Evidence map›Paper›PMID 19412923›Full record

ArticleRapid communications in mass spectrometry : RCM2009

Synthesis of biotin-tagged chemical cross-linkers and their applications for mass spectrometry.

Sebyung Kang, Liyuan Mou, Jason Lanman, Sadanandan Velu, Wayne J Brouillette, Peter E Prevelige

Abstract readEvaluation Study
In one paragraph

Article in Rapid communications in mass spectrometry : RCM, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. An optimized protocol forSTAR protocols · 2022
    Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Development of Large-scale Cross-linking Mass Spectrometry.Molecular & cellular proteomics : MCP · 2018
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Quaternary diamines as mass spectrometry cleavable crosslinkers for protein interactions.Journal of the American Society for Mass Spectrometry · 2012
    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

6 authors.

Sebyung KangDepartment of Microbiology, University of Alabama at Birmingham, Birmingham, Alabama 35294-2170, USA.
Liyuan Mou
Jason Lanman
Sadanandan Velu
Wayne J Brouillette
Peter E Prevelige

Funding

BIOPHYSICAL STUDIES OF HIV ASSEMBLY AND MATURATIONR01AI044626 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI PREVELIGE, PETER E. · 2000 to 2010
$2.7M
Identification of Subunit Interfaces in Protein ComplexR21AI053821 · NIAID · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI PREVELIGE, PETER E. · 2002 to 2003
$423k
NIAID NIH HHS AI44626NIAID NIH HHS AI53821NIAID NIH HHS R01 AI044626NIAID NIH HHS R21 AI053821
6 · The paper itself

Abstract

Chemical cross-linking combined with mass spectrometry (MS) has been used to elucidate protein structures and protein-protein interactions. However, heterogeneity of the samples and the relatively low abundance of cross-linked peptides make this approach challenging. As an effort to overcome this hurdle, we have synthesized lysine-reactive homobifunctional cross-linkers with the biotin in the middle of the linker and used them to enrich cross-linked peptides. The reaction of biotin-tagged cross-linkers with purified HIV-1 CA resulted in the formation of hanging and intramolecular cross-links. The peptides modified with biotinylated cross-linkers were effectively enriched and recovered using a streptavidin-coated plate and MS-friendly buffers. The enrichment of modified peptides and removal of the dominantly unmodified peptides simplify mass spectra and their analyses. The combination of the high mass accuracy of Fourier transform ion cyclotron resonance (FT-ICR) MS and the tandem mass spectrometric (MS/MS) capability of the linear ion trap allows us to unambiguously identify the cross-linking sites and additional modification, such as oxidation.

Indexed as

BiotinCapsid ProteinsCross-Linking ReagentsHIV-1Spectroscopy, Fourier Transform InfraredTandem Mass SpectrometryBiotinCapsid ProteinsCross-Linking Reagents

Identifiers

PMID19412923
PMCPMC2748246

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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.