Evidence map›Paper›PMID 24457955›Full record

ReviewCell death & disease2014

Modulation of apoptosis sensitivity through the interplay with autophagic and proteasomal degradation pathways.

M E Delgado, L Dyck, M A Laussmann, M Rehm

Open access · goldAbstract readReview
In one paragraph

Review in Cell death & disease, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
4.3field-weighted citation impact, top 6% 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

25 citing papers in PubMed, 48 citations in OpenAlex.

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  18. Crosstalk Between Mammalian Autophagy and the Ubiquitin-Proteasome System.Frontiers in cell and developmental biology · 2018
    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

4 authors at 1 institution in 1 country.

M E Delgado1] Centre for Systems Medicine, Dublin 2, Ireland [2] Department of Physiology & Medical Physics, Royal College of Surgeons in Ireland, Dublin 2, Ireland.
L Dyck1] Centre for Systems Medicine, Dublin 2, Ireland [2] Department of Physiology & Medical Physics, Royal College of Surgeons in Ireland, Dublin 2, Ireland.
M A Laussmann1] Centre for Systems Medicine, Dublin 2, Ireland [2] Department of Physiology & Medical Physics, Royal College of Surgeons in Ireland, Dublin 2, Ireland.
M Rehm1] Centre for Systems Medicine, Dublin 2, Ireland [2] Department of Physiology & Medical Physics, Royal College of Surgeons in Ireland, Dublin 2, Ireland.ORCID 0000000161499261
Royal College of Surgeons in Ireland · IE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Autophagic and proteasomal degradation constitute the major cellular proteolysis pathways. Their physiological and pathophysiological adaptation and perturbation modulates the relative abundance of apoptosis-transducing proteins and thereby can positively or negatively adjust cell death susceptibility. In addition to balancing protein expression amounts, components of the autophagic and proteasomal degradation machineries directly interact with and co-regulate apoptosis signal transduction. The influence of autophagic and proteasomal activity on apoptosis susceptibility is now rapidly gaining more attention as a significant modulator of cell death signalling in the context of human health and disease. Here we present a concise and critical overview of the latest knowledge on the molecular interplay between apoptosis signalling, autophagy and proteasomal protein degradation. We highlight that these three pathways constitute an intricate signalling triangle that can govern and modulate cell fate decisions between death and survival. Owing to rapid research progress in recent years, it is now possible to provide detailed insight into the mechanisms of pathway crosstalk, common signalling nodes and the role of multi-functional proteins in co-regulating both protein degradation and cell death.

Indexed as

ApoptosisAutophagyProteolysisAnimalsHumansProteasome Endopeptidase ComplexProteinsProteasome Endopeptidase ComplexProteins

Identifiers

PMID24457955
PMCPMC4040655
OpenAlexW2053628391

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.