Evidence map›Paper›PMID 30755463›Full record

ArticleThe Biochemical journal2019

The lipid head group is the key element for substrate recognition by the P4 ATPase ALA2: a phosphatidylserine flippase.

Lisa Theorin, Kristina Faxén, Danny Mollerup Sørensen, Rebekka Migotti, Gunnar Dittmar, Jürgen Schiller, David L Daleke, Michael Palmgren, Rosa Laura López-Marqués, Thomas Günther Pomorski

Open access · hybridAbstract read
In one paragraph

Article in The Biochemical journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing 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

10 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. 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 4 institutions in 3 countries.

Lisa TheorinDepartment of Plant and Environmental Sciences, University of Copenhagen, Copenhagen, Denmark.
Kristina FaxénDepartment of Plant and Environmental Sciences, University of Copenhagen, Copenhagen, Denmark.
Danny Mollerup SørensenDepartment of Plant and Environmental Sciences, University of Copenhagen, Copenhagen, Denmark.
Rebekka MigottiMax-Delbrück Centrum for Molecular Medicine, Berlin, Germany.
Gunnar DittmarMax-Delbrück Centrum for Molecular Medicine, Berlin, Germany.
Jürgen SchillerInstitute of Medical Physics and Biophysics, University of Leipzig, Leipzig, Germany.
David L DalekeMedical Sciences/Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Bloomington, IN, U.S.A.
Michael PalmgrenDepartment of Plant and Environmental Sciences, University of Copenhagen, Copenhagen, Denmark.
Rosa Laura López-MarquésDepartment of Plant and Environmental Sciences, University of Copenhagen, Copenhagen, Denmark rlo@plen.ku.dk Thomas.Guenther-Pomorski@rub.de.
Thomas Günther PomorskiDepartment of Plant and Environmental Sciences, University of Copenhagen, Copenhagen, Denmark rlo@plen.ku.dk Thomas.Guenther-Pomorski@rub.de.
University of Copenhagen · DKMax Delbrück Center · DELeipzig University · DERuhr University Bochum · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Type IV P-type ATPases (P4 ATPases) are lipid flippases that catalyze phospholipid transport from the exoplasmic to the cytoplasmic leaflet of cellular membranes, but the mechanism by which they recognize and transport phospholipids through the lipid bilayer remains unknown. In the present study, we succeeded in purifying recombinant aminophospholipid ATPase 2 (ALA2), a member of the P4 ATPase subfamily in

Indexed as

Adenosine TriphosphatasesArabidopsisArabidopsis ProteinsPhosphatidylserinesPhospholipid Transfer ProteinsProtein DomainsRecombinant ProteinsAdenosine TriphosphatasesArabidopsis ProteinsAVI1 protein, ArabidopsisPhosphatidylserinesPhospholipid Transfer ProteinsRecombinant ProteinsArabidopsis thalianaFLAG-tag purificationlipid flippaselysophospholipidmembrane protein complex

Identifiers

PMID30755463
PMCPMC6402034
OpenAlexW2911693410

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.