Evidence map›Paper›PMID 26657352›Full record

ArticleScientific reports2015

Integrated analysis of global proteome, phosphoproteome, and glycoproteome enables complementary interpretation of disease-related protein networks.

Jong-Moon Park, Ji-Hwan Park, Dong-Gi Mun, Jingi Bae, Jae Hun Jung, Seunghoon Back, Hangyeore Lee, Hokeun Kim, Hee-Jung Jung, Hark Kyun Kim and 4 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

16 citing papers in PubMed, 34 citations in OpenAlex.

  1. Review
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  12. Sweet and SourFrontiers in microbiology · 2019
    Article
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  16. Diacylglycerol Kinase-ε: Properties and Biological Roles.Frontiers in cell and developmental biology · 2016
    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

14 authors at 6 institutions in 1 country.

Jong-Moon ParkDepartment of Pharmaceutics, College of Pharmacy, Gachon University, Incheon 406-799, Republic of Korea.
Ji-Hwan ParkDepartment of Chemical Engineering, POSTECH, Pohang 790-784, Republic of Korea.
Dong-Gi MunDepartment of Chemistry, Research Institute for Natural Sciences, Korea University, Seoul 136-701, Republic of Korea.
Jingi BaeDepartment of Chemistry, Research Institute for Natural Sciences, Korea University, Seoul 136-701, Republic of Korea.
Jae Hun JungDepartment of Applied Chemistry, College of Applied Sciences, Kyung Hee University, Yong-in 446-701, Republic of Korea.
Seunghoon BackDepartment of Chemistry, Research Institute for Natural Sciences, Korea University, Seoul 136-701, Republic of Korea.
Hangyeore LeeDepartment of Chemistry, Research Institute for Natural Sciences, Korea University, Seoul 136-701, Republic of Korea.
Hokeun KimDepartment of Chemistry, Research Institute for Natural Sciences, Korea University, Seoul 136-701, Republic of Korea.
Hee-Jung JungDepartment of New Biology and Center for Plant Aging Research, Institute for Basic Science, DGIST, Daegu 711-873, Republic of Korea.
Hark Kyun KimNational Cancer Center, Goyang 410-769, Republic of Korea.
Hookeun LeeDepartment of Pharmaceutics, College of Pharmacy, Gachon University, Incheon 406-799, Republic of Korea.
Kwang Pyo KimDepartment of Applied Chemistry, College of Applied Sciences, Kyung Hee University, Yong-in 446-701, Republic of Korea.
Daehee HwangDepartment of Chemical Engineering, POSTECH, Pohang 790-784, Republic of Korea.
Sang-Won LeeDepartment of Chemistry, Research Institute for Natural Sciences, Korea University, Seoul 136-701, Republic of Korea.
Korea University · KRDaegu Gyeongbuk Institute of Science and Technology · KRKyung Hee University · KRNational Cancer Center · KRGachon University · KRPohang University of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Multi-dimensional proteomic analyses provide different layers of protein information, including protein abundance and post-translational modifications. Here, we report an integrated analysis of protein expression, phosphorylation, and N-glycosylation by serial enrichments of phosphorylation and N-glycosylation (SEPG) from the same tissue samples. On average, the SEPG identified 142,106 unmodified peptides of 8,625 protein groups, 18,846 phosphopeptides (15,647 phosphosites), and 4,019 N-glycopeptides (2,634 N-glycosites) in tumor and adjacent normal tissues from three gastric cancer patients. The combined analysis of these data showed that the integrated analysis additively improved the coverages of gastric cancer-related protein networks; phosphoproteome and N-glycoproteome captured predominantly low abundant signal proteins, and membranous or secreted proteins, respectively, while global proteome provided abundances for general population of the proteome. Therefore, our results demonstrate that the SEPG can serve as an effective approach for multi-dimensional proteome analyses, and the holistic profiles of protein expression and PTMs enabled improved interpretation of disease-related networks by providing complementary information.

Indexed as

Protein Interaction MappingProtein Interaction MapsProteomeProteomicsAdultCluster AnalysisFemaleGlycoproteinsHumansMaleMiddle AgedModels, BiologicalPhosphoproteinsStomach NeoplasmsGlycoproteinsPhosphoproteinsProteome

Identifiers

PMID26657352
PMCPMC4676070
OpenAlexW2286926891

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.