Evidence map›Paper›PMID 33877613›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2021

Probing Protein-Membrane Interactions and Dynamics Using Hydrogen-Deuterium Exchange Mass Spectrometry (HDX-MS).

Jordan T B Stariha, Reece M Hoffmann, David J Hamelin, John E Burke

Abstract read
PubMed Publisher
In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
18.0field-weighted citation impact, top 1% 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

28 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
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  4. Mapping SARS-CoV-2 Nucleocapsid Function with Nanobodies.bioRxiv : the preprint server for biology · 2026
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  17. Molecular basis for plasma membrane recruitment of PI4KA by EFR3.bioRxiv : the preprint server for biology · 2024
    Article
  18. Article
  19. Article
  20. Spartin-mediated lipid transfer facilitates lipid droplet turnover.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
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

4 authors at 1 institution in 1 country.

Jordan T B StarihaDepartment of Biochemistry and Microbiology, University of Victoria, Victoria, BC, Canada.
Reece M HoffmannDepartment of Biochemistry and Microbiology, University of Victoria, Victoria, BC, Canada.
David J HamelinDepartment of Biochemistry and Microbiology, University of Victoria, Victoria, BC, Canada.
John E BurkeDepartment of Biochemistry and Microbiology, University of Victoria, Victoria, BC, Canada. jeburke@uvic.ca.
University of Victoria · CA

Funding

CIHR CRN-142393
6 · The paper itself

Abstract

Cellular membranes are a central hub for initiation and execution of many signaling processes. Integral to these processes being accomplished appropriately is the highly controlled recruitment and assembly of proteins at membrane surfaces. The study of the molecular mechanisms that mediate protein-membrane interactions can be facilitated by utilizing hydrogen-deuterium exchange mass spectrometry (HDX-MS). HDX-MS is a robust analytical technique that allows for the measurement of the exchange rate of backbone amide hydrogens with solvent to make inferences about protein structure and conformation. This chapter discusses the use of HDX-MS as a tool to study the conformational changes that occur within peripheral membrane proteins upon association with membrane. Particular reference will be made to the analysis of the protein kinase Akt and its activation upon binding phosphatidylinositol (3,4,5) tris-phosphate (PIP

Indexed as

Biophysical PhenomenaCell MembraneHydrogen Deuterium Exchange-Mass SpectrometryMolecular Dynamics SimulationPhosphatidylinositol PhosphatesProtein BindingProtein ConformationProteomicsProto-Oncogene Proteins c-aktphosphatidylinositol 3,4,5-triphosphatePhosphatidylinositol PhosphatesProto-Oncogene Proteins c-aktHDX-MSHydrogen–deuterium exchangeLipid signalingMass spectrometryProtein dynamicsProtein–membrane interactionsStructural proteomics

Identifiers

PMID33877613
OpenAlexW3154889462

What OpenQuestion holds

Textmetadata
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.