Evidence map›Paper›PMID 22610688›Full record

ReviewProteomics2012

In vivo protein complex topologies: sights through a cross-linking lens.

James E Bruce

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 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing 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

38 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Improving Identification ofMolecular & cellular proteomics : MCP · 2020
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. On the Reproducibility of Label-Free Quantitative Cross-Linking/Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2018
    Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

1 author.

James E BruceDepartment of Genome Sciences, University of Washington, Seattle, WA 98109, USA. jimbruce@u.washington.edu

Funding

Quantitation of protein interactions in cancer cellsR01GM086688 · NIGMS · UNIVERSITY OF WASHINGTON · PI BRUCE, JAMES EDWARD · 2009 to 2019
$4.2M
Instrumentation Development: MS Array for Quantitative ProteomicsR01GM097112 · NIGMS · UNIVERSITY OF WASHINGTON · PI BRUCE, JAMES EDWARD · 2011 to 2020
$2.9M
Investigating bacterial-host interactions driving CF Pulmonary ExacerbationsR01HL110879 · NHLBI · UNIVERSITY OF WASHINGTON · PI BRUCE, JAMES EDWARD, SINGH, PRADEEP K · 2011 to 2014
$1.6M
New Technology for Protein Interaction Network and Topology AnalysisR01RR023334 · NCRR · WASHINGTON STATE UNIVERSITY · PI BRUCE, JAMES EDWARD · 2007 to 2009
$750k
NCRR NIH HHS 5R01RR023334NCRR NIH HHS R01 RR023334NHLBI NIH HHS 1R01HL110879NHLBI NIH HHS R01 HL110879NIGMS NIH HHS 1R01GM097112NIGMS NIH HHS 5R01GM086688NIGMS NIH HHS R01 GM086688NIGMS NIH HHS R01 GM097112
6 · The paper itself

Abstract

Proteins are a remarkable class of molecules that exhibit wide diversity of shapes or topological features that underpin protein interactions and give rise to biological function. In addition to quantitation of abundance levels of proteins in biological systems under a variety of conditions, the field of proteome research has as a primary mission the assignment of function for proteins and if possible, illumination of factors that enable function. For many years, chemical cross-linking methods have been used to provide structural data on single purified proteins and purified protein complexes. However, these methods also offer the alluring possibility to extend capabilities to complex biological samples such as cell lysates or intact living cells where proteins may exhibit native topological features that do not exist in purified form. Recent efforts are beginning to provide glimpses of protein complexes and topologies in cells that suggest continued development will yield novel capabilities to view functional topological features of many proteins and complexes as they exist in cells, tissues, or other complex samples. This review will describe rationale, challenges, and a few success stories along the path of development of cross-linking technologies for measurement of in vivo protein interaction topologies.

Indexed as

Cross-Linking ReagentsProtein ConformationProtein Interaction MappingProteinsProteomicsCross-Linking ReagentsProteins

Identifiers

PMID22610688
PMCPMC3654877

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.