Evidence map›Paper›PMID 22857735›Full record

ArticleOrganic letters2012

Synthesis of frame-shifted farnesyl diphosphate analogs.

Andrew T Placzek, James L Hougland, Richard A Gibbs

Abstract read
In one paragraph

Article in Organic letters, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing 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

7 citing papers in PubMed.

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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

3 authors.

Andrew T PlaczekDepartment of Medicinal Chemistry and Molecular Pharmacology, College of Pharmacy, Purdue University, West Lafayette, Indiana 47907, United States.
James L Hougland
Richard A Gibbs

Funding

CHEMICAL PROBES OF PROTEIN PRENYLATIONR01CA078819 · NCI · WAYNE STATE UNIVERSITY · PI GIBBS, RICHARD A · 1998 to 2007
$1.1M
NCI NIH HHS P30 CA21328NCI NIH HHS R01 CA078819NCI NIH HHS R01 CA78819
6 · The paper itself

Abstract

A set of synthetic approaches were developed and applied to the synthesis of eight frame-shifted farnesyl diphosphate (FPP) analogs. These analogs bear increased or decreased methylene units between the double bonds and/or diphosphate moieties of the isoprenoid structure. Evaluation versus mammalian FTase revealed that small structural changes can lead to dramatic changes in substrate ability.

Indexed as

Alkyl and Aryl TransferasesMolecular StructurePolyisoprenyl PhosphatesSesquiterpenesStructure-Activity RelationshipAlkyl and Aryl Transferasesfarnesyl pyrophosphatep21(ras) farnesyl-protein transferasePolyisoprenyl PhosphatesSesquiterpenes

Identifiers

PMID22857735
PMCPMC6863160

What OpenQuestion holds

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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.