Evidence map›Paper›PMID 22131227›Full record

ArticleJournal of the American Society for Mass Spectrometry2012

Quaternary diamines as mass spectrometry cleavable crosslinkers for protein interactions.

Billy Clifford-Nunn, H D Hollis Showalter, Philip C Andrews

Abstract read
In one paragraph

Article in Journal of the American Society for Mass Spectrometry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.4field-weighted citation impact, top 13% 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

27 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. All-in-One Pseudo-MSJournal of the American Society for Mass Spectrometry · 2023
    Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. ETD-Cleavable Linker for Confident Cross-linked Peptide Identifications.Journal of the American Society for Mass Spectrometry · 2019
    Article
  9. Altered Domain Structure of the Prion Protein Caused by CuStructure (London, England : 1993) · 2019
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
  15. Cytosolic Ku70 regulates Bax-mediated cell death.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
    Article
  16. Revealing Higher Order Protein Structure Using Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2016
    Article
  17. Article
  18. The neuronal porosome complex in health and disease.Experimental biology and medicine (Maywood, N.J.) · 2016
    Review
  19. 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

3 authors at 1 institution in 1 country.

Billy Clifford-NunnDepartment of Chemistry, University of Michigan, 930 North University Avenue, Ann Arbor, MI, USA.
H D Hollis Showalter
Philip C Andrews
University of Michigan–Ann Arbor · US

Funding

UNDERSTANDING THE PATHOGENESIS OF CAMPYLOBACTER JEJUNIP41RR018627 · NCRR · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI FINLEY, RUSSELL L · 2003 to 2007
$12.4M
Next-generation Mass Spectrometry Technologies for Integrated Structural Proteomics- RenewalR01GM095832 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI RUOTOLO, BRANDON T · 2011 to 2024
$5.8M
NCRR NIH HHS 1P41RR018627NCRR NIH HHS P41 RR018627NIGMS NIH HHS R01 GM095832NIGMS NIH HHS R01GM09583201.
6 · The paper itself

Abstract

Mapping protein interactions and their dynamics is crucial to defining physiologic states, building effective models for understanding cell function, and to allow more effective targeting of new drugs. Crosslinking studies can estimate the proximity of proteins, determine sites of protein-protein interactions, and have the potential to provide a snapshot of dynamic interactions by covalently locking them in place for analysis. Several major challenges are associated with the use of crosslinkers in mass spectrometry, particularly in complex mixtures. We describe the synthesis and characterization of a MS-cleavable crosslinker containing cyclic amines, which address some of these challenges. The DC4 crosslinker contains two intrinsic positive charges, which allow crosslinked peptides to fragment into their component peptides by collision-induced dissociation (CID) or in-source decay. Initial fragmentation events result in cleavage on either side of the positive charges so crosslinked peptides are identified as pairs of ions separated by defined masses. The structures of the component peptides can then be robustly determined by MS(3) because their fragmentation products rearrange to generate a mobile proton. The DC4 crosslinking reagent is stable to storage, highly reactive, highly soluble (1 M solutions), quite labile to CID, and MS(3) results in productive backbone fragmentation.

Indexed as

Amino Acid SequenceCross-Linking ReagentsDiaminesFructose-Bisphosphate AldolaseIonsModels, MolecularMolecular Sequence DataPeptidesProtein Interaction MappingProteinsTandem Mass SpectrometryCross-Linking ReagentsDiaminesFructose-Bisphosphate AldolaseIonsPeptidesProteins

Identifiers

PMID22131227
PMCPMC3573217
OpenAlexW1983743164

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.