Evidence map›Paper›PMID 34927332›Full record

ArticleAngewandte Chemie (International ed. in English)2022

A Membrane-Permeable and Immobilized Metal Affinity Chromatography (IMAC) Enrichable Cross-Linking Reagent to Advance In Vivo Cross-Linking Mass Spectrometry.

Pin-Lian Jiang, Cong Wang, Anne Diehl, Rosa Viner, Chris Etienne, Premchendar Nandhikonda, Leigh Foster, Ryan D Bomgarden, Fan Liu

Open access · hybridAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
5.9field-weighted citation impact, top 2% 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

36 citing papers in PubMed, 79 citations in OpenAlex.

  1. Article
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  3. Mapping the architecture of protein complexes inProceedings of the National Academy of Sciences of the United States of America · 2026
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  9. State-of-the-Art and Future Directions in Structural Proteomics.Molecular & cellular proteomics : MCP · 2025
    Review
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  11. Protein Secondary Structure Patterns in Short-Range Cross-Link Atlas.Angewandte Chemie (International ed. in English) · 2025
    Article
  12. Article
  13. Article
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  17. A Photo-Caged Cross-Linker for Identifying Protein-Protein Interactions.Chembiochem : a European journal of chemical biology · 2024
    Article
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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

9 authors at 2 institutions in 3 countries.

Pin-Lian JiangDepartment of Structural Biology, Leibniz-Forschungsinstitut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP), Campus Berlin-Buch, Robert-Roessle-Str. 10, 13125, Berlin, Germany.
Cong WangDepartment of Structural Biology, Leibniz-Forschungsinstitut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP), Campus Berlin-Buch, Robert-Roessle-Str. 10, 13125, Berlin, Germany.
Anne DiehlDepartment of Structural Biology, Leibniz-Forschungsinstitut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP), Campus Berlin-Buch, Robert-Roessle-Str. 10, 13125, Berlin, Germany.
Rosa VinerThermo Fisher Scientific, 355 River Oaks Pkwy, San Jose, CA 95134, USA.
Chris EtienneThermo Fisher Scientific, 3747N Meridian Rd, Rockford, IL 61101, USA.
Premchendar NandhikondaThermo Fisher Scientific, 3747N Meridian Rd, Rockford, IL 61101, USA.
Leigh FosterThermo Fisher Scientific, 3747N Meridian Rd, Rockford, IL 61101, USA.
Ryan D BomgardenThermo Fisher Scientific, 3747N Meridian Rd, Rockford, IL 61101, USA.
Fan LiuDepartment of Structural Biology, Leibniz-Forschungsinstitut für Molekulare Pharmakologie im Forschungsverbund Berlin e.V. (FMP), Campus Berlin-Buch, Robert-Roessle-Str. 10, 13125, Berlin, Germany.ORCID 0000-0002-2358-549X
Thermo Fisher Scientific (United States) · USLeibniz-Forschungsinstitut für Molekulare Pharmakologie · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cross-linking mass spectrometry (XL-MS) is an attractive method for the proteome-wide characterization of protein structures and interactions. Currently, the depth of in vivo XL-MS studies is lagging behind the established applications to cell lysates, because cross-linking reagents that can penetrate intact cells and strategies to enrich cross-linked peptides lack efficiency. To tackle these limitations, we have developed a phosphonate-containing cross-linker, tBu-PhoX, that efficiently permeates various biological membranes and can be robustly enriched using routine immobilized metal ion affinity chromatography. We have established a tBu-PhoX-based in vivo XL-MS approach that enables cross-links in intact human cells to be identified in high numbers with substantially reduced analysis time. Collectively, the developed cross-linker and XL-MS approach pave the way for the comprehensive XL-MS characterization of living systems.

Indexed as

ProteomeChromatography, AffinityCross-Linking ReagentsHumansImidazolesMass SpectrometryCross-Linking Reagentsimidazoleacetic acidImidazolesProteomeCross-linkingMass spectrometryProtein-protein interactionsProtein structuresProteomics

Identifiers

PMID34927332
PMCPMC9303249
OpenAlexW4200523156

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.