Evidence map›Paper›PMID 37238591›Full record

ArticleBiomolecules2023

NMR and Patch-Clamp Characterization of Yeast Mitochondrial Pyruvate Carrier Complexes.

Zhen Wang, Wen Ding, Maosen Ruan, Yong Liu, Jing Yang, Huiqin Zhang, Bing Shen, Junfeng Wang, Yunyan Li

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

Article in Biomolecules, 2023. 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 77% 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, 0 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

9 authors at 4 institutions in 1 country.

Zhen WangHigh Magnetic Field Laboratory, CAS Key Laboratory of High Magnetic Field and Ion Beam Physical Biology, Hefei Institutes of Physical Science, Chinese Academy of Sciences, Hefei 230031, China.
Wen DingSchool of Basic Medical Sciences, Anhui Medical University, Hefei 230032, China.
Maosen RuanHigh Magnetic Field Laboratory, CAS Key Laboratory of High Magnetic Field and Ion Beam Physical Biology, Hefei Institutes of Physical Science, Chinese Academy of Sciences, Hefei 230031, China.ORCID 0009-0005-1298-6414
Yong LiuHigh Magnetic Field Laboratory, CAS Key Laboratory of High Magnetic Field and Ion Beam Physical Biology, Hefei Institutes of Physical Science, Chinese Academy of Sciences, Hefei 230031, China.
Jing YangHigh Magnetic Field Laboratory, CAS Key Laboratory of High Magnetic Field and Ion Beam Physical Biology, Hefei Institutes of Physical Science, Chinese Academy of Sciences, Hefei 230031, China.ORCID 0000-0003-4664-5528
Huiqin ZhangHigh Magnetic Field Laboratory, CAS Key Laboratory of High Magnetic Field and Ion Beam Physical Biology, Hefei Institutes of Physical Science, Chinese Academy of Sciences, Hefei 230031, China.
Bing ShenSchool of Basic Medical Sciences, Anhui Medical University, Hefei 230032, China.ORCID 0000-0001-7263-4748
Junfeng WangHigh Magnetic Field Laboratory, CAS Key Laboratory of High Magnetic Field and Ion Beam Physical Biology, Hefei Institutes of Physical Science, Chinese Academy of Sciences, Hefei 230031, China.ORCID 0000-0002-9608-6851
Yunyan LiHigh Magnetic Field Laboratory, CAS Key Laboratory of High Magnetic Field and Ion Beam Physical Biology, Hefei Institutes of Physical Science, Chinese Academy of Sciences, Hefei 230031, China.ORCID 0000-0003-0029-6035
Chinese Academy of Sciences · CNUniversity of Science and Technology of China · CNAnhui Medical University · CNAnhui University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mitochondrial pyruvate carrier (Mpc) plays an indispensable role in the transport of pyruvates across the mitochondrial inner membrane. Despite the two distinct homologous proteins, Mpc1 and Mpc2, were identified in 2012, there are still controversies on the basic functional units and oligomeric state of Mpc complexes. In this study, yeast Mpc1 and Mpc2 proteins were expressed in a prokaryotic heterologous system. Both homo- and hetero-dimers were successfully reconstituted in mixed detergents. Interactions among Mpc monomers were recorded utilizing paramagnetic relaxation enhancement (PRE) nuclear magnetic resonance (NMR) methods. By single-channel patch-clamp assays, we discovered that both the Mpc1-Mpc2 hetero-dimer and Mpc1 homo-dimer are able to transport K

Indexed as

Monocarboxylic Acid TransportersSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAnion Transport ProteinsMagnetic Resonance SpectroscopyMembrane ProteinsMitochondrial Membrane Transport ProteinsPhosphotransferases (Alcohol Group Acceptor)PyruvatesAnion Transport ProteinsGPI13 protein, S cerevisiaeMembrane ProteinsMitochondrial Membrane Transport ProteinsMonocarboxylic Acid TransportersMPC2 protein, S cerevisiaePhosphotransferases (Alcohol Group Acceptor)PyruvatesSaccharomyces cerevisiae ProteinsMpcNMRoligomeric statepatch-clampPREprotein interactions

Identifiers

PMID37238591
PMCPMC10216714
OpenAlexW4366832847

What Socratic 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 Socratic graph.