Evidence map›Paper›PMID 33176830›Full record

ArticleMolecular brain2020

Functional identification of potential non-canonical N-glycosylation sites within Ca

Vendula Ficelova, Ivana A Souza, Leos Cmarko, Maria A Gandini, Robin N Stringer, Gerald W Zamponi, Norbert Weiss

Open access · goldAbstract read
In one paragraph

Article in Molecular brain, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.7field-weighted citation impact, top 32% 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

8 citing papers in PubMed, 10 citations in OpenAlex.

  1. Structural basis for human CaCell research · 2024
    Article
  2. The T-type calcium channelosome.Pflugers Archiv : European journal of physiology · 2024
    Review
  3. Review
  4. Regulation of CaPflugers Archiv : European journal of physiology · 2022
    Article
  5. Review
  6. Article
  7. Targeting T-type/CaV3.2 channels for chronic pain.Translational research : the journal of laboratory and clinical medicine · 2021
    Review
  8. The life cycle of voltage-gated CaNeuronal signaling · 2021
    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

7 authors at 3 institutions in 2 countries.

Vendula FicelovaInstitute of Biology and Medical Genetics, First Faculty of Medicine, Charles University, Prague, Czech Republic.
Ivana A SouzaDepartment of Physiology and Pharmacology, Cumming School of Medicine, University of Calgary, Calgary, Canada.
Leos CmarkoInstitute of Biology and Medical Genetics, First Faculty of Medicine, Charles University, Prague, Czech Republic.
Maria A GandiniDepartment of Physiology and Pharmacology, Cumming School of Medicine, University of Calgary, Calgary, Canada.
Robin N StringerInstitute of Biology and Medical Genetics, First Faculty of Medicine, Charles University, Prague, Czech Republic.
Gerald W ZamponiDepartment of Physiology and Pharmacology, Cumming School of Medicine, University of Calgary, Calgary, Canada.ORCID 0000-0002-0644-9066
Norbert WeissInstitute of Biology and Medical Genetics, First Faculty of Medicine, Charles University, Prague, Czech Republic. weiss@uochb.cas.cz.ORCID 0000-0002-0040-1109
Charles University · CZUniversity of Calgary · CACzech Academy of Sciences · CZ

Funding

CIHR
6 · The paper itself

Abstract

Low-voltage-activated T-type calcium channels are important contributors to nervous system function. Post-translational modification of these channels has emerged as an important mechanism to control channel activity. Previous studies have documented the importance of asparagine (N)-linked glycosylation and identified several asparagine residues within the canonical consensus sequence N-X-S/T that is essential for the expression and function of Ca

Indexed as

Amino Acid MotifsAsparagineCalcium Channels, T-TypeGlycosylationHumansStructure-Activity RelationshipAsparagineCACNA1H protein, humanCalcium Channels, T-TypeAsparagine-linked glycosylationCalcium channelcav3.2 ChannelN-glycosylationNon-canonical glycosylationTraffickingT-type channel

Identifiers

PMID33176830
PMCPMC7659234
OpenAlexW3103944527

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.