Evidence map›Paper›PMID 40992846›Full record

ArticleMethods in enzymology2025

Profiling of C-terminal prenylated proteins using tandem mass tagging.

Harinarayanan Kottala, Yuanzhe Chen, Mark D Distefano

Abstract read
In one paragraph

Article in Methods in enzymology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

3 authors.

Harinarayanan KottalaUniversity of Minnesota, Twin Cities, Minneapolis, MN, United States.
Yuanzhe ChenUniversity of Minnesota, Twin Cities, Minneapolis, MN, United States.
Mark D DistefanoUniversity of Minnesota, Twin Cities, Minneapolis, MN, United States. Electronic address: diste001@umn.edu.

Funding

Chemical Approaches for Exploring Protein Prenylation in Living CellsR35GM141853 · NIGMS · UNIVERSITY OF MINNESOTA · PI MARK D DISTEFANO · 2021 to 2026
$2.4M
NIGMS NIH HHS R35 GM141853
6 · The paper itself

Abstract

Protein prenylation is a crucial post translational modification that involves the attachment of one or two isoprenoid groups at the C-terminus of a protein, facilitating membrane localization and regulating protein function. Consequently, prenylation is linked to numerous diseases. Identification of prenylated proteins and their quantification is crucial to defining the role of prenylation in these diseases and therapy development. Here, a method for profiling and quantifying prenylated proteins using a bio-orthogonal probe is described. The workflow consists of metabolic incorporation of the probe and click chemistry-mediated biotinylation followed by streptavidin purification and LC-MS

Indexed as

Protein PrenylationProteinsProteomicsTandem Mass SpectrometryAnimalsBiotinBiotinylationChromatography, LiquidClick ChemistryHumansStreptavidinBiotinProteinsStreptavidinFarnesylationGeranylgeranylationPost-translational modificationPrenylationTandem mass tagging

Identifiers

PMID40992846
PMCPMC12497479

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.