Evidence map›Paper›PMID 25147561›Full record

ReviewFrontiers in genetics2014

Physicochemical mechanisms of protein regulation by phosphorylation.

Hafumi Nishi, Alexey Shaytan, Anna R Panchenko

Abstract readReview
In one paragraph

Review in Frontiers in genetics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 113 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
113citing papers in PubMed, 1 pooled it
–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

113 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
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  18. Long noncoding RNAs regulating enzymatic reactions in cancer.Experimental & molecular medicine · 2025
    Review
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  20. Review

53 more citing papers are in PubMed but not listed here.

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.

Hafumi NishiGraduate School of Medical Life Science, Yokohama City University Yokohama Japan.
Alexey ShaytanNational Center for Biotechnology Information, National Library of Medicine, National Institutes of Health Bethesda, MD USA.
Anna R PanchenkoNational Center for Biotechnology Information, National Library of Medicine, National Institutes of Health Bethesda, MD USA.

Funding

Protein-protein binding: regulation and effect of disease mutationsZIALM090313 · NLM · NATIONAL LIBRARY OF MEDICINE · PI PANCHENKO, ANNA · 2013 to 2018
$5.2M
6 · The paper itself

Abstract

Phosphorylation offers a dynamic way to regulate protein activity and subcellular localization, which is achieved through its reversibility and fast kinetics. Adding or removing a dianionic phosphate group somewhere on a protein often changes the protein's structural properties, its stability and dynamics. Moreover, the majority of signaling pathways involve an extensive set of protein-protein interactions, and phosphorylation can be used to regulate and modulate protein-protein binding. Losses of phosphorylation sites, as a result of disease mutations, might disrupt protein binding and deregulate signal transduction. In this paper we focus on the effects of phosphorylation on protein stability, dynamics, and binding. We describe several physico-chemical mechanisms of protein regulation through phosphorylation and pay particular attention to phosphorylation in protein complexes and phosphorylation in the context of disorder-order and order-disorder transitions. Finally we assess the role of multiple phosphorylation sites in a protein molecule, their possible cooperativity and function.

Indexed as

allosteric regulationmultisite phosphorylationprotein disorderprotein phosphorylationprotein–protein interactions

Identifiers

PMID25147561
PMCPMC4124799

What OpenQuestion holds

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LicenceCC BY
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.