Evidence map›Paper›PMID 22611037›Full record

ReviewProteomics2012

Integrating mass spectrometry of intact protein complexes into structural proteomics.

Suk-Joon Hyung, Brandon T Ruotolo

Abstract readReview
In one paragraph

Review in Proteomics, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing 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

46 citing papers in PubMed.

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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.

Suk-Joon HyungDepartment of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.
Brandon T Ruotolo

Funding

Next-generation Mass Spectrometry Technologies for Integrated Structural Proteomics- RenewalR01GM095832 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RUOTOLO, BRANDON T · 2011 to 2024
$5.8M
NIGMS NIH HHS 1-R01-GM-095832-01NIGMS NIH HHS R01 GM095832
6 · The paper itself

Abstract

MS analysis of intact protein complexes has emerged as an established technology for assessing the composition and connectivity within dynamic, heterogeneous multiprotein complexes at low concentrations and in the context of mixtures. As this technology continues to move forward, one of the main challenges is to integrate the information content of such intact protein complex measurements with other MS approaches in structural biology. Methods such as H/D exchange, oxidative foot-printing, chemical cross-linking, affinity purification, and ion mobility separation add complementary information that allows access to every level of protein structure and organization. Here, we survey the structural information that can be retrieved by such experiments, demonstrate the applicability of integrative MS approaches in structural proteomics, and look to the future to explore upcoming innovations in this rapidly advancing area.

Indexed as

AnimalsHigh-Throughput Screening AssaysHumansMass SpectrometryMultiprotein ComplexesProteomicsSystems BiologyMultiprotein Complexes

Identifiers

PMID22611037
PMCPMC3895494

What OpenQuestion holds

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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.