Evidence map›Paper›PMID 30058775›Full record

ArticleCurrent protocols in chemical biology2018

Metabolic Labeling of Prenylated Proteins Using Alkyne-Modified Isoprenoid Analogues.

Kiall F Suazo, Alexander K Hurben, Kevin Liu, Feng Xu, Pa Thao, Ch Sudheer, Ling Li, Mark D Distefano

Abstract read
In one paragraph

Article in Current protocols in chemical biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
0.9field-weighted citation impact, top 30% 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

21 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Review
  3. ACS chemical biology · 2025
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  14. ACS chemical biology · 2022
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  16. Review
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  19. Article
  20. Splice switching an oncogenic ratio of SmgGDS isoforms as a strategy to diminish malignancy.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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

8 authors at 1 institution in 1 country.

Kiall F SuazoDepartment of Chemistry, University of Minnesota, Minneapolis, Minnesota.
Alexander K HurbenDepartment of Chemistry, University of Minnesota, Minneapolis, Minnesota.
Kevin LiuDepartment of Chemistry, University of Minnesota, Minneapolis, Minnesota.
Feng XuDepartment of Chemistry, University of Minnesota, Minneapolis, Minnesota.
Pa ThaoDepartment of Chemistry, University of Minnesota, Minneapolis, Minnesota.
Ch SudheerDepartment of Chemistry, University of Minnesota, Minneapolis, Minnesota.
Ling LiDepartment of Experimental and Clinical Pharmacology, University of Minnesota, Minneapolis, Minnesota.
Mark D DistefanoDepartment of Chemistry, University of Minnesota, Minneapolis, Minnesota.
University of Minnesota · US

Funding

Enzymatic Protein LabelingR01GM084152 · NIGMS · UNIVERSITY OF MINNESOTA · PI DISTEFANO, MARK D · 2010 to 2019
$2.6M
Dysregulation of Protein Prenylation in the Pathogenesis of Alzheimer's DiseaseRF1AG056976 · NIA · UNIVERSITY OF MINNESOTA · PI DISTEFANO, MARK D, LI, LING · 2017 to 2017
$1.9M
NIA NIH HHS RF1 AG056976NIGMS NIH HHS R01 GM084152
6 · The paper itself

Abstract

Protein prenylation involves the attachment of a farnesyl or geranylgeranyl group onto a cysteine residue located near the C-terminus of a protein, recognized via a specific prenylation motif, and results in the formation of a thioether bond. To identify putative prenylated proteins and investigate changes in their levels of expression, metabolic labeling and subsequent bioorthogonal labeling has become one of the methods of choice. In that strategy, synthetic analogues of biosynthetic precursors for post-translational modification bearing bioorthogonal functionality are added to the growth medium from which they enter cells and become incorporated into proteins. Subsequently, the cells are lysed and proteins bearing the analogues are then covalently modified using selective chemical reagents that react via bioorthogonal processes, allowing a variety of probes for visualization or enrichment to be attached for subsequent analysis. Here, we describe protocols for synthesizing several different isoprenoid analogues and describe how they are metabolically incorporated into mammalian cells, and the incorporation into prenylated proteins visualized via in-gel fluorescence analysis. © 2018 by John Wiley & Sons, Inc.

Indexed as

AlkynesMolecular StructureProtein PrenylationProteinsTerpenesAlkynesProteinsTerpenesalkyne-containing analoguefarnesyl diphosphatefarnesyltransferasegeranylgeranyl diphosphategeranylgeranyltransferaseisoprenoidmetabolic labelingprotein prenylation

Identifiers

PMID30058775
PMCPMC6158066
OpenAlexW2886501703

What Socratic 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 Socratic graph.