Evidence map›Paper›PMID 27342750›Full record

ArticleBioorganic & medicinal chemistry letters2016

Exploration of GGTase-I substrate requirements. Part 1: Synthesis and biochemical evaluation of novel aryl-modified geranylgeranyl diphosphate analogs.

Kayla J Temple, Elia N Wright, Carol A Fierke, Richard A Gibbs

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Bioorganic & medicinal chemistry letters, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.2field-weighted citation impact, top 46% 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

1 citing paper in PubMed, 1 citations in OpenAlex.

  1. Article
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

4 authors at 2 institutions in 1 country.

Kayla J TempleDepartment of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, IN 47907, USA; The Purdue University Center for Cancer Research, Purdue University, West Lafayette, IN 47909, USA. Electronic address: kayla.temple@vanderbilt.edu.
Elia N WrightDepartment of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.
Carol A FierkeDepartment of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109, USA; Department of Chemistry, University of Michigan, Ann Arbor, MI 48109, USA.
Richard A GibbsDepartment of Medicinal Chemistry and Molecular Pharmacology, Purdue University, West Lafayette, IN 47907, USA; The Purdue University Center for Cancer Research, Purdue University, West Lafayette, IN 47909, USA.
Center for Cancer Research · USUniversity of Michigan–Ann Arbor · US

Funding

Transgenic Mouse Core Facility Shared Resource (TMCF-SR)P30CA023168 · NCI · PURDUE UNIVERSITY WEST LAFAYETTE · PI John Tesmer · 1985 to 2026
$43.4M
STRUCTURE/FUNCTION OF ZINC METALLOPROTEINSR01GM040602 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI FIERKE, CAROL A · 1993 to 2017
$6.0M
CHEMICAL PROBES OF PROTEIN PRENYLATIONR01CA078819 · NCI · WAYNE STATE UNIVERSITY · PI GIBBS, RICHARD A · 1998 to 2007
$1.1M
NCI NIH HHS P30 CA023168NCI NIH HHS R01 CA078819NIGMS NIH HHS R01 GM040602
6 · The paper itself

Abstract

Protein geranylgeranylation is a type of post-translational modification that aids in the localization of proteins to the plasma member where they elicit cellular signals. To better understand the isoprenoid requirements of GGTase-I, a series of aryl-modified geranylgeranyl diphosphate analogs were synthesized and screened against mammalian GGTase-I. Of our seven-member library of compounds, six analogs proved to be substrates of GGTase-I, with 6d having a krel=1.93 when compared to GGPP (krel=1.0).

Indexed as

Alkyl and Aryl TransferasesAnimalsDose-Response Relationship, DrugEnzyme InhibitorsHumansMolecular StructurePolyisoprenyl PhosphatesStructure-Activity RelationshipAlkyl and Aryl TransferasesEnzyme Inhibitorsgeranylgeranyl pyrophosphategeranylgeranyltransferase type-IPolyisoprenyl PhosphatesAryl-modified GGPP analogsGeranylgeranylationGGTase-IPost-translational modificationProtein prenylation

Identifiers

PMID27342750
PMCPMC4955810
OpenAlexW2421241607

What OpenQuestion holds

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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.