Evidence map›Paper›PMID 29409909›Full record

ArticleBiochimica et biophysica acta. Biomembranes2018

Threonine 67 is a key component in the coupling of the NSS amino acid transporter KAAT1.

M Giovanola, A Vollero, R Cinquetti, E Bossi, L R Forrest, E S Di Cairano, M Castagna

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Biochimica et biophysica acta. Biomembranes, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Article
  2. The "www" ofMembranes · 2022
    Review
  3. 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

7 authors.

M GiovanolaDepartment of Pharmacological and Biomolecular Sciences, Università degli Studi di Milano, Via Trentacoste 2, 20134, Milano, Italy.
A VolleroDepartment of Biotechnology and Life Sciences, University of Insubria, Via J.H. Dunant 3, 21100, Varese, Italy.
R CinquettiDepartment of Biotechnology and Life Sciences, University of Insubria, Via J.H. Dunant 3, 21100, Varese, Italy.
E BossiDepartment of Biotechnology and Life Sciences, University of Insubria, Via J.H. Dunant 3, 21100, Varese, Italy.
L R ForrestComputational Structural Biology Section, NIH NINDS, 35 Convent Drive, Bethesda, MD 20892-3761, USA.
E S Di CairanoDepartment of Pharmacological and Biomolecular Sciences, Università degli Studi di Milano, Via Trentacoste 2, 20134, Milano, Italy.
M CastagnaDepartment of Pharmacological and Biomolecular Sciences, Università degli Studi di Milano, Via Trentacoste 2, 20134, Milano, Italy. Electronic address: Michela.Castagna@unimi.it.

Funding

Computational Studies of Membrane Transport ProteinsZIANS003139 · NINDS · NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE · PI FORREST, LUCY · 2014 to 2025
$13.7M
Intramural NIH HHS ZIA NS003139
6 · The paper itself

Abstract

PubMed holds no abstract for this paper.

Indexed as

Protein Interaction Domains and MotifsAmino Acid SequenceAmino Acid Transport Systems, NeutralAnimalsBiological TransportFemaleInsect ProteinsIon Channel GatingManducaMembrane PotentialsOocytesProtein BindingThreonineXenopus laevisAmino Acid Transport Systems, NeutralInsect ProteinsKAAT1 protein, insectThreonineAmino acid uptakeHomology modelIon selectivityNSS familyStructure-function analysis, coupling mechanismXenopus laevis oocytes

Identifiers

PMID29409909
PMCPMC6166433

What OpenQuestion holds

Textmetadata
LicenceTDM
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.