Evidence map›Paper›PMID 25150376›Full record

ArticleBioorganic & medicinal chemistry letters2014

Design and synthesis of non-hydrolyzable homoisoprenoid α-monofluorophosphonate inhibitors of PPAPDC family integral membrane lipid phosphatases.

Thangaiah Subramanian, Hongmei Ren, Karunai Leela Subramanian, Manjula Sunkara, Fredrick O Onono, Andrew J Morris, H Peter Spielmann

Abstract read
In one paragraph

Article in Bioorganic & medicinal chemistry letters, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

7 authors.

Thangaiah SubramanianDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY 40536, USA.
Hongmei RenDivision of Cardiovascular Medicine UK COM, University of Kentucky, Lexington, KY 40536, USA.
Karunai Leela SubramanianDivision of Cardiovascular Medicine UK COM, University of Kentucky, Lexington, KY 40536, USA.
Manjula SunkaraDivision of Cardiovascular Medicine UK COM, University of Kentucky, Lexington, KY 40536, USA.
Fredrick O OnonoDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY 40536, USA.
Andrew J MorrisDivision of Cardiovascular Medicine UK COM, University of Kentucky, Lexington, KY 40536, USA; Lexington Veterans Affairs Medical Center, University of Kentucky, Lexington, KY 40536, USA.
H Peter SpielmannDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY 40536, USA; Markey Cancer Center, University of Kentucky, Lexington, KY 40536, USA; Kentucky Center for Structural Biology, University of Kentucky, Lexington, KY 40536, USA; Department of Chemistry, University of Kentucky, Lexington, KY 40536, USA. Electronic address: hps@uky.edu.

Funding

The role of IKKß in linking obesity to adipose tissue inflammation and adipogeneP20GM103527 · NIGMS · UNIVERSITY OF KENTUCKY · PI CASSIS, LISA A · 2012 to 2017
$13.7M
Role of Lipid Phosphatases in Cholesterol and Triglyceride SynthesisR01GM050388 · NIGMS · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI MORRIS, ANDREW J · 1994 to 2011
$2.7M
Synthetic Probes of Protein PrenylationR01GM066152 · NIGMS · UNIVERSITY OF KENTUCKY · PI SPIELMANN, H PETER · 2002 to 2011
$2.5M
Thermo/Finnigan TSQ AM Triple Stage Quadrupole Mass SpectrometerS10RR024598 · NCRR · UNIVERSITY OF KENTUCKY · PI MORRIS, ANDREW J · 2008 to 2008
$493k
NCRR NIH HHS S10 RR024598NIGMS NIH HHS P20 GM103527NIGMS NIH HHS R01 GM050388NIGMS NIH HHS R01 GM066152NIGMS NIH HHS R01 GM50388NIGMS NIH HHS R01 GM66152
6 · The paper itself

Abstract

An efficient, diversity oriented synthesis of homoisoprenoid α-monofluorophosphonates utilizing electrophilic fluorination is presented along with their activity as inhibitors of PPAPDC2 family integral membrane lipid phosphatases. These novel phosphatase-resistant analogues of isoprenoid monophosphates are a platform for further structure-activity relationship studies and provide access to other isoprenoid family members where the phosphate ester oxygen is replaced by a α-monofluoromethylene moiety.

Indexed as

Drug DesignDose-Response Relationship, DrugEnzyme InhibitorsMolecular StructurePhosphoric Monoester HydrolasesPolyisoprenyl PhosphatesStructure-Activity RelationshipEnzyme InhibitorsPhosphoric Monoester HydrolasesPolyisoprenyl PhosphatesFarnesyl diphosphateIsoprenolMevalonate pathwayPhosphatase inhibitorPhosphonate

Identifiers

PMID25150376
PMCPMC4206410

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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.