Evidence map›Paper›PMID 21697552›Full record

ArticleMolecular & cellular proteomics : MCP2011

Cross-linking measurements of in vivo protein complex topologies.

Chunxiang Zheng, Li Yang, Michael R Hoopmann, Jimmy K Eng, Xiaoting Tang, Chad R Weisbrod, James E Bruce

Abstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing 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

55 citing papers in PubMed.

  1. Article
  2. Review
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  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. The First MS-Cleavable, Photo-Thiol-Reactive Cross-Linker for Protein Structural Studies.Journal of the American Society for Mass Spectrometry · 2019
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Review
  19. Mitochondrial protein interactome elucidated by chemical cross-linking mass spectrometry.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  20. Review
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

7 authors.

Chunxiang ZhengDepartment of Chemistry, Washington State University, Pullman, WA 99164, USA.
Li Yang
Michael R Hoopmann
Jimmy K Eng
Xiaoting Tang
Chad R Weisbrod
James E Bruce

Funding

Quantitation of protein interactions in cancer cellsR01GM086688 · NIGMS · UNIVERSITY OF WASHINGTON · PI BRUCE, JAMES EDWARD · 2009 to 2019
$4.2M
An LC-FTICR Mass Spectrometer for Proteomics and Metabolomics ResearchS10RR025107 · NCRR · UNIVERSITY OF WASHINGTON · PI BRUCE, JAMES EDWARD · 2008 to 2008
$990k
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 7S10RR025107NCRR NIH HHS R01 RR023334NCRR NIH HHS S10 RR025107NIGMS NIH HHS 5R01GM086688NIGMS NIH HHS R01 GM086688
6 · The paper itself

Abstract

Identification and measurement of in vivo protein interactions pose critical challenges in the goal to understand biological systems. The measurement of structures and topologies of proteins and protein complexes as they exist in cells is particularly challenging, yet critically important to improve understanding of biological function because proteins exert their intended function only through the structures and interactions they exhibit in vivo. In the present study, protein interactions in E. coli cells were identified in our unbiased cross-linking approach, yielding the first in vivo topological data on many interactions and the largest set of identified in vivo cross-linked peptides produced to date. These data show excellent agreement with protein and complex crystal structures where available. Furthermore, our unbiased data provide novel in vivo topological information that can impact understanding of biological function, even for cases where high resolution structures are not yet available.

Indexed as

Binding SitesCation Exchange ResinsChromatography, LiquidCross-Linking ReagentsEscherichia coliHumansMass SpectrometryMolecular ConformationMultiprotein ComplexesPeptidesProtein BindingProtein Interaction Domains and MotifsProtein Interaction MapsCation Exchange ResinsCross-Linking ReagentsMultiprotein ComplexesPeptides

Identifiers

PMID21697552
PMCPMC3205858

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.