Evidence map›Paper›PMID 12207561›Full record

ArticleThe Biochemical journal2002

Phosphorylation is required for PMA- and cell-cycle-induced degradation of protein kinase Cdelta.

Jyoti Srivastava, Katarzyna J Procyk, Xavier Iturrioz, Peter J Parker

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

19 citing papers in PubMed, 46 citations in OpenAlex.

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  12. The life and death of protein kinase C.Current drug targets · 2008
    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.

Jyoti SrivastavaProtein Phosphorylation Laboratory, Cancer Research UK London Institute, Lincoln's Inn Fields Laboratories, 44 Lincoln's Inn Fields, London WC2A 3PX, U.K.
Katarzyna J Procyk
Xavier Iturrioz
Peter J Parker
The Honourable Society of Lincoln's Inn · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Classical and novel protein kinase C (PKC) isoforms are down-regulated as a result of chronic activation by certain tumour promoters and physiological stimuli; however, the mechanisms leading to down-regulation are not fully understood. In the present study, we have studied the PMA ('TPA')-induced degradation of PKCdelta in NIH 3T3 cells under culture conditions where PKCdelta displays cell-cycle-dependent down-regulation. In contrast with previous studies, a hyperphosphorylated form of this PKC isoform, promoted by calyculin A, was rapidly degraded in PMA-treated cells. Similarly, the presence of calyculin A enhanced the down-regulation of PKCdelta observed on G(1)/S-phase progression through the cell cycle. Analysis of phosphorylation-site mutants indicated that the T-loop Thr(505) phosphorylation site was critical for induced degradation.

Indexed as

3T3 CellsAnimalsCell CycleDown-RegulationIsoenzymesMarine ToxinsMiceOxazolesPhosphorylationProtein Kinase CProtein Kinase C-deltaS PhaseTetradecanoylphorbol AcetateThreonineUbiquitincalyculin AIsoenzymesMarine ToxinsOxazolesPrkcd protein, mouseProtein Kinase CProtein Kinase C-deltaTetradecanoylphorbol AcetateThreonineUbiquitin

Identifiers

PMID12207561
PMCPMC1222988
OpenAlexW1998434266

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.