Evidence map›Paper›PMID 29104064›Full record

ArticleCell chemical biology2018

A Chemical Proteomics Approach to Reveal Direct Protein-Protein Interactions in Living Cells.

Ralph E Kleiner, Lisa E Hang, Kelly R Molloy, Brian T Chait, Tarun M Kapoor

Open access · bronzeAbstract read
In one paragraph

Article in Cell chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
3.1field-weighted citation impact, top 7% 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

43 citing papers in PubMed, 77 citations in OpenAlex.

  1. Review
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  4. A chemical epigenetic tool to probe site-specific DNA-binding protein complexes.Proceedings of the National Academy of Sciences of the United States of America · 2025
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 1 institution in 1 country.

Ralph E KleinerLaboratory of Chemistry and Cell Biology, The Rockefeller University, New York, NY 10065, USA.
Lisa E HangLaboratory of Chemistry and Cell Biology, The Rockefeller University, New York, NY 10065, USA.
Kelly R MolloyLaboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, NY 10065, USA.
Brian T ChaitLaboratory of Mass Spectrometry and Gaseous Ion Chemistry, The Rockefeller University, New York, NY 10065, USA.
Tarun M KapoorLaboratory of Chemistry and Cell Biology, The Rockefeller University, New York, NY 10065, USA. Electronic address: kapoor@rockefeller.edu.
Rockefeller University · US

Funding

TR&D Project 4. The Imaging Stage: Multiscale Spatiotemporal Modeling of Macromolecular Systems in Cellular NeighborhoodsP41GM109824 · NIGMS · ROCKEFELLER UNIVERSITY · PI ROUT, MICHAEL P · 2014 to 2023
$18.8M
National Resource for Mass Spectrom of Biological MacromoleculesP41GM103314 · NIGMS · ROCKEFELLER UNIVERSITY · PI CHAIT, BRIAN T · 2012 to 2017
$9.9M
Mechanisms of Cell Regulation and TransformationT32CA009673 · NCI · ROCKEFELLER UNIVERSITY · PI KAPOOR, TARUN M. · 1991 to 2018
$7.0M
Studying chromosome function using chemical biologyR01GM098579 · NIGMS · ROCKEFELLER UNIVERSITY · PI KAPOOR, TARUN M. · 2011 to 2018
$3.3M
NCI NIH HHS T32 CA009673NIGMS NIH HHS P41 GM103314NIGMS NIH HHS P41 GM109824NIGMS NIH HHS R01 GM098579
6 · The paper itself

Abstract

Protein-protein interactions mediate essential cellular processes, however the detection of native interactions is challenging since they are often low affinity and context dependent. Here, we develop a chemical proteomics approach in vivo CLASPI [iCLASPI] (in vivo crosslinking-assisted and stable isotope labeling by amino acids in cell culture [SILAC]-based protein identification) relying upon photo-crosslinking, amber suppression, and SILAC-based quantitative proteomics to profile context-dependent protein-protein interactions in living cells. First, we use iCLASPI to profile in vivo binding partners of the N-terminal tails of soluble histone H3 or H4. We identify known histone chaperones and modifying proteins, thereby validating our approach, and find an interaction between soluble histone H3 and UBR7, an E3 ubiquitin ligase, mediated by UBR7's PHD domain. Furthermore, we apply iCLASPI to profile the context-dependent protein-protein interactions of chromatin-associated histone H3 at different cell-cycle stages, and identify ANP32A as a mitosis-specific interactor. Our results demonstrate that the iCLASPI approach can provide a general strategy for identifying native, context-dependent direct protein-protein interactions using photo-crosslinking and quantitative proteomics.

Indexed as

ProteomicsAmino AcidsAnimalsCell Culture TechniquesCell CycleCell LineChromatinCross-Linking ReagentsHEK293 CellsHistonesHumansIsotope LabelingMiceProtein BindingUbiquitin-Protein LigasesAmino AcidsChromatinCross-Linking ReagentsHistonesUbiquitin-Protein Ligaseschemical proteomicschromatinprotein-protein interactions

Identifiers

PMID29104064
PMCPMC5775914
OpenAlexW2765673456

What OpenQuestion holds

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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.