Evidence map›Paper›PMID 12190618›Full record

ArticleThe Biochemical journal2002

Autophosphorylation kinetics of protein kinases.

Zhi-Xin Wang, Jia-Wei Wu

Open access · bronzeAbstract 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 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.5field-weighted citation impact, top 39% 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

20 citing papers in PubMed, 39 citations in OpenAlex.

  1. Thermodynamics of Darwinian selection in molecular replicators.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025
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  18. Circadian rhythmicity by autocatalysis.PLoS computational biology · 2006
    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

2 authors at 1 institution in 1 country.

Zhi-Xin WangNational Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing 100101, P.R. China. zwang@sun5.ibp.ac.cn
Jia-Wei Wu
Institute of Biophysics · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein kinases play a central role in cellular signal transduction, by transmitting biochemical information between activated membrane-bound receptors and physiological target proteins. In addition to phosphorylating other proteins, almost all protein kinases catalyse autophosphorylation reactions (i.e. reactions in which the kinase serves as its own substrate). The autophosphorylation reactions can be intramolecular or intermolecular. In the present study, a detailed kinetic analysis of the intermolecular autophosphorylation reaction is presented. On the basis of the kinetic equations, a new procedure is developed to evaluate the kinetic parameters of the autophosphorylation reaction. This method was used to analyse the intermolecular autophosphorylation of an S6/H4 kinase from human placenta. At a fixed ATP concentration of 0.125 mM, the apparent catalytic-centre activity (turnover number; k (cat)) and apparent Michaelis-Menten constant ( K (m)) for the autophosphorylation reaction were determined to be 0.91 min(-1) and 0.86 microM respectively.

Indexed as

PhosphorylationAdenosine TriphosphateCatalytic DomainDose-Response Relationship, DrugHumansKineticsModels, ChemicalPlacentaProtein KinasesProtein Serine-Threonine KinasesProtein Structure, TertiarySubstrate SpecificityTime FactorsAdenosine TriphosphateProtein KinasesProtein Serine-Threonine Kinases

Identifiers

PMID12190618
PMCPMC1223023
OpenAlexW1995175116

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.