Evidence map›Paper›PMID 36652389›Full record

ArticleAnalytical chemistry2023

Exploring an Alternative Cysteine-Reactive Chemistry to Enable Proteome-Wide PPI Analysis by Cross-Linking Mass Spectrometry.

Fenglong Jiao, Leah J Salituro, Clinton Yu, Craig B Gutierrez, Scott D Rychnovsky, Lan Huang

Open access · greenAbstract read
In one paragraph

Article in Analytical chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

13 citing papers in PubMed, 18 citations in OpenAlex.

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  9. Mechanism of autocatalytic activation during proteasome assembly.Nature structural & molecular biology · 2024
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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 at 1 institution in 1 country.

Fenglong JiaoDepartment of Physiology and Biophysics, University of California, Irvine, Irvine, California 92697, United States.
Leah J SalituroDepartment of Chemistry, University of California, Irvine, Irvine, California 92697, United States.
Clinton YuDepartment of Physiology and Biophysics, University of California, Irvine, Irvine, California 92697, United States.
Craig B GutierrezDepartment of Physiology and Biophysics, University of California, Irvine, Irvine, California 92697, United States.
Scott D RychnovskyDepartment of Chemistry, University of California, Irvine, Irvine, California 92697, United States.ORCID 0000-0002-7223-4389
Lan HuangDepartment of Physiology and Biophysics, University of California, Irvine, Irvine, California 92697, United States.ORCID 0000-0002-3140-4687
University of California, Irvine · US

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
Supplement: Advancing Proteomics Technologies to Decipher the Ubiquitin-Proteasome SystemR35GM145249 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI Lan Huang · 2022 to 2026
$3.2M
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 GM130144NIGMS NIH HHS R35 GM145249
6 · The paper itself

Abstract

The development of MS-cleavable cross-linking mass spectrometry (XL-MS) has enabled the effective capture and identification of endogenous protein-protein interactions (PPIs) and their residue contacts at the global scale without cell engineering. So far, only lysine-reactive cross-linkers have been successfully applied for proteome-wide PPI profiling. However, lysine cross-linkers alone cannot uncover the complete PPI map in cells. Previously, we have developed a maleimide-based cysteine-reactive MS-cleavable cross-linker (bismaleimide sulfoxide (BMSO)) that is effective for mapping PPIs of protein complexes to yield interaction contacts complementary to lysine-reactive reagents. While successful, the hydrolysis and limited selectivity of maleimides at physiological pH make their applications in proteome-wide XL-MS challenging. To enable global PPI mapping, we have explored an alternative cysteine-labeling chemistry and thus designed and synthesized a sulfoxide-containing MS-cleavable haloacetamide-based cross-linker, Dibromoacetamide sulfoxide (DBrASO). Our results have demonstrated that DBrASO cross-linked peptides display the same fragmentation characteristics as other sulfoxide-containing MS-cleavable cross-linkers, permitting their unambiguous identification by MS

Indexed as

CysteineProteomeCross-Linking ReagentsHEK293 CellsHumansLysineMass SpectrometryPeptidesSulfoxidesCross-Linking ReagentsCysteineLysinePeptidesProteomeSulfoxides

Identifiers

PMID36652389
PMCPMC10284117
OpenAlexW4317358705

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.