Evidence map›Paper›PMID 22253360›Full record

ArticleThe journal of histochemistry and cytochemistry : official journal of the Histochemistry Society2012

Cellular localization and biochemical analysis of mammalian CDC50A, a glycosylated β-subunit for P4 ATPases.

Dineke E Folmer, Kam S Mok, Sebastiaan W de Wee, Suzanne Duijst, Johan K Hiralall, Jurgen Seppen, Ronald P J Oude Elferink, Coen C Paulusma

Open access · bronzeAbstract read
In one paragraph

Article in The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society, 2012. 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
0.9field-weighted citation impact, top 25% 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, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. The phosphatidylserine flippase β-subunit Tmem30a is essential for normal insulin maturation and secretion.Molecular therapy : the journal of the American Society of Gene Therapy · 2021
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. P4 ATPases: flippases in health and disease.International journal of molecular sciences · 2013
    Review
  14. 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

8 authors at 1 institution in 1 country.

Dineke E FolmerTytgat Institute for Liver and Intestinal Research, Academic Medical Center, Amsterdam, Netherlands.
Kam S Mok
Sebastiaan W de Wee
Suzanne Duijst
Johan K Hiralall
Jurgen Seppen
Ronald P J Oude Elferink
Coen C Paulusma
Academic Medical Center · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

CDC50 proteins are β-subunits for P4 ATPases, which upon heterodimerization form a functional phospholipid translocation complex. Emerging evidence in mouse models and men links mutations in P4 ATPase genes with human disease. This study analyzed the tissue distribution and cellular localization of CDC50A, the most abundant and ubiquitously expressed CDC50 homologue in the mouse. The authors have raised antibodies that detect mouse and human CDC50A and studied CDC50A localization and glycosylation status in mouse liver cells. CDC50A is a terminal-glycosylated glycoprotein and is expressed in hepatocytes and liver sinusoidal endothelial cells, where it resides in detergent-resistant membranes. In pancreas and stomach, CDC50A localized to secretory vesicles, whereas in the kidney, CDC50A localized to the apical region of proximal convoluted tubules of the cortex. In WIF-B9 cells, CDC50A partially costains with the trans-Golgi network. Data suggest that CDC50A is present as a fully glycosylated protein in vivo, which presumes interaction with distinct P4 ATPases.

Indexed as

Adenosine TriphosphatasesAnimalsBlotting, WesternCell LineCell MembraneCricetinaeEndothelial CellsGastric MucosaGlycosylationHepatocytesHumansImmunohistochemistryIsoenzymesKidneyLiverMembrane ProteinsAdenosine TriphosphatasesIsoenzymesMembrane ProteinsTMEM30a protein, humanTMEM30a protein, mouseTmem30c protein, mouse

Identifiers

PMID22253360
PMCPMC3351125
OpenAlexW2021284579

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.