Evidence map›Paper›PMID 37236440›Full record

ReviewMolecular & cellular proteomics : MCP2023

In-Depth Characterization of Apoptosis N-Terminome Reveals a Link Between Caspase-3 Cleavage and Posttranslational N-Terminal Acetylation.

Rawad Hanna, Andrey Rozenberg, Layla Saied, Daniel Ben-Yosef, Tali Lavy, Oded Kleifeld

Open access · goldAbstract readReview
In one paragraph

Review in Molecular & cellular proteomics : MCP, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed, 1 pooled it
5.5field-weighted citation impact, top 4% 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

15 citing papers in PubMed, 1 synthesis or guideline pooled it, 24 citations in OpenAlex.

  1. Pooled it
  2. Caspase-mediated cleavage events hidden by secondary proteolysis during apoptosis.Protein science : a publication of the Protein Society · 2026
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  13. StageTip: a little giant unveiling the potential of mass spectrometry-based proteomics.Analytical sciences : the international journal of the Japan Society for Analytical Chemistry · 2025
    Review
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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.

Rawad HannaFaculty of Biology, Technion-Israel Institute of Technology, Haifa, Israel.
Andrey RozenbergFaculty of Biology, Technion-Israel Institute of Technology, Haifa, Israel.
Layla SaiedFaculty of Biology, Technion-Israel Institute of Technology, Haifa, Israel.
Daniel Ben-YosefFaculty of Biology, Technion-Israel Institute of Technology, Haifa, Israel.
Tali LavyFaculty of Biology, Technion-Israel Institute of Technology, Haifa, Israel.
Oded KleifeldFaculty of Biology, Technion-Israel Institute of Technology, Haifa, Israel. Electronic address: okleifeld@technion.ac.il.
Technion – Israel Institute of Technology · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The N termini of proteins contain information about their biochemical properties and functions. These N termini can be processed by proteases and can undergo other co- or posttranslational modifications. We have developed LATE (LysN Amino Terminal Enrichment), a method that uses selective chemical derivatization of α-amines to isolate the N-terminal peptides, in order to improve N-terminome identification in conjunction with other enrichment strategies. We applied LATE alongside another N-terminomic method to study caspase-3-mediated proteolysis both in vitro and during apoptosis in cells. This has enabled us to identify many unreported caspase-3 cleavages, some of which cannot be identified by other methods. Moreover, we have found direct evidence that neo-N-termini generated by caspase-3 cleavage can be further modified by Nt-acetylation. Some of these neo-Nt-acetylation events occur in the early phase of the apoptotic process and may have a role in translation inhibition. This has provided a comprehensive overview of the caspase-3 degradome and has uncovered previously unrecognized cross talk between posttranslational Nt-acetylation and caspase proteolytic pathways.

Indexed as

Caspase 3Protein Processing, Post-TranslationalAcetylationApoptosisPeptide HydrolasesProteolysisCaspase 3Peptide Hydrolasescaspase-3degradomicsLysNN-terminal acetylationN-terminomicspeptidyl-Lys metalloendopeptidase

Identifiers

PMID37236440
PMCPMC10362333
OpenAlexW4377965504

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.