Evidence map›Paper›PMID 35235311›Full record

ArticleAnalytical chemistry2022

Two-Dimensional Fractionation Method for Proteome-Wide Cross-Linking Mass Spectrometry Analysis.

Fenglong Jiao, Clinton Yu, Andrew Wheat, Xiaorong Wang, Scott D Rychnovsky, Lan Huang

Abstract read
In one paragraph

Article in Analytical chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing 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

32 citing papers in PubMed.

  1. Review
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  9. Article
  10. Review
  11. Article
  12. Methods for the Investigation of Protein-Ligands Interactions.Advances in experimental medicine and biology · 2026
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Mapping amBio · 2025
    Article
  20. 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

6 authors.

Fenglong JiaoDepartment of Physiology & Biophysics, University of California, Irvine, Irvine, California 92694, United States.
Clinton YuDepartment of Physiology & Biophysics, University of California, Irvine, Irvine, California 92694, United States.
Andrew WheatDepartment of Physiology & Biophysics, University of California, Irvine, Irvine, California 92694, United States.
Xiaorong WangDepartment of Physiology & Biophysics, University of California, Irvine, Irvine, California 92694, United States.
Scott D RychnovskyDepartment of Chemistry, University of California, Irvine, Irvine, California 92694, United States.ORCID 0000-0002-7223-4389
Lan HuangDepartment of Physiology & Biophysics, University of California, Irvine, Irvine, California 92694, United States.ORCID 0000-0002-3140-4687

Funding

Univ.of Calif., Irvine Cancer Center Support GrantP30CA062203 · NCI · UNIVERSITY OF CALIFORNIA-IRVINE · PI Melanie Funes · 1994 to 2026
$57.9M
Proteomics of the Proteasome Interacting NetworksR01GM074830 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI HUANG, LAN · 2005 to 2022
$6.1M
Structural dynamics and function of the COP9 signalosomeR01GM130144 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI HUANG, LAN · 2018 to 2021
$1.2M
NCI NIH HHS P30 CA062203NIGMS NIH HHS R01 GM074830NIGMS NIH HHS R01 GM130144
6 · The paper itself

Abstract

Cross-linking mass spectrometry (XL-MS) is an emergent technology for studying protein-protein interactions (PPIs) and elucidating architectures of protein complexes. The development of various MS-cleavable cross-linkers has facilitated the identification of cross-linked peptides, enabling XL-MS studies at the systems level. However, the scope and depth of cellular networks revealed by current XL-MS technologies remain limited. Due to the inherently broad dynamic range and complexity of proteomes, interference from highly abundant proteins impedes the identification of low-abundance cross-linked peptides in complex samples. Thus, peptide enrichment prior to MS analysis is necessary to enhance cross-link identification for proteome-wide studies. Although chromatographic techniques including size exclusion (SEC) and strong cation exchange (SCX) have been successful in isolating cross-linked peptides, new fractionation methods are still needed to further improve the depth of PPI mapping. Here, we present a two-dimensional (2D) separation strategy by integrating peptide SEC with tip-based high pH reverse-phase (HpHt) fractionation to expand the coverage of proteome-wide XL-MS analyses. Combined with the MS-cleavable cross-linker DSSO, we have successfully mapped

Indexed as

Mass SpectrometryPeptidesProteomeChemical FractionationCross-Linking ReagentsHEK293 CellsHumansCross-Linking ReagentsPeptidesProteome

Identifiers

PMID35235311
PMCPMC9056026

What OpenQuestion holds

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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.