Evidence map›Paper›PMID 38787738›Full record

ArticleJournal of the American Chemical Society2024

Chemoproteomics Identifies State-Dependent and Proteoform-Selective Caspase-2 Inhibitors.

José O Castellón, Samuel Ofori, Nikolas R Burton, Ashley R Julio, Alexandra C Turmon, Ernest Armenta, Carina Sandoval, Lisa M Boatner, Evan E Takayoshi, Marina Faragalla and 9 more

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing 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

14 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Chemoproteomics-EnabledJournal of the American Chemical Society · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

19 authors.

José O CastellónBiological Chemistry Department, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, United States.
Samuel OforiBiological Chemistry Department, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, United States.
Nikolas R BurtonBiological Chemistry Department, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, United States.
Ashley R JulioBiological Chemistry Department, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, United States.
Alexandra C TurmonBiological Chemistry Department, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, United States.
Ernest ArmentaBiological Chemistry Department, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, United States.
Carina SandovalDepartment of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, California 90095, United States.ORCID 0000-0002-4085-6810
Lisa M BoatnerBiological Chemistry Department, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, United States.ORCID 0000-0003-0757-4982
Evan E TakayoshiBiological Chemistry Department, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, United States.ORCID 0000-0002-6163-8708
Marina FaragallaBiological Chemistry Department, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, United States.
Cameron TaylorCalifornia NanoSystems Institute (CNSI), UCLA, Los Angeles, California 90095, United States.
Ann L ZhouBiological Chemistry Department, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, United States.
Ky TranBiological Chemistry Department, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, United States.
Jeremy ShekBiological Chemistry Department, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, United States.
Tianyang YanBiological Chemistry Department, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, United States.
Heta S DesaiBiological Chemistry Department, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, United States.
Oliver I FregosoDepartment of Microbiology, Immunology, and Molecular Genetics, University of California, Los Angeles, California 90095, United States.
Robert DamoiseauxJonsson Comprehensive Cancer Center, UCLA, Los Angeles, California 90095, United States.
Keriann M BackusBiological Chemistry Department, David Geffen School of Medicine, UCLA, Los Angeles, California 90095, United States.ORCID 0000-0001-8541-1404

Funding

Women's CancersP30CA016042 · NCI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Samuel Wheeler French · 1985 to 2026
$134.5M
UCLA NIGMS T32 Program AssessmentT32GM007185 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI TORRES, JORGE · 1985 to 2020
$21.7M
Systems in Integrative BiologyT32GM008185 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI CHOU, TOM · 1987 to 2022
$4.6M
A systems-level approach to decipher the protein interactome.DP2GM146246 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI BACKUS, KERIANN MARIE · 2021 to 2024
$2.3M
Defining the regulation of double-strand DNA break repair by HIV VprR01AI147837 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI FREGOSO, OLIVER I · 2019 to 2023
$1.9M
NCI NIH HHS P30 CA016042NIAID NIH HHS R01 AI147837NIGMS NIH HHS DP2 GM146246NIGMS NIH HHS T32 GM007185NIGMS NIH HHS T32 GM008185
6 · The paper itself

Abstract

Caspases are a highly conserved family of cysteine-aspartyl proteases known for their essential roles in regulating apoptosis, inflammation, cell differentiation, and proliferation. Complementary to genetic approaches, small-molecule probes have emerged as useful tools for modulating caspase activity. However, due to the high sequence and structure homology of all 12 human caspases, achieving selectivity remains a central challenge for caspase-directed small-molecule inhibitor development efforts. Here, using mass spectrometry-based chemoproteomics, we first identify a highly reactive noncatalytic cysteine that is unique to caspase-2. By combining both gel-based activity-based protein profiling (ABPP) and a

Indexed as

Caspase 2Caspase InhibitorsProteomicsCysteine EndopeptidasesHumansMolecular StructureCASP2 protein, humanCaspase 2Caspase InhibitorsCysteine Endopeptidases

Identifiers

PMID38787738
PMCPMC11832190

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.