Evidence map›Paper›PMID 19320430›Full record

ArticleThe Journal of organic chemistry2009

Solid-phase synthesis of prenylcysteine analogs.

James L Donelson, Heather B Hodges-Loaiza, Brian S Henriksen, Christine A Hrycyna, Richard A Gibbs

Open access · greenAbstract read
In one paragraph

Article in The Journal of organic chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

6 citing papers in PubMed, 13 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 1 institution in 1 country.

James L DonelsonDepartment of Medicinal Chemistry and Molecular Pharmacology, Purdue Cancer Center, Purdue University, West Lafayette, Indiana 47907, USA.
Heather B Hodges-Loaiza
Brian S Henriksen
Christine A Hrycyna
Richard A Gibbs
Purdue University West Lafayette · US

Funding

Inhibition of Prenylated Protein ProcessingR01CA112483 · NCI · PURDUE UNIVERSITY · PI GIBBS, RICHARD A · 2007 to 2009
$791k
NCI NIH HHS P30CA21368NCI NIH HHS R01 CA112483NCI NIH HHS R01CA112483
6 · The paper itself

Abstract

Prenylcysteine derivatives are of interest for a variety of different biological reasons, including probing the CaaX protein processing pathway. A solid-phase synthesis protocol for the preparation of prenylcysteines using 2-chlorotrityl chloride resin as a solid support has been developed. A series of novel amide-modified farnesylcysteine analogs were synthesized in both high purity and yield under mild conditions. The farnesylcysteine analogs were evaluated using human isoprenylcysteine carboxyl methyltransferase as a biological target, and several new inhibitors, one with significantly enhanced potency, were identified.

Indexed as

Amino Acid SequenceChromatography, High Pressure LiquidCysteineHumansMolecular StructureProtein MethyltransferasesSolid Phase ExtractionTriphenylmethyl Compounds2-chlorotrityl chlorideCysteineprenylcysteineProtein Methyltransferasesprotein-S-isoprenylcysteine O-methyltransferaseS-farnesylcysteineTriphenylmethyl Compounds

Identifiers

PMID19320430
PMCPMC2702710
OpenAlexW2049468465

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.