Evidence map›Paper›PMID 17644338›Full record

ReviewCellular signalling2007

Processive phosphorylation: mechanism and biological importance.

Parag Patwardhan, W Todd Miller

Abstract readReview
In one paragraph

Review in Cellular signalling, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing 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

55 citing papers in PubMed.

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  13. A walk-through MAPK structure and functionality with the 30-year-old yeast MAPK Slt2.International microbiology : the official journal of the Spanish Society for Microbiology · 2021
    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

2 authors.

Parag PatwardhanDepartment of Physiology and Biophysics, School of Medicine, Stony Brook University, Stony Brook, NY 11794, USA.
W Todd Miller

Funding

SUSTRATE SPECIFICITY OF NONRECEPTOR TYROSINE KINASER01CA058530 · NCI · STATE UNIVERSITY NEW YORK STONY BROOK · PI MILLER, W TODD · 1999 to 2018
$3.7M
SUBSTRATE SPECIFICITY OF NONRECEPTOR TYROSINE KINASESR29CA058530 · NCI · STATE UNIVERSITY NEW YORK STONY BROOK · PI MILLER, W TODD · 1993 to 1997
–
NCI NIH HHS CA58530NCI NIH HHS R01 CA058530
6 · The paper itself

Abstract

Recent proteomic data indicate that a majority of the phosphorylated proteins in a eucaryotic cell contain multiple sites of phosphorylation. In many signaling events, a single kinase phosphorylates multiple sites on a target protein. Processive phosphorylation occurs when a protein kinase binds once to a substrate and phosphorylates all of the available sites before dissociating. In this review, we discuss examples of processive phosphorylation by serine/threonine kinases and tyrosine kinases. We describe current experimental approaches for distinguishing processive from non-processive phosphorylation. Finally, we contrast the biological situations that are suited to regulation by processive and non-processive phosphorylation.

Indexed as

Protein Processing, Post-TranslationalAnimalsCrk-Associated Substrate ProteinHumansNuclear ProteinsPhosphorylationRNA-Binding ProteinsSerine-Arginine Splicing FactorsCrk-Associated Substrate ProteinNuclear ProteinsRNA-Binding ProteinsSerine-Arginine Splicing Factors

Identifiers

PMID17644338
PMCPMC2034209

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.