Evidence map›Paper›PMID 19778720›Full record

ReviewChemistry & biology2009

The alpha,alpha-difluorinated phosphonate L-pSer-analogue: an accessible chemical tool for studying kinase-dependent signal transduction.

Kaushik Panigrahi, MariJean Eggen, Jun-Ho Maeng, Quanrong Shen, David B Berkowitz

Open access · greenAbstract readReview
In one paragraph

Review in Chemistry & biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.6field-weighted citation impact, top 18% 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

21 citing papers in PubMed, 60 citations in OpenAlex.

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  11. Synthetic approaches to protein phosphorylation.Current opinion in chemical biology · 2015
    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

5 authors at 1 institution in 1 country.

Kaushik PanigrahiDepartment of Chemistry, University of Nebraska, Lincoln, NE 68588, USA.
MariJean Eggen
Jun-Ho Maeng
Quanrong Shen
David B Berkowitz
University of Nebraska–Lincoln · US

Funding

EXTRAMURAL RES FACILITIES CONSTRC06RR016544 · NCRR · UNIVERSITY OF NEBRASKA LINCOLN · PI PAUL, PREM S · 2001 to 2001
$2.0M
NCRR NIH HHS C06 RR016544
6 · The paper itself

Abstract

This overview focuses on the (alpha,alpha-difluoromethylene)phosphonate mimic of phosphoserine (pCF(2)Ser) and its application to the study of kinase-mediated signal transduction-pathways of great interest to drug development. The most versatile modes of access to these chemical biological tools are discussed, organized by method of PCF(2)-C bond formation. The pCF(2)-Ser mimic may be site-specifically incorporated into peptides (SPPS) and proteins (expressed protein ligation). This isopolar, dianionic pSer mimic results in a "constitutive phosphorylation" phenotype and is seen to support native protein-protein interactions that depend on serine phosphorylation. Signal transduction pathways studied with this chemical biological approach include the regulation of p53 tumor suppressor protein activity and of melatonin production. Given these successes, the future is bright for the use of such "teflon phospho-amino acid mimics" to map kinase-based signaling pathways.

Indexed as

Signal TransductionClodronic AcidMAP Kinase Signaling SystemMelatoninPhosphorylationPhosphoserineProtein Interaction Domains and MotifsTumor Suppressor Protein p53Clodronic Aciddifluoromethylene diphosphonateMelatoninPhosphoserineTumor Suppressor Protein p53

Identifiers

PMID19778720
PMCPMC2766077
OpenAlexW1996399586

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.