proteins are described.

Indexed as

Deuterium Exchange MeasurementLipidsMass SpectrometryMembrane ProteinsNanostructuresLipidsMembrane ProteinsConformational dynamicsConformational exchangeH/DX mass spectrometryMembrane proteinNanodisc

Identifiers

PMID30802434
PMCPMC6480397
OpenAlexW2916290647

What OpenQuestion holds

Textmetadata
LicenceTDM
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.