Evidence map›Paper›PMID 22321213›Full record

ArticleBioorganic & medicinal chemistry letters2012

Effect of alkyl chain length on sphingosine kinase 2 selectivity.

Kenneth Knott, Yugesh Kharel, Mithun R Raje, Kevin R Lynch, Webster L Santos

Open access · greenAbstract read
In one paragraph

Article in Bioorganic & medicinal chemistry letters, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

11 citing papers in PubMed, 19 citations in OpenAlex.

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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 2 institutions in 1 country.

Kenneth KnottDepartment of Chemistry, Virginia Tech, Blacksburg, VA 24061, USA.
Yugesh Kharel
Mithun R Raje
Kevin R Lynch
Webster L Santos
Virginia Tech · USUniversity of Virginia · US

Funding

Molecular Pharmacology of Sphingosine 1-PhosphateR01GM067958 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI LYNCH, KEVIN R. · 2004 to 2014
$3.7M
NIGMS NIH HHS R01 GM067958
6 · The paper itself

Abstract

The conversion of sphingosine to sphingosine-1-phosphate is catalyzed by sphingosine kinase (SphK), which has been implicated in disease states such as cancer and fibrosis. Because SphK exists as two different isoforms, SphK1 and SphK2, understanding the physiological function of each isoenzyme is important. Of the two isoenzymes, SphK2 is significantly less understood, which is evident by the lack of selective small molecule inhibitors. Building on our initial work that focused on the structure-activity relationship study on an FTY720-derived cylohexylamine scaffold, we report that varying the alkyl chain length on the hydrophobic tail can impart selectivity toward SphK2 over SphK1.

Indexed as

CyclohexylaminesEnzyme InhibitorsFingolimod HydrochlorideIsoenzymesPhosphotransferases (Alcohol Group Acceptor)Propylene GlycolsProtein BindingSphingosineSphingosine KinaseStructure-Activity RelationshipCyclohexylaminesEnzyme InhibitorsFingolimod HydrochlorideIsoenzymesPhosphotransferases (Alcohol Group Acceptor)Propylene GlycolsSphingosineSphingosine Kinase

Identifiers

PMID22321213
PMCPMC3394931
OpenAlexW2046117789

What OpenQuestion 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 OpenQuestion graph.