Evidence map›Paper›PMID 25242165›Full record

ReviewThe Biochemical journal2014

Biochemical characterization of P-type copper ATPases.

Giuseppe Inesi, Rajendra Pilankatta, Francesco Tadini-Buoninsegni

Open access · hybridAbstract readReview
In one paragraph

Review in The Biochemical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.5field-weighted citation impact, top 8% 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

27 citing papers in PubMed, 52 citations in OpenAlex.

  1. Balancing cellular copper levels via the post-translational regulation of copper transport.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2026
    Review
  2. Monoallelic ATP7B variants in adult-onset cerebellar ataxia.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2026
    Article
  3. Article
  4. Copper in Gynecological Diseases.International journal of molecular sciences · 2023
    Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Genetics and epigenetic factors of Wilson disease.Annals of translational medicine · 2019
    Review
  12. Copper signalling: causes and consequences.Cell communication and signaling : CCS · 2018
    Review
  13. Review
  14. Review
  15. Review
  16. Drug Interactions With the CaFrontiers in molecular biosciences · 2018
    Review
  17. 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
  18. Article
  19. Copper Resistance inFrontiers in microbiology · 2017
    Article
  20. 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

3 authors at 2 institutions in 2 countries.

Giuseppe Inesi*California Pacific Medical Center Research Institute, San Francisco, CA 94920, U.S.A.
Rajendra Pilankatta†Department of Biochemistry and Molecular Biology, Central University of Kerala, Padennakkad (P.O), Nileshwar, Kasaragod-671 314, Kerala, India.
Francesco Tadini-Buoninsegni‡Department of Chemistry "Ugo Schiff", University of Florence, 50019 Sesto Fiorentino, Italy.
Central University of Kerala · INUniversity of Florence · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Copper ATPases, in analogy with other members of the P-ATPase superfamily, contain a catalytic headpiece including an aspartate residue reacting with ATP to form a phosphoenzyme intermediate, and transmembrane helices containing cation-binding sites [TMBS (transmembrane metal-binding sites)] for catalytic activation and cation translocation. Following phosphoenzyme formation by utilization of ATP, bound copper undergoes displacement from the TMBS to the lumenal membrane surface, with no H+ exchange. Although PII-type ATPases sustain active transport of alkali/alkali-earth ions (i.e. Na+, Ca2+) against electrochemical gradients across defined membranes, PIB-type ATPases transfer transition metal ions (i.e. Cu+) from delivery to acceptor proteins and, prominently in mammalian cells, undergo trafficking from/to various membrane compartments. A specific component of copper ATPases is the NMBD (N-terminal metal-binding domain), containing up to six copper-binding sites in mammalian (ATP7A and ATP7B) enzymes. Copper occupancy of NMBD sites and interaction with the ATPase headpiece are required for catalytic activation. Furthermore, in the presence of copper, the NMBD allows interaction with protein kinase D, yielding phosphorylation of serine residues, ATP7B trafficking and protection from proteasome degradation. A specific feature of ATP7A is glycosylation and stabilization on plasma membranes. Cisplatin, a platinum-containing anti-cancer drug, binds to copper sites of ATP7A and ATP7B, and undergoes vectorial displacement in analogy with copper.

Indexed as

Adenosine TriphosphatasesAnimalsBiocatalysisCation Transport ProteinsCopperHumansProtein Structure, TertiaryAdenosine TriphosphatasesCation Transport ProteinsCopper

Identifiers

PMID25242165
PMCPMC4179477
OpenAlexW2136524945

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.