Evidence map›Paper›PMID 19851794›Full record

ReviewJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2010

Structural organization of human Cu-transporting ATPases: learning from building blocks.

Amanda N Barry, Ujwal Shinde, Svetlana Lutsenko

Abstract readReview
PubMed Publisher
In one paragraph

Review in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
6.9field-weighted citation impact, top 3% 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

48 citing papers in PubMed, 95 citations in OpenAlex.

  1. Review
  2. Review
  3. Dietary copper improves intestinal structural integrity in juvenile grass carp (Animal nutrition (Zhongguo xu mu shou yi xue hui) · 2024
    Article
  4. In vitro reconstitution of transition metal transporters.The Journal of biological chemistry · 2024
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Copper metabolism as a unique vulnerability in cancer.Biochimica et biophysica acta. Molecular cell research · 2021
    Review
  12. The CopA2-Type PFrontiers in microbiology · 2021
    Article
  13. Review
  14. Transmembrane Cu(I) P-type ATPase pumps are electrogenic uniporters.Dalton transactions (Cambridge, England : 2003) · 2020
    Article
  15. The molecular mechanisms of copper metabolism and its roles in human diseases.Pflugers Archiv : European journal of physiology · 2020
    Review
  16. Genetics and epigenetic factors of Wilson disease.Annals of translational medicine · 2019
    Review
  17. Review
  18. Article
  19. Thiol oxidase ability of copper ion is specifically retained upon chelation by aldose reductase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 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 1 institution in 1 country.

Amanda N BarryDepartment of Physiology, Johns Hopkins University, Baltimore, MD 21205, USA.
Ujwal Shinde
Svetlana Lutsenko
Johns Hopkins University · US

Funding

Molecular Mechanisms of ATP-dependent Copper TransportersR01DK071865 · NIDDK · OREGON HEALTH & SCIENCE UNIVERSITY · PI SVETLANA LUTSENKO · 2005 to 2026
$7.9M
Copper Transport Mechanism of Menkes disease protein and Wilson disease proteinF32DK077429 · NIDDK · OREGON HEALTH & SCIENCE UNIVERSITY · PI BARRY, AMANDA · 2008 to 2010
$143k
NIDDK NIH HHS F32DK077429NIDDK NIH HHS R01 DK071865
6 · The paper itself

Abstract

Copper-transporting ATPases (Cu-ATPases) ATP7A and ATP7B play an essential role in human physiological function. Their primary function is to deliver copper to the secretory pathway and export excess copper from the cell for removal or further utilization. Cells employ Cu-ATPases in numerous physiological processes that include the biosynthesis of copper-dependent enzymes, lactation, and response to hypoxia. Biochemical studies of human Cu-ATPases and their orthologs have demonstrated that Cu-ATPases share many common structural and mechanistic characteristics with other members of the P-type ATPase family. Nevertheless, the Cu-ATPases have a unique coordinate environment for their ligands, copper and ATP, and additional domains that are required for sophisticated regulation of their intracellular localization and activity. Here, we review recent progress that has been made in understanding the structure of Cu-ATPases from the analysis of their individual domains and orthologs from microorganisms, and speculate about the implications of these findings for the function and regulation of human copper pumps.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateAmino Acid SequenceAnimalsBiological TransportCation Transport ProteinsCopperCopper-Transporting ATPasesHumansIntracellular SpaceMolecular Sequence DataProtein Structure, TertiaryAdenosine TriphosphatasesAdenosine TriphosphateCation Transport ProteinsCopperCopper-Transporting ATPases

Identifiers

PMID19851794
OpenAlexW1992735902

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.