Evidence map›Paper›PMID 28100928›Full record

ReviewQuarterly reviews of biophysics2016

Mass Spectrometry: A Technique of Many Faces.

Maya A Olshina, Michal Sharon

Abstract readReview
In one paragraph

Review in Quarterly reviews of biophysics, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

  1. Mass Spectrometry Applications to Study Human Microbiome.Advances in experimental medicine and biology · 2024
    Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Catalysts (Basel, Switzerland) · 2017
    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

2 authors.

Maya A OlshinaDepartment of Biomolecular Sciences, Weizmann Institute of Science, Rehovot 7610001, Israel.
Michal SharonDepartment of Biomolecular Sciences, Weizmann Institute of Science, Rehovot 7610001, Israel.

Funding

European Research Council 636752
6 · The paper itself

Abstract

Protein complexes form the critical foundation for a wide range of biological process, however understanding the intricate details of their activities is often challenging. In this review we describe how mass spectrometry plays a key role in the analysis of protein assemblies and the cellular pathways which they are involved in. Specifically, we discuss how the versatility of mass spectrometric approaches provides unprecedented information on multiple levels. We demonstrate this on the ubiquitin-proteasome proteolytic pathway, a process that is responsible for protein turnover. We follow the various steps of this degradation route and illustrate the different mass spectrometry workflows that were applied for elucidating molecular information. Overall, this review aims to stimulate the integrated use of multiple mass spectrometry approaches for analyzing complex biological systems.

Indexed as

HumansMass SpectrometryProteasome Endopeptidase ComplexUbiquitinationATP dependent 26S proteaseProteasome Endopeptidase Complex

Identifiers

PMID28100928
PMCPMC5238952

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.