Evidence map›Paper›PMID 33202651›Full record

ArticleMolecules (Basel, Switzerland)2020

LC-MS Quantification of Site-Specific Phosphorylation Degree by Stable-Isotope Dimethyl Labeling Coupled with Phosphatase Dephosphorylation.

Sin-Hong Chen, Ya-Chi Lin, Ming-Kuei Shih, Li-Fei Wang, Shyh-Shyan Liu, Jue-Liang Hsu

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecules (Basel, Switzerland), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact, top 89% 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

1 citing paper in PubMed, 2 citations in OpenAlex.

  1. 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

6 authors at 2 institutions in 1 country.

Sin-Hong ChenDepartment of Veterinary Medicine, National Pingtung University of Science and Technology, Pingtung 91201, Taiwan.
Ya-Chi LinDepartment of Biological Science and Technology, National Pingtung University of Science and Technology, Pingtung 91201, Taiwan.
Ming-Kuei ShihGraduate Institute of Food Culture and Innovation, National Kaohsiung University of Hospitality and Tourism, Kaohsiung 81271, Taiwan.ORCID 0000-0001-5830-8591
Li-Fei WangHospitality and Tourism Research Center, National Kaohsiung University of Hospitality and Tourism, Kaohsiung 81271, Taiwan.ORCID 0000-0001-5106-5865
Shyh-Shyan LiuDepartment of Veterinary Medicine, National Pingtung University of Science and Technology, Pingtung 91201, Taiwan.
Jue-Liang HsuDepartment of Biological Science and Technology, National Pingtung University of Science and Technology, Pingtung 91201, Taiwan.ORCID 0000-0002-6771-6690
National Pingtung University of Science and Technology · TWNational Kaohsiung University of Hospitality and Tourism · TW

Funding

Ministry of Science and Technology, Taiwan MOST 108-2113-M-020-001 & MOST 108-3017-F-020-001
6 · The paper itself

Abstract

Protein phosphorylation is a crucial post-translational modification that plays an important role in the regulation of cellular signaling processes. Site-specific quantitation of phosphorylation levels can help decipher the physiological functions of phosphorylation modifications under diverse physiological statuses. However, quantitative analysis of protein phosphorylation degrees is still a challenging task due to its dynamic nature and the lack of an internal standard simultaneously available for the samples differently prepared for various phosphorylation extents. In this study, stable-isotope dimethyl labeling coupled with phosphatase dephosphorylation (DM + deP) was tried to determine the site-specific degrees of phosphorylation in proteins. Firstly, quantitation accuracy of the (DM + deP) approach was confirmed using synthetic peptides of various simulated phosphorylation degrees. Afterwards, it was applied to evaluate the phosphorylation stoichiometry of milk caseins. The phosphorylation degree of Ser130 on α-S1-casein was also validated by absolute quantification with the corresponding synthetic phosphorylated and nonphosphorylated peptides under a selected reaction monitoring (SRM) mode. Moreover, this (DM + deP) method was used to detect the phosphorylation degree change of Ser82 on the Hsp27 protein of HepG2 cells caused by

Indexed as

Isotope LabelingAmino Acid SequenceCaseinsChromatography, LiquidHep G2 CellsHSP27 Heat-Shock ProteinsHumansPeptidesPhosphoric Monoester HydrolasesPhosphorylationPhosphoserineReproducibility of ResultsTandem Mass Spectrometrytert-ButylhydroperoxideCaseinsHSP27 Heat-Shock ProteinsPeptidesPhosphoric Monoester HydrolasesPhosphoserinetert-ButylhydroperoxideLC-MSphosphatase dephosphorylationphosphorylation degreeSRMstable-isotope dimethyl labeling

Identifiers

PMID33202651
PMCPMC7697701
OpenAlexW3104868141

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.