Evidence map›Paper›PMID 28118712›Full record

ArticleThe journal of physical chemistry. B2017

Effect of Dimerization on the Dynamics of Neurotransmitter:Sodium Symporters.

Mert Gur, Mary Hongying Cheng, Elia Zomot, Ivet Bahar

Abstract read
In one paragraph

Article in The journal of physical chemistry. B, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

14 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Oligomerization of Monoamine Transporters.Sub-cellular biochemistry · 2024
    Review
  3. Review
  4. Review
  5. Article
  6. SLC6 transporter oligomerization.Journal of neurochemistry · 2021
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Shared dynamics of LeuT superfamily members and allosteric differentiation by structural irregularities and multimerization.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Article
  12. Article
  13. Article
  14. 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

4 authors at 2 institutions in 3 countries.

Mert GurDepartment of Computational and Systems Biology, School of Medicine, University of Pittsburgh , Pittsburgh, Pennsylvania 15260, United States.ORCID 0000-0003-0983-4397
Mary Hongying ChengDepartment of Computational and Systems Biology, School of Medicine, University of Pittsburgh , Pittsburgh, Pennsylvania 15260, United States.
Elia ZomotDepartment of Biomolecular Sciences, Weizmann Institute of Science , Rehovot 7610001, Israel.
Ivet BaharDepartment of Computational and Systems Biology, School of Medicine, University of Pittsburgh , Pittsburgh, Pennsylvania 15260, United States.
University of Pittsburgh · USWeizmann Institute of Science · IL

Funding

TrainingP41GM103712 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI AYOOB, JOSEPH C · 2012 to 2021
$16.3M
NIDA Center of Excellence OF Computational Drug Abuse Research (CDAR)P30DA035778 · NIDA · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI BAHAR, IVET, XIE, XIANG-QUN · 2014 to 2018
$5.4M
Continued Development of Protein Dynamics Software ProDyR01GM099738 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI BAHAR, IVET · 2012 to 2015
$1.1M
NIDA NIH HHS P30 DA035778NIGMS NIH HHS P41 GM103712NIGMS NIH HHS R01 GM099738
6 · The paper itself

Abstract

Dimerization is a common feature among the members of the neurotransmitter:sodium symporter (NSS) family of membrane proteins. Yet, the effect of dimerization on the mechanism of action of NSS members is not fully understood. In this study, we examined the collective dynamics of two members of the family, leucine transporter (LeuT) and dopamine transporter (DAT), to assess the significance of dimerization in modulating the functional motions of the monomers. We used to this aim the anisotropic network model (ANM), an efficient and robust method for modeling the intrinsic motions of proteins and their complexes. Transporters belonging to the NSS family are known to alternate between outward-facing (OF) and inward-facing (IF) states, which enables the uptake and release of their substrate (neurotransmitter) respectively, as the substrate is transported from the exterior to the interior of the cell. In both LeuT and DAT, dimerization is found to alter the collective motions intrinsically accessible to the individual monomers in favor of the functional transitions (OF ↔ IF), suggesting that dimerization may play a role in facilitating transport.

Indexed as

Molecular Dynamics SimulationProtein MultimerizationAnisotropyNeurotransmitter AgentsSodiumSymportersNeurotransmitter AgentsSodiumSymporters

Identifiers

PMID28118712
PMCPMC5402697
OpenAlexW2580159849

What OpenQuestion holds

Textmetadata
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.