Evidence map›Paper›PMID 32499574›Full record

ArticleScientific reports2020

S92 phosphorylation induces structural changes in the N-terminus domain of human mitochondrial calcium uniporter.

Youngjin Lee, Jongseo Park, Gihwan Lee, Sanghwa Yoon, Choon Kee Min, Tae Gyun Kim, Takenori Yamamoto, Do Han Kim, Keun Woo Lee, Soo Hyun Eom

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

11 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Sodium citrate targeting CaJournal of advanced research · 2024
    Article
  6. Article
  7. Review
  8. Review
  9. Mitochondrial CaArteriosclerosis, thrombosis, and vascular biology · 2022
    Article
  10. Article
  11. 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

10 authors at 4 institutions in 2 countries.

Youngjin Lee *School of Life Sciences, Gwangju Institute of Science and Technology (GIST), Buk-gu, Gwangju, 61005, Republic of Korea. yjlee86@kribb.re.kr.
Jongseo Park *School of Life Sciences, Gwangju Institute of Science and Technology (GIST), Buk-gu, Gwangju, 61005, Republic of Korea.
Gihwan LeeDivision of Life Science, Division of Applied Life Science (BK21 Plus), Plant Molecular Biology and Biotechnology Research Center (PMBBRC), Research Institute of Natural Science (RINS), Gyeongsang National University (GNU), 501 Jinju-daero, Jinju, 52828, Republic of Korea.
Sanghwa YoonDivision of Life Science, Division of Applied Life Science (BK21 Plus), Plant Molecular Biology and Biotechnology Research Center (PMBBRC), Research Institute of Natural Science (RINS), Gyeongsang National University (GNU), 501 Jinju-daero, Jinju, 52828, Republic of Korea.
Choon Kee MinSchool of Life Sciences, Gwangju Institute of Science and Technology (GIST), Buk-gu, Gwangju, 61005, Republic of Korea.
Tae Gyun KimSchool of Life Sciences, Gwangju Institute of Science and Technology (GIST), Buk-gu, Gwangju, 61005, Republic of Korea.
Takenori YamamotoInstitute for Genome Research, Tokushima University, Kuramotocho-3, Tokushima, 770-8503, Japan.
Do Han KimSchool of Life Sciences, Gwangju Institute of Science and Technology (GIST), Buk-gu, Gwangju, 61005, Republic of Korea.
Keun Woo LeeDivision of Life Science, Division of Applied Life Science (BK21 Plus), Plant Molecular Biology and Biotechnology Research Center (PMBBRC), Research Institute of Natural Science (RINS), Gyeongsang National University (GNU), 501 Jinju-daero, Jinju, 52828, Republic of Korea.
Soo Hyun EomSchool of Life Sciences, Gwangju Institute of Science and Technology (GIST), Buk-gu, Gwangju, 61005, Republic of Korea. eom@gist.ac.kr.
Gwangju Institute of Science and Technology · KRGyeongsang National University · KROkinawa Institute of Science and Technology Graduate University · JPTokushima University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mitochondrial calcium uniporter (MCU) plays essential roles in mitochondrial calcium homeostasis and regulates cellular functions, such as energy synthesis, cell growth, and development. Thus, MCU activity is tightly controlled by its regulators as well as post-translational modification, including phosphorylation by protein kinases such as proline-rich tyrosine kinase 2 (Pyk2) and AMP-activated protein kinase (AMPK). In our in vitro kinase assay, the MCU N-terminal domain (NTD) was phosphorylated by protein kinase C isoforms (PKC

Indexed as

Calcium ChannelsCrystallography, X-RayDimerizationHumansHydrogen BondingMitochondriaMolecular Dynamics SimulationMutagenesis, Site-DirectedPhosphorylationProtein DomainsProtein IsoformsProtein Kinase CProtein Structure, TertiaryStatic ElectricityCalcium Channelsmitochondrial calcium uniporterProtein IsoformsProtein Kinase C

Identifiers

PMID32499574
PMCPMC7272466
OpenAlexW3033740613

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.