Evidence map›Paper›PMID 23354917›Full record

ArticleMolecular & cellular proteomics : MCP2013

Protein interactions, post-translational modifications and topologies in human cells.

Juan D Chavez, Chad R Weisbrod, Chunxiang Zheng, Jimmy K Eng, James E Bruce

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
5.2field-weighted citation impact, top 4% of its field
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

70 citing papers in PubMed, 131 citations in OpenAlex.

  1. Review
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  9. Article
  10. Review
  11. Review
  12. An optimized protocol forSTAR protocols · 2022
    Article
  13. Review
  14. Article
  15. Overview of protein posttranslational modifications in Arthropoda venoms.The journal of venomous animals and toxins including tropical diseases · 2022
    Review
  16. MS Annika: A New Cross-Linking Search Engine.Journal of proteome research · 2021
    Article
  17. Crosslinking mass spectrometry: A link between structural biology and systems biology.Protein science : a publication of the Protein Society · 2021
    Review
  18. Article
  19. Review
  20. Article

10 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

Juan D ChavezDepartment of Genome Science, University of Washington, Seattle, Washington 98109, USA.
Chad R Weisbrod
Chunxiang Zheng
Jimmy K Eng
James E Bruce
University of Washington · US

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
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 RR025107NHLBI 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

The unique and remarkable physicochemical properties of protein surface topologies give rise to highly specific biomolecular interactions, which form the framework through which living systems are able to carry out their vast array of functions. Technological limitations undermine efforts to probe protein structures and interactions within unperturbed living systems on a large scale. Rapid chemical stabilization of proteins and protein complexes through chemical cross-linking offers the alluring possibility to study details of the protein structure to function relationships as they exist within living cells. Here we apply the latest technological advances in chemical cross-linking combined with mass spectrometry to study protein topologies and interactions from living human cells identifying a total of 368 cross-links. These include cross-links from all major cellular compartments including membrane, cytosolic and nuclear proteins. Intraprotein and interprotein cross-links were also observed for core histone proteins, including several cross-links containing post-translational modifications which are known histone marks conferring distinct epigenetic functions. Excitingly, these results demonstrate the applicability of cross-linking to make direct topological measurements on post-translationally modified proteins. The results presented here provide new details on the structures of known multi-protein complexes as well as evidence for new protein-protein interactions.

Indexed as

Protein Interaction MappingProtein Processing, Post-TranslationalAmino Acid MotifsChromatography, AffinityChromatography, Ion ExchangeHeLa CellsHumansProtein Interaction Domains and MotifsProtein Interaction MapsProteomeProteome

Identifiers

PMID23354917
PMCPMC3650351
OpenAlexW1966891407

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.