Evidence map›Paper›PMID 20965182›Full record

ArticleFEBS letters2010

ATP dependent charge movement in ATP7B Cu+-ATPase is demonstrated by pre-steady state electrical measurements.

Francesco Tadini-Buoninsegni, Gianluca Bartolommei, Maria Rosa Moncelli, Rajendra Pilankatta, David Lewis, Giuseppe Inesi

Open access · bronzeAbstract read
In one paragraph

Article in FEBS letters, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

19 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
  2. Transmembrane Cu(I) P-type ATPase pumps are electrogenic uniporters.Dalton transactions (Cambridge, England : 2003) · 2020
    Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Phosphatidylserine flipping by the P4-ATPase ATP8A2 is electrogenic.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  8. The six metal binding domains in human copper transporter, ATP7B: molecular biophysics and disease-causing mutations.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2017
    Review
  9. Article
  10. Review
  11. Article
  12. Translocation of platinum anticancer drugs by human copper ATPases ATP7A and ATP7B.Angewandte Chemie (International ed. in English) · 2014
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
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

6 authors at 2 institutions in 2 countries.

Francesco Tadini-BuoninsegniDepartment of Chemistry Ugo Schiff, University of Florence, 50019 Sesto Fiorentino, Italy. francesco.tadini@unifi.it
Gianluca Bartolommei
Maria Rosa Moncelli
Rajendra Pilankatta
David Lewis
Giuseppe Inesi
California Pacific Medical Center · USUniversity of Florence · IT

Funding

Molecular and Cellular Studies of Ca2+ Transport ATPaseR01HL069830 · NHLBI · UNIVERSITY OF MARYLAND BALTIMORE · PI INESI, GIUSEPPE · 2002 to 2010
$4.6M
NHLBI NIH HHS R01 HL069830PHS HHS R0301-69830
6 · The paper itself

Abstract

ATP7B is a copper dependent P-type ATPase, required for copper homeostasis. Taking advantage of high yield heterologous expression of recombinant protein, we investigated charge transfer in ATP7B. We detected charge displacement within a single catalytic cycle upon ATP addition and formation of phosphoenzyme intermediate. We attribute this charge displacement to movement of bound copper within ATP7B. Based on specific mutations, we demonstrate that enzyme activation by copper requires occupancy of a site in the N-terminus extension which is not present in other transport ATPases, as well as of a transmembrane site corresponding to the cation binding site of other ATPases.

Indexed as

ElectricityAdenosine TriphosphatasesAdenosine TriphosphateAdsorptionAnimalsCation Transport ProteinsCell MembraneChlorocebus aethiopsCopper-Transporting ATPasesCOS CellsElectric ConductivityElectron TransportHumansMetalsProtein Structure, TertiaryAdenosine TriphosphatasesAdenosine TriphosphateATP7B protein, humanCation Transport ProteinsCopper-Transporting ATPasesMetals

Identifiers

PMID20965182
PMCPMC2981626
OpenAlexW2141342865

What OpenQuestion holds

Textmetadata
LicenceTDM
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.