Evidence map›Paper›PMID 20103566›Full record

ArticleMolecular & cellular proteomics : MCP2010

A tagging-via-substrate approach to detect the farnesylated proteome using two-dimensional electrophoresis coupled with Western blotting.

Fredrick O Onono, Michael A Morgan, H Peter Spielmann, Douglas A Andres, Thangaiah Subramanian, Arnold Ganser, Christoph W M Reuter

Open access · hybridAbstract readEvaluation Study
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

33 citing papers in PubMed, 54 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

7 authors at 2 institutions in 2 countries.

Fredrick O OnonoDepartment of Hematology, Hemostasis, Oncology, and Stem Cell Transplantation, Hannover Medical School, Hannover, Germany.
Michael A Morgan
H Peter Spielmann
Douglas A Andres
Thangaiah Subramanian
Arnold Ganser
Christoph W M Reuter
Medizinische Hochschule Hannover · DEUniversity of Kentucky · US

Funding

Synthetic Probes of Protein PrenylationR01GM066152 · NIGMS · UNIVERSITY OF KENTUCKY · PI SPIELMANN, H PETER · 2002 to 2011
$2.5M
NIGMS NIH HHS GM66152NIGMS NIH HHS R01 GM066152
6 · The paper itself

Abstract

Prenylation is a post-translational modification critical for the proper function of multiple physiologically important proteins, including small G-proteins, such as Ras. Methods allowing rapid and selective detection of protein farnesylation and geranylgeranylation are fundamental for the understanding of prenylated protein function and for monitoring efficacy of drugs such as farnesyltransferase inhibitors (FTIs). Although the natural substrates for prenyltransferases are farnesyl pyrophosphate and geranylgeranyl pyrophosphate, farnesyltransferase has been shown to incorporate isoprenoid analogues into protein substrates. In this study, protein prenyltransferase targets were labeled using anilinogeraniol, the alcohol precursor to the unnatural farnesyl pyrophosphate analogue 8-anilinogeranyl diphosphate in a tagging-via-substrate approach. Antibodies specific for the anilinogeranyl moiety were used to detect the anilinogeranyl-modified proteins. Coupling this highly effective labeling/detection method with two-dimensional electrophoresis and subsequent Western blotting allowed simple, rapid analysis of the complex farnesylated proteome. For example, this method elucidated the differential effects induced by two chemically distinct FTIs, BMS-214,662 and L-778,123. Although both FTIs strongly inhibited farnesylation of many proteins such as Lamins, NAP1L1, N-Ras, and H-Ras, only the dual prenylation inhibitor L-778,123 blocked prenylation of Pex19, RhoB, K-Ras, Cdc42, and Rap1. This snapshot approach has significant advantages over traditional techniques, including radiolabeling, anti-farnesyl antibodies, or mass spectroscopy, and enables dynamic analysis of the farnesylated proteome.

Indexed as

Protein PrenylationAniline CompoundsBlotting, WesternCell Line, TumorElectrophoresis, Gel, Two-DimensionalEnzyme InhibitorsFarnesyltranstransferaseHL-60 CellsHumansImidazolesK562 CellsModels, BiologicalProteomeProteomicsStaining and LabelingSubstrate SpecificityAniline CompoundsEnzyme InhibitorsFarnesyltranstransferaseImidazolesL 778,123Proteome

Identifiers

PMID20103566
PMCPMC2860237
OpenAlexW2131216606

What OpenQuestion holds

Textmetadata
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.