Evidence map›Paper›PMID 30111833›Full record

ArticleScientific reports2018

Apoptosis regulation by subcellular relocation of caspases.

Evgeniia A Prokhorova, Gelina S Kopeina, Inna N Lavrik, Boris Zhivotovsky

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 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, 81 citations in OpenAlex.

  1. Review
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  9. Exploring caspase functions in mouse models.Apoptosis : an international journal on programmed cell death · 2024
    Review
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  11. Article
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  13. Review
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  16. Programmed Cell Death in Diabetic Nephropathy: A Review of Apoptosis, Autophagy, and Necroptosis.Medical science monitor : international medical journal of experimental and clinical research · 2022
    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 5 countries.

Evgeniia A ProkhorovaFaculty of Medicine, Lomonosov Moscow State University, 119991, Moscow, Russia.ORCID 0000-0002-5467-5586
Gelina S KopeinaFaculty of Medicine, Lomonosov Moscow State University, 119991, Moscow, Russia.
Inna N LavrikFaculty of Medicine, Lomonosov Moscow State University, 119991, Moscow, Russia.
Boris ZhivotovskyFaculty of Medicine, Lomonosov Moscow State University, 119991, Moscow, Russia. Boris.Zhivotovsky@ki.se.
Lomonosov Moscow State University · RU

Funding

Barncancerfonden (Swedish Childhood Cancer Foundation) PR2016-0090Cancerfonden (Swedish Cancer Society) 160733Radiumhemmets Forskningsfonder (Cancer Research Foundations of Radiumhemmet) 161292Russian Foundation for Basic Research (RFBR) 18-015-00211Russian Foundation for Basic Research (RFBR) 18-04-00207Russian Science Foundation (RSF) 14-25-00056Russian Science Foundation (RSF) 17-75-20102Vetenskapsrådet (Swedish Research Council) 521-2014-2258
6 · The paper itself

Abstract

The cleavage of nuclear proteins by caspases promotes nuclear breakdown and, therefore, plays a key role in apoptosis execution. However, the detailed molecular mechanisms of these events remain unclear. To get more insights into the mechanisms of nuclear events during apoptosis we set up a rapid fractionation protocol for the separation of the cytoplasmic and nuclear fractions of cells undergoing cisplatin-induced apoptosis. Importantly, nuclear accumulation of effector caspase-3 as well as initiator caspase-2, -8 and -9 was observed using the developed protocol and immunofluorescence microscopy. The detection of caspases and their cleavage products in the nucleus occurred within the same time interval after cisplatin treatment and took place shortly before nuclear fragmentation. The entry of initiator caspases to the nucleus was independent of caspase-3. Given that all three initiator caspases had catalytic activity in the nuclei, our findings indicate that initiator caspases might participate in the proteolysis of nuclear components during apoptosis, promoting its disintegration and apoptotic cell death.

Indexed as

ApoptosisCaspase 2Caspase 3Caspase 8CaspasesCell FractionationCell Line, TumorCell NucleusCisplatinCysteine EndopeptidasesCytoplasmDNA FragmentationHeLa CellsHumansMCF-7 CellsNuclear ProteinsCASP2 protein, humanCASP3 protein, humanCASP8 protein, humanCaspase 2Caspase 3Caspase 8CaspasesCisplatinCysteine EndopeptidasesNuclear Proteins

Identifiers

PMID30111833
PMCPMC6093910
OpenAlexW2887837540

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.