Evidence map›Paper›PMID 28570513›Full record

ArticleJournal of visualized experiments : JoVE2017

Oligopeptide Competition Assay for Phosphorylation Site Determination.

Min Sung Joo, Ja Hyun Koo, Sol-Bi Shin, Hyungshin Yim, Sang Geon Kim

Abstract readVideo-Audio Media
In one paragraph

Article in Journal of visualized experiments : JoVE, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

5 authors.

Min Sung JooCollege of Pharmacy and Research Institute of Pharmaceutical Sciences, Seoul National University.
Ja Hyun KooCollege of Pharmacy and Research Institute of Pharmaceutical Sciences, Seoul National University.
Sol-Bi ShinCollege of Pharmacy and Institute of Pharmaceutical Science and Technology, Hanyang University.
Hyungshin YimCollege of Pharmacy and Institute of Pharmaceutical Science and Technology, Hanyang University.
Sang Geon KimCollege of Pharmacy and Research Institute of Pharmaceutical Sciences, Seoul National University; sgk@snu.ac.kr.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein phosphorylation at specific sites determines its conformation and interaction with other molecules. Thus, protein phosphorylation affects biological functions and characteristics of the cell. Currently, the most common method for discovering phosphorylation sites is by liquid chromatography/mass spectrometry (LC/MS) analysis, a rapid and sensitive method. However, relatively labile phosphate moieties are often released from phosphopeptides during the fragmentation step, which often yields false-negative signals. In such cases, a traditional in vitro kinase assay using site-directed mutants would be more accurate, but this method is laborious and time-consuming. Therefore, an alternative method using peptide competition may be advantageous. The consensus recognition motif of 5' adenosine monophosphate-activated protein kinase (AMPK) has been established

Indexed as

AMP-Activated Protein KinasesBinding SitesChromatography, LiquidMass SpectrometryOligopeptidesPeptide LibraryPhosphorylationAMP-Activated Protein KinasesOligopeptidesPeptide Library

Identifiers

PMID28570513
PMCPMC5608007

What Socratic 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 Socratic graph.