Evidence map›Paper›PMID 29752403›Full record

ArticleThe Journal of biological chemistry2018

Cryo-EM structure of the cytoplasmic domain of murine transient receptor potential cation channel subfamily C member 6 (TRPC6).

Caleigh M Azumaya, Francisco Sierra-Valdez, Julio F Cordero-Morales, Terunaga Nakagawa

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

32 citing papers in PubMed, 53 citations in OpenAlex.

  1. Review
  2. Article
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  8. Review
  9. Vascular mechanotransduction.Physiological reviews · 2023
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Sequence-assignment validation in cryo-EM models with checkMySequence.Acta crystallographica. Section D, Structural biology · 2022
    Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Imaging the kidney: from light to super-resolution microscopy.Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association · 2021
    Review
  20. 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

4 authors at 3 institutions in 1 country.

Caleigh M AzumayaFrom the Department of Molecular Physiology and Biophysics.
Francisco Sierra-ValdezDepartment of Physiology, University of Tennessee Health Science Center, Memphis, Tennessee 38163.
Julio F Cordero-MoralesDepartment of Physiology, University of Tennessee Health Science Center, Memphis, Tennessee 38163 jcordero@uthsc.edu.
Terunaga NakagawaFrom the Department of Molecular Physiology and Biophysics, terunaga.nakagawa@vanderbilt.edu.
University of Tennessee Health Science Center · USVanderbilt Health · USVanderbilt University · US

Funding

MOLECULAR BIOPHYSICS TRAINING PROGRAM AT VANDERBILTT32GM008320 · NIGMS · VANDERBILT UNIVERSITY · PI CHAZIN, WALTER J. · 1989 to 2023
$7.9M
The Role of Bioactive Lipids in Transient Receptor Potential Channels GatingR01GM125629 · NIGMS · UNIVERSITY OF TENNESSEE HEALTH SCI CTR · PI CORDERO-MORALES, JULIO F · 2018 to 2022
$1.5M
Molecular Anatomy of Mature and Immature Glutamate ReceptorsR01HD061543 · NICHD · VANDERBILT UNIVERSITY · PI NAKAGAWA, TERUNAGA · 2010 to 2014
$1.5M
Network-Attached Biomedical Research Data Management SystemS10RR031634 · NCRR · VANDERBILT UNIVERSITY · PI SMITH, JARROD ANSON · 2011 to 2011
$600k
NCRR NIH HHS S10 RR031634NICHD NIH HHS R01 HD061543NIGMS NIH HHS R01 GM125629NIGMS NIH HHS T32 GM008320
6 · The paper itself

Abstract

The kidney maintains the internal milieu by regulating the retention and excretion of proteins, ions, and small molecules. The glomerular podocyte forms the slit diaphragm of the ultrafiltration filter, whose damage leads to progressive kidney failure and focal segmental glomerulosclerosis (FSGS). The canonical transient receptor potential 6 (TRPC6) ion channel is expressed in the podocyte, and mutations in its cytoplasmic domain cause FSGS in humans.

Indexed as

Cryoelectron MicroscopyAnimalsCytoplasmHEK293 CellsHumansMiceMutationProtein DomainsTRPC6 Cation ChannelTRPC6 Cation Channelcalcium channelcryo-electron microscopyelectrophysiologyglomerulosclerosision channelkidneymembrane proteinpurificationtransient receptor potential channels (TRP channels)TRPC6vasoconstriction

Identifiers

PMID29752403
PMCPMC6028952
OpenAlexW2799964739

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.