Evidence map›Paper›PMID 35819771›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2022

Light Scattering Techniques to Assess Self-Assembly and Hydrodynamics of Membrane Trafficking Proteins.

Marijn G J Ford, Rajesh Ramachandran

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2022. 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
0.5field-weighted citation impact, top 42% 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

0 citing papers in PubMed, 1 citations in OpenAlex.

No citing paper in PubMed yet.

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

2 authors at 2 institutions in 1 country.

Marijn G J FordDepartment of Cell Biology, University of Pittsburgh School of Medicine, Pittsburgh, PA, USA. marijn@pitt.edu.ORCID 0000-0002-9115-4413
Rajesh RamachandranDepartment of Physiology and Biophysics, Case Western Reserve University School of Medicine, Cleveland, OH, USA. rxr275@case.edu.ORCID 0000-0002-4645-2841
University of Pittsburgh · USUniversity School · US

Funding

MOLECULAR MECHANISMS OF DYNAMIN-RELATED PROTEIN 1-MEDIATED MITOCHONDRIAL FISSIONR01GM121583 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI RAMACHANDRAN, RAJESH · 2017 to 2021
$1.8M
Regulation of membrane remodeling by the SNX-BAR protein familyR35GM139546 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI FORD, MARIJN GERARD JOHANNES · 2021 to 2021
$511k
NIGMS NIH HHS R01 GM121583NIGMS NIH HHS R35 GM139546
6 · The paper itself

Abstract

Light scattering methods permit the determination of molar mass and hydrodynamic radius for a protein from first principles. They are, therefore, particularly useful for the biophysical characterization of any protein. Molar mass and hydrodynamic radius determinations may be used to demonstrate that the protein of interest multimerizes. In the endomembrane system, reversible and regulated assembly and multimerization of proteins is critical for building coats required for vesicle budding, for the function of membrane remodeling machines, for fission and fusion and for assembling and disassembling trafficking intermediates. Light scattering methods have therefore significantly contributed to the understanding of the underlying trafficking processes. Herein, we describe methods to express and purify the recombinant fungal SNX-BAR Mvp1, a membrane remodeling protein required for retrograde trafficking at the endosome. Using Mvp1 as an example, we provide protocols for determining its molar mass and hydrodynamic radius by multiangle static light scattering and dynamic light scattering, respectively. These methods can be applied directly to the study of other membrane trafficking proteins, yielding a wealth of biophysical and biochemical information.

Indexed as

HydrodynamicsProteinsEndosomesMembranesMolecular WeightProteinsDLSLight scatteringMembrane remodelingMultimerizationMvp1SEC-MALSSLS

Identifiers

PMID35819771
OpenAlexW4285078967

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.