Evidence map›Paper›PMID 34406752›Full record

ReviewChemical reviews2022

Characterizing Endogenous Protein Complexes with Biological Mass Spectrometry.

Rivkah Rogawski, Michal Sharon

Abstract readReview
In one paragraph

Review in Chemical reviews, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing 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

35 citing papers in PubMed.

  1. Article
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  13. The potent PHL4 transcription factor effector domain contains significant disorder.Protein science : a publication of the Protein Society · 2024
    Article
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  16. Thermal Remodeling of Human HDL Particles Reveals Diverse Subspecies.Journal of the American Society for Mass Spectrometry · 2024
    Article
  17. Review
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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.

Rivkah RogawskiDepartment of Biomolecular Sciences, Weizmann Institute of Science, Rehovot 7610001, Israel.
Michal SharonDepartment of Biomolecular Sciences, Weizmann Institute of Science, Rehovot 7610001, Israel.ORCID 0000-0003-3933-0595

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Biological mass spectrometry (MS) encompasses a range of methods for characterizing proteins and other biomolecules. MS is uniquely powerful for the structural analysis of endogenous protein complexes, which are often heterogeneous, poorly abundant, and refractive to characterization by other methods. Here, we focus on how biological MS can contribute to the study of endogenous protein complexes, which we define as complexes expressed in the physiological host and purified intact, as opposed to reconstituted complexes assembled from heterologously expressed components. Biological MS can yield information on complex stoichiometry, heterogeneity, topology, stability, activity, modes of regulation, and even structural dynamics. We begin with a review of methods for isolating endogenous complexes. We then describe the various biological MS approaches, focusing on the type of information that each method yields. We end with future directions and challenges for these MS-based methods.

Indexed as

ProteinsMass SpectrometryProteins

Identifiers

PMID34406752
PMCPMC9052418

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Registered trials

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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.