Evidence map›Paper›PMID 29282289›Full record

ArticleThe Journal of biological chemistry2018

Efficient farnesylation of an extended C-terminal C(

Melanie J Blanden, Kiall F Suazo, Emily R Hildebrandt, Daniel S Hardgrove, Meet Patel, William P Saunders, Mark D Distefano, Walter K Schmidt, James L Hougland

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. 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
1.5field-weighted citation impact, top 18% 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, 49 citations in OpenAlex.

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  12. Physiological adventures inMicrobiology and molecular biology reviews : MMBR · 2024
    Review
  13. Comprehensive analysis of CXXX sequence space reveals thatbioRxiv : the preprint server for biology · 2024
    Article
  14. Review
  15. Article
  16. Article
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  18. Promiscuous Enzymes for Residue-Specific Peptide and Protein Late-Stage Functionalization.Chembiochem : a European journal of chemical biology · 2023
    Review
  19. Article
  20. Review
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

9 authors at 3 institutions in 1 country.

Melanie J BlandenDepartment of Chemistry, Syracuse University, Syracuse, New York 13244.
Kiall F SuazoDepartment of Chemistry, University of Minnesota, Minneapolis, Minnesota 55455.
Emily R HildebrandtDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602.
Daniel S HardgroveDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602.
Meet PatelDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602.
William P SaundersDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602.
Mark D DistefanoDepartment of Chemistry, University of Minnesota, Minneapolis, Minnesota 55455.
Walter K SchmidtDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602.
James L HouglandDepartment of Chemistry, Syracuse University, Syracuse, New York 13244. Electronic address: hougland@syr.edu.
University of Georgia · USSyracuse University · USUniversity of Minnesota · US

Funding

Enzymatic Protein LabelingR01GM084152 · NIGMS · UNIVERSITY OF MINNESOTA · PI DISTEFANO, MARK D · 2010 to 2019
$2.6M
Role of Proteolysis in Regulating CaaX Protein FunctionR01GM117148 · NIGMS · UNIVERSITY OF GEORGIA · PI SCHMIDT, WALTER K · 2016 to 2019
$1.2M
NIGMS NIH HHS R01 GM084152NIGMS NIH HHS R01 GM117148
6 · The paper itself

Abstract

Protein prenylation is a post-translational modification that has been most commonly associated with enabling protein trafficking to and interaction with cellular membranes. In this process, an isoprenoid group is attached to a cysteine near the C terminus of a substrate protein by protein farnesyltransferase (FTase) or protein geranylgeranyltransferase type I or II (GGTase-I and GGTase-II). FTase and GGTase-I have long been proposed to specifically recognize a four-amino acid C

Indexed as

Models, MolecularProtein PrenylationAlkyl and Aryl TransferasesAmino Acid MotifsAnimalsDatabases, ProteinEnzyme InhibitorsGenes, ReporterGreen Fluorescent ProteinsHEK293 CellsHumansMicroscopy, FluorescenceProtein SubunitsProteomicsRatsRecombinant Fusion ProteinsAlkyl and Aryl Transferasesenhanced green fluorescent proteinEnzyme Inhibitorsgeranylgeranyltransferase type-IGreen Fluorescent Proteinsp21(ras) farnesyl-protein transferaseProtein SubunitsRecombinant Fusion ProteinsSaccharomyces cerevisiae Proteinsenzymemass spectrometry (MS)post-translational modificationprotein farnesylationprotein isoprenylationRas proteinyeast genetics

Identifiers

PMID29282289
PMCPMC5827447
OpenAlexW2777381435

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.