Evidence map›Paper›PMID 23917845›Full record

ReviewJournal of structural and functional genomics2013

Cross-linking and mass spectrometry methodologies to facilitate structural biology: finding a path through the maze.

Eric D Merkley, John R Cort, Joshua N Adkins

Abstract readReview
In one paragraph

Review in Journal of structural and functional genomics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.1field-weighted citation impact, top 15% 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

16 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Article
  6. ETD-Cleavable Linker for Confident Cross-linked Peptide Identifications.Journal of the American Society for Mass Spectrometry · 2019
    Article
  7. Article
  8. Review
  9. How to prove the existence of metabolons?Phytochemistry reviews : proceedings of the Phytochemical Society of Europe · 2018
    Review
  10. Cross-linking reveals laminin coiled-coil architecture.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. 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

3 authors at 1 institution in 1 country.

Eric D MerkleyMS K8-98, Biological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99352, USA. Eric.Merkley@pnnl.gov
John R Cort
Joshua N Adkins
Pacific Northwest National Laboratory · US

Funding

Consortia for High-Throughput-Enabled Structural Biology Partnerships (U01)U01GM094623 · NIGMS · BATTELLE PACIFIC NORTHWEST LABORATORIES · PI ADKINS, JOSHUA N. · 2010 to 2014
$5.2M
NIGMS NIH HHS GM094623NIGMS NIH HHS U01 GM094623
6 · The paper itself

Abstract

Multiprotein complexes, rather than individual proteins, make up a large part of the biological macromolecular machinery of a cell. Understanding the structure and organization of these complexes is critical to understanding cellular function. Chemical cross-linking coupled with mass spectrometry is emerging as a complementary technique to traditional structural biology methods and can provide low-resolution structural information for a multitude of purposes, such as distance constraints in computational modeling of protein complexes. In this review, we discuss the experimental considerations for successful application of chemical cross-linking-mass spectrometry in biological studies and highlight three examples of such studies from the recent literature. These examples (as well as many others) illustrate the utility of a chemical cross-linking-mass spectrometry approach in facilitating structural analysis of large and challenging complexes.

Indexed as

Adaptor Proteins, Signal TransducingCapsid ProteinsComputational BiologyCross-Linking ReagentsIntracellular Signaling Peptides and ProteinsLuteoviridaeMass SpectrometryModels, MolecularMolecular ChaperonesMultiprotein ComplexesProtein Phosphatase 2Adaptor Proteins, Signal TransducingCapsid ProteinsCross-Linking ReagentsIGBP1 protein, humanIntracellular Signaling Peptides and ProteinsMolecular ChaperonesMultiprotein ComplexesProtein Phosphatase 2

Identifiers

PMID23917845
PMCPMC3796448
OpenAlexW2043040060

What OpenQuestion holds

Textmetadata
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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.