Evidence map›Paper›PMID 30266947›Full record

ArticleExperimental & molecular medicine2018

A mitochondrial proteome profile indicative of type 2 diabetes mellitus in skeletal muscles.

Sehyun Chae, Su-Jin Kim, Young Do Koo, Jung Hwa Lee, Hokeun Kim, Byung Yong Ahn, Yong-Chan Ha, Yong-Hak Kim, Mi Gyeong Jang, Kyung-Hoi Koo and 7 more

Open access · goldAbstract read
In one paragraph

Article in Experimental & molecular medicine, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed, 2 pooled it
1.9field-weighted citation impact, top 13% 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

35 citing papers in PubMed, 2 syntheses or guidelines pooled it, 49 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Trial
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. SERCA blockade as a treatment strategy for obesity.European journal of applied physiology · 2025
    Review
  10. Article
  11. Mitochondrial Dysfunction in Diabetes: Shedding Light on a Widespread Oversight.Pathophysiology : the official journal of the International Society for Pathophysiology · 2025
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Mitochondrial heterogeneity in diseases.Signal transduction and targeted therapy · 2023
    Review
  18. Article
  19. Article
  20. 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

17 authors at 6 institutions in 3 countries.

Sehyun Chae *Department of New Biology, Daegu Gyeongbuk Institute of Science and Technology, Daegu, 42988, Republic of Korea.
Su-Jin Kim *Department of Chemistry, Research Institute for Natural Sciences, Korea University, Seoul, 136-701, Republic of Korea.
Young Do Koo *Department of Internal Medicine, Seoul National University College of Medicine, Seoul, 03080, Republic of Korea.
Jung Hwa 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.
Byung Yong AhnDepartment of Internal Medicine, Seoul National University College of Medicine, Seoul, 03080, Republic of Korea.
Yong-Chan HaDepartment of Orthopedic Surgery, Seoul National University Bundang Hospital, Seongnam, Gyeonggi-do, 13620, Republic of Korea.
Yong-Hak KimDepartment of Microbiology, Catholic University of Daegu School of Medicine, Daegu, 42472, Republic of Korea.
Mi Gyeong JangDepartment of Molecular Medicine and Biopharmaceutical Sciences, Graduate School of Convergence Science and Technology, Seoul National University, Seoul, 03080, Republic of Korea.ORCID http://orcid.org/0000-0003-3648-656X
Kyung-Hoi KooDepartment of Orthopedic Surgery, Seoul National University Bundang Hospital, Seongnam, Gyeonggi-do, 13620, Republic of Korea.
Sung Hee ChoiDepartment of Internal Medicine, Seoul National University Bundang Hospital, Seongnam, 13620, Republic of Korea.
Soo LimDepartment of Internal Medicine, Seoul National University Bundang Hospital, Seongnam, 13620, Republic of Korea.ORCID http://orcid.org/0000-0002-4137-1671
Young Joo ParkDepartment of Internal Medicine, Seoul National University College of Medicine, Seoul, 03080, Republic of Korea.
Hak Chul JangDepartment of Internal Medicine, Seoul National University Bundang Hospital, Seongnam, 13620, Republic of Korea.
Daehee HwangDepartment of New Biology, Daegu Gyeongbuk Institute of Science and Technology, Daegu, 42988, Republic of Korea. dhwang@dgist.ac.kr.
Sang-Won LeeDepartment of Chemistry, Research Institute for Natural Sciences, Korea University, Seoul, 136-701, Republic of Korea. sw_lee@korea.ac.kr.
Kyong Soo ParkDepartment of Internal Medicine, Seoul National University College of Medicine, Seoul, 03080, Republic of Korea. kspark@snu.ac.kr.ORCID http://orcid.org/0000-0003-3597-342X
Seoul National University Bundang Hospital · KRKorea University · KRSeoul National University · KRDaegu Gyeongbuk Institute of Science and Technology · KRDaegu Catholic University · KRSeoul National University of Science and Technology · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The pathogenesis of type 2 diabetes mellitus (T2DM) is closely associated with mitochondrial functions in insulin-responsive tissues. The mitochondrial proteome, compared with the mitochondrial genome, which only contains 37 genes in humans, can provide more comprehensive information for thousands of mitochondrial proteins regarding T2DM-associated mitochondrial functions. However, T2DM-associated protein signatures in insulin-responsive tissues are still unclear. Here, we performed extensive proteome profiling of mitochondria from skeletal muscles in nine T2DM patients and nine nondiabetic controls. A comparison of the mitochondrial proteomes identified 335 differentially expressed proteins (DEPs) between T2DM and nondiabetic samples. Functional and network analyses of the DEPs showed that mitochondrial metabolic processes were downregulated and mitochondria-associated ER membrane (MAM) processes were upregulated. Of the DEPs, we selected two (NDUFS3 and COX2) for downregulated oxidative phosphorylation and three (CALR, SORT, and RAB1A) for upregulated calcium and protein transport as representative mitochondrial and MAM processes, respectively, and then confirmed their differential expression in independent mouse and human samples. Therefore, we propose that these five proteins be used as a potential protein profile that is indicative of the dysregulation of mitochondrial functions in T2DM, representing downregulated oxidative phosphorylation and upregulated MAM functions.

Indexed as

AnimalsDatabases, ProteinDiabetes Mellitus, Type 2HumansMice, Inbred C57BLMitochondriaMitochondrial ProteinsModels, BiologicalMuscle, SkeletalPeptidesProteomeProteomicsReproducibility of ResultsMitochondrial ProteinsPeptidesProteome

Identifiers

PMID30266947
PMCPMC6162255
OpenAlexW2892870885

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.