Evidence map›Paper›PMID 22339618›Full record

ArticleAnalytical chemistry2012

Designer reagents for mass spectrometry-based proteomics: clickable cross-linkers for elucidation of protein structures and interactions.

Chang Ho Sohn, Heather D Agnew, J Eugene Lee, Michael J Sweredoski, Robert L J Graham, Geoffrey T Smith, Sonja Hess, Gregg Czerwieniec, Joseph A Loo, James R Heath and 2 more

Open access · greenAbstract read
In one paragraph

Article in Analytical chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

17 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Development of Large-scale Cross-linking Mass Spectrometry.Molecular & cellular proteomics : MCP · 2018
    Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Electrospray ionization-induced protein unfolding.Journal of the American Society for Mass Spectrometry · 2012
    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

12 authors at 2 institutions in 1 country.

Chang Ho SohnDivision of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125, United States.
Heather D Agnew
J Eugene Lee
Michael J Sweredoski
Robert L J Graham
Geoffrey T Smith
Sonja Hess
Gregg Czerwieniec
Joseph A Loo
James R Heath
Raymond J Deshaies
J L Beauchamp
California Institute of Technology · USUniversity of California, Los Angeles · US

Funding

UCLA Institute for Molecular Medicine (IMED) CoreU54CA151819 · NCI · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI HEATH, JAMES R. · 2010 to 2014
$12.1M
Regulation of cullin - RING ubiquitin ligasesR01GM065997 · NIGMS · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI DESHAIES, RAYMOND J · 2002 to 2018
$4.5M
UV Laser for Photodissociation-Mass Spectrometry of Proteins and Protein ComplexesR01GM103479 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LOO, JOSEPH A · 2012 to 2021
$3.2M
Mass Spectrometry of Protein AssembliesR01RR020004 · NCRR · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI LOO, JOSEPH A · 2004 to 2011
$2.7M
Proteome-wide protein Identification Facilitated by in Vivo Cross-linkingF32CA138126 · NCI · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI LEE, JINHWAN EUGENE · 2009 to 2011
$162k
NCI NIH HHS CA138126NCI NIH HHS F32 CA138126NCI NIH HHS U54 CA151819NCI NIH HHS U54CA151819-01NCRR NIH HHS R01 RR020004NCRR NIH HHS RR 20004NIGMS NIH HHS R01 GM065997NIGMS NIH HHS R01 GM103479
6 · The paper itself

Abstract

We present novel homobifunctional amine-reactive clickable cross-linkers (CXLs) for investigation of three-dimensional protein structures and protein-protein interactions (PPIs). CXLs afford consolidated advantages not previously available in a simple cross-linker, including (1) their small size and cationic nature at physiological pH, resulting in good water solubility and cell-permeability, (2) an alkyne group for bio-orthogonal conjugation to affinity tags via the click reaction for enrichment of cross-linked peptides, (3) a nucleophilic displacement reaction involving the 1,2,3-triazole ring formed in the click reaction, yielding a lock-mass reporter ion for only clicked peptides, and (4) higher charge states of cross-linked peptides in the gas-phase for augmented electron transfer dissociation (ETD) yields. Ubiquitin, a lysine-abundant protein, is used as a model system to demonstrate structural studies using CXLs. To validate the sensitivity of our approach, biotin-azide labeling and subsequent enrichment of cross-linked peptides are performed for cross-linked ubiquitin digests mixed with yeast cell lysates. Cross-linked peptides are detected and identified by collision induced dissociation (CID) and ETD with linear quadrupole ion trap (LTQ)-Fourier transform ion cyclotron resonance (FTICR) and LTQ-Orbitrap mass spectrometers. The application of CXLs to more complex systems (e.g., in vivo cross-linking) is illustrated by Western blot detection of Cul1 complexes including known binders, Cand1 and Skp2, in HEK 293 cells, confirming good water solubility and cell-permeability.

Indexed as

Amino Acid SequenceAvidinChromatography, AffinityCross-Linking ReagentsHEK293 CellsHumansMass SpectrometryModels, MolecularMolecular Sequence DataPeptidesProteinsProteomicsUbiquitinAvidinCross-Linking ReagentsPeptidesProteinsUbiquitin

Identifiers

PMID22339618
PMCPMC3310289
OpenAlexW2154565582

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.