Evidence map›Paper›PMID 8917729›Full record

ReviewExperientia1996

Role of protein kinase activity in apoptosis.

M F Lavin, D Watters, Q Song

Abstract readReview
PubMed Publisher
In one paragraph

Review in Experientia, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing 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

11 citing papers in PubMed.

  1. Article
  2. Review
  3. ER Stress-Mediated Signaling: Action Potential and Ca(2+) as Key Players.International journal of molecular sciences · 2016
    Review
  4. Review
  5. Article
  6. How protein kinase C activation protects nerve cells from oxidative stress-induced cell death.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2001
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Inhibition of CPP32-like proteases rescues axotomized retinal ganglion cells from secondary cell death in vivo.The Journal of neuroscience : the official journal of the Society for Neuroscience · 1998
    Article
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

3 authors.

M F LavinCancer Research Unit, Queensland Institute of Medical Research, Bancroft Centre, PO Royal Brisbane Hospital, Herston, Australia.
D Watters
Q Song

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The transmission of signals from the plasma membrane to the nucleus involves a number of different pathways all of which have in common protein modification. The modification is primarily in the form of phosphorylation which leads to the activation of a series of protein kinases. It is now evident that these pathways are common to stimuli that lead to mitogenic and apoptotic responses. Even the same stimuli under different physiological conditions can cause either cell proliferation or apoptosis. Activation of specific protein kinases can in some circumstances protect against cell death, while in others it protects the cell against apoptosis. Some of the pathways involved lead to activation of transcription factors and the subsequent induction of genes involved in the process of cell death or proliferation. In other cases, such as for the tumour suppressor gene product p53, activation may be initiated both at the level of gene expression or through pre-existing proteins. Yet in others, while the initial steps in the pathway are ill-defined, it is clear that downstream activation of a series of cystein proteases is instrumental in pushing the cell towards apoptosis. In this report we review the involvement of protein kinases at several different levels in the control of cell behaviour.

Indexed as

ApoptosisDNA-Binding ProteinsAnimalsCell CycleDNA-Activated Protein KinaseHumansNuclear ProteinsPhosphatidylinositol 3-KinasesPhosphoproteinsPhosphotransferases (Alcohol Group Acceptor)Protein Kinase CProtein Serine-Threonine KinasesProtein-Tyrosine KinasesSignal TransductionDNA-Activated Protein KinaseDNA-Binding ProteinsNuclear ProteinsPhosphatidylinositol 3-KinasesPhosphoproteinsPhosphotransferases (Alcohol Group Acceptor)PRKDC protein, humanProtein Kinase CProtein Serine-Threonine KinasesProtein-Tyrosine Kinases

Identifiers

PMID8917729

What OpenQuestion holds

Textmetadata
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.