Evidence map›Paper›PMID 23060447›Full record

ArticleThe Journal of biological chemistry2012

Biochemical characterization of P4-ATPase mutations identified in patients with progressive familial intrahepatic cholestasis.

Alex Stone, Christopher Chau, Christian Eaton, Emily Foran, Mridu Kapur, Edward Prevatt, Nathan Belkin, David Kerr, Torvald Kohlin, Patrick Williamson

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.1field-weighted citation impact, top 22% 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

12 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Directed evolution of a sphingomyelin flippase reveals mechanism of substrate backbone discrimination by a P4-ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  8. Article
  9. P4-ATPases: lipid flippases in cell membranes.Pflugers Archiv : European journal of physiology · 2014
    Review
  10. P4 ATPases: flippases in health and disease.International journal of molecular sciences · 2013
    Review
  11. Article
  12. Decoding P4-ATPase substrate interactions.Critical reviews in biochemistry and molecular biology
    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

10 authors at 1 institution in 1 country.

Alex StoneDepartment of Biology, Amherst College, Amherst, Massachusetts 01002, USA.
Christopher Chau
Christian Eaton
Emily Foran
Mridu Kapur
Edward Prevatt
Nathan Belkin
David Kerr
Torvald Kohlin
Patrick Williamson
Amherst College · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Mutations in the P4-ATPase ATP8B1 cause the inherited liver disease progressive familial intrahepatic cholestasis. Several of these mutations are located in conserved regions of the transmembrane domain associated with substrate binding and transport. Assays for P4-ATPase-mediated transport in living yeast cells were developed and used to characterize the specificity and kinetic parameters of this transport. Progressive familial intrahepatic cholestasis mutations were introduced into the yeast plasma membrane P4-ATPase Dnf2p, and the effect of these mutations on its catalysis of phospholipid transport were determined. The results of these measurements have implications for the basis of the disease and for the mechanism of phospholipid transit through the enzyme during the reaction cycle.

Indexed as

MutationAdenosine TriphosphatasesAmino Acid SequenceATP-Binding Cassette TransportersCholestasis, IntrahepaticHumansKineticsMolecular Sequence DataPhenotypePhospholipidsRegression AnalysisSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSubstrate SpecificityAdenosine TriphosphatasesATP8B1 protein, humanATP-Binding Cassette TransportersCDC50 protein, S cerevisiaeDnf2 protein, S cerevisiaePhospholipidsSaccharomyces cerevisiae Proteins

Identifiers

PMID23060447
PMCPMC3510814
OpenAlexW2076155632

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.