Evidence map›Paper›PMID 11085927›Full record

ArticleThe Biochemical journal2000

Cloning and expression of a cDNA encoding human inositol 1,4,5-trisphosphate 3-kinase C.

V Dewaste, V Pouillon, C Moreau, S Shears, K Takazawa, C Erneux

Open access · greenAbstract read
In one paragraph

Article in The Biochemical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

24 citing papers in PubMed, 56 citations in OpenAlex.

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  9. Inositol trisphosphate 3-kinases: focus on immune and neuronal signaling.Cellular and molecular life sciences : CMLS · 2010
    Review
  10. Article
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  17. Inositol (1,4,5) trisphosphate 3 kinase B controls positive selection of T cells and modulates Erk activity.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  18. Article
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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 2 institutions in 2 countries.

V DewasteInterdisciplinary Research Institute (IRIBHN), Université Libre de Bruxelles, Campus Erasme, Bldg. C, 808 Route de Lennik, 1070 Brussels, Belgium.
V Pouillon
C Moreau
S Shears
K Takazawa
C Erneux
Tokyo Metropolitan Police Hospital · JPUniversité Libre de Bruxelles · BE

Funding

Inositol SignallingZIAES080046 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI SHEARS, STEPHEN B · 2009 to 2023
$31.3M
REGULATION OF INOSITOL LIPID SIGNALLING MECHANISMSZ01ES080046 · NIEHS · NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES · PI SHEARS, STEPHEN B · 1990 to 2008
$4.3M
6 · The paper itself

Abstract

Inositol 1,4,5-trisphosphate [Ins(1,4,5)P(3)] 3-kinase catalyses the phosphorylation of Ins(1,4,5)P(3) to Ins(1,3,4,5)P(4). cDNAs encoding two isoenzymes of Ins(1,4,5)P(3) 3-kinase (3-kinases A and B) have been described previously. In the present study, we report the cloning of a full-length 2052 bp cDNA encoding a third human isoenzyme of the Ins(1,4,5)P(3) 3-kinase family, referred to as isoform C. This novel enzyme has a calculated molecular mass of 75. 207 kDa and a K(m) for Ins(1,4,5)P(3) of 6 microM. Northern-blot analysis showed the presence of a transcript of approx. 3.9 kb in various human tissues. Inositol trisphosphate 3-kinase C demonstrates enzymic activity when expressed in DH5alphaF' bacteria or COS-7 cells. Calcium alone decreases the Ins(1,4,5)P(3) 3-kinase activity of the 3-kinase C isoenzyme in transfected COS-7 cells. This inhibitory effect is reversed in the presence of calmodulin. The recombinant bacterial 3-kinase C can be adsorbed on calmodulin-Sepharose in the presence of calcium. The present data show that Ins(1,4,5)P(3) 3-kinase C: (i) shares a conserved catalytic domain of about 275 amino acids with the two other mammalian isoforms, (ii) could be purified on a calmodulin-Sepharose column and (iii) could be distinguished from the A and B isoenzymes by the effects of calcium and of calmodulin.

Indexed as

Amino Acid SequenceAnimalsBase SequenceCalciumChromatography, High Pressure LiquidCloning, MolecularCOS CellsDNA, ComplementaryDNA PrimersHumansMolecular Sequence DataPhosphotransferases (Alcohol Group Acceptor)Recombinant ProteinsSequence Homology, Amino AcidCalciumDNA, ComplementaryDNA PrimersInositol 1,4,5-trisphosphate 3-kinasePhosphotransferases (Alcohol Group Acceptor)Recombinant Proteins

Identifiers

PMID11085927
PMCPMC1221465
OpenAlexW2045177771

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.