Evidence map›Paper›PMID 25952057›Full record

ArticleBiochemical pharmacology2015

In vitro studies in a myelogenous leukemia cell line suggest an organized binding of geranylgeranyl diphosphate synthase inhibitors.

Jacqueline E Reilly, Xiang Zhou, Huaxiang Tong, Craig H Kuder, David F Wiemer, Raymond J Hohl

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochemical pharmacology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.2field-weighted citation impact, top 43% 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

3 citing papers in PubMed, 3 citations in OpenAlex.

  1. Article
  2. The role of cholesterol metabolism in leukemia.Blood science (Baltimore, Md.) · 2019
    Review
  3. 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

6 authors at 2 institutions in 1 country.

Jacqueline E ReillyDepartment of Pharmacology, University of Iowa, 375 Newton Rd, 5219 MERF, Iowa City, IA 52242, USA. Electronic address: jacqueline-reilly@uiowa.edu.
Xiang ZhouDepartment of Chemistry, E531 Chemistry Building, University of Iowa, Iowa City, IA 52242, USA. Electronic address: xiang-zhou@uiowa.edu.
Huaxiang TongDepartment of Internal Medicine, University of Iowa, 375 Newton Rd, 5219 MERF, Iowa City, IA 52242, USA. Electronic address: huaxiang-tong@uiowa.edu.
Craig H KuderDepartment of Internal Medicine, University of Iowa, 375 Newton Rd, 5219 MERF, Iowa City, IA 52242, USA. Electronic address: craig.kuder@gmail.com.
David F WiemerDepartment of Chemistry, E531 Chemistry Building, University of Iowa, Iowa City, IA 52242, USA. Electronic address: david-wiemer@uiowa.edu.
Raymond J HohlDepartment of Pharmacology, University of Iowa, 375 Newton Rd, 5219 MERF, Iowa City, IA 52242, USA; Department of Internal Medicine, University of Iowa, 375 Newton Rd, 5219 MERF, Iowa City, IA 52242, USA; Department of Medicine, Pennsylvania State University, Penn State Hershey Cancer Institute, 500 University Dr, Hershey, PA 17033-0850, USA; Department of Pharmacology, Pennsylvania State University, Penn State Hershey Cancer Institute, 500 University Dr, Hershey, PA 17033-0850, USA. Electronic address: rhohl@hmc.psu.edu.
University of Iowa · USPenn State Milton S. Hershey Medical Center · US

Funding

Predoctoral Training in the Pharmacological SciencesT32GM067795 · NIGMS · UNIVERSITY OF IOWA · PI STRACK, STEFAN · 2004 to 2021
$3.4M
NIGMS NIH HHS 2 T32 GM067795NIGMS NIH HHS T32 GM067795
6 · The paper itself

Abstract

A small set of isoprenoid bisphosphonates ethers has been tested in the K562 chronic myelogenous leukemia cell line to determine their impact on isoprenoid biosynthesis. Five of these compounds inhibit geranylgeranyl diphosphate synthase (GGDPS) with IC50 values below 1 μM in enzyme assays, but in cells their apparent activity is more varied. In particular, the isomeric C-geranyl-O-prenyl and C-prenyl-O-geranyl bisphosphonates are quite different in their activity with the former consistently demonstrating greater impairment of geranylgeranylation in cells but the latter showing greater impact in the enzyme assays with GGDPS. Together, these findings suggest an organized binding of these inhibitors in the two hydrophobic channels of the geranylgeranyl diphosphate synthase enzyme.

Indexed as

DiphosphonatesEthersFarnesyltranstransferaseHumansK562 CellsPolyisoprenyl PhosphatesProtein BindingProtein Prenylationrab GTP-Binding Proteinsrap1 GTP-Binding Proteinsras ProteinsStructure-Activity RelationshipTerpenesDiphosphonatesEthersFarnesyltranstransferasegeranylgeranyl pyrophosphatePolyisoprenyl PhosphatesRab6 proteinrab GTP-Binding Proteinsrap1 GTP-Binding Proteinsras ProteinsTerpenesBisphosphonateChronic myelogenous leukemia (CML)Geranylgeranyl diphosphate synthaseIsoprenoidProtein isoprenylationStatin

Identifiers

PMID25952057
PMCPMC4831703
OpenAlexW290516818

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.