Evidence map›Paper›PMID 17562324›Full record

ReviewArchives of biochemistry and biophysics2007

Biochemical basis of regulation of human copper-transporting ATPases.

Svetlana Lutsenko, Erik S LeShane, Ujwal Shinde

Open access · greenAbstract readReview
In one paragraph

Review in Archives of biochemistry and biophysics, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed, 2 pooled it
8.7field-weighted citation impact, top 2% 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

60 citing papers in PubMed, 2 syntheses or guidelines pooled it, 145 citations in OpenAlex.

  1. Pooled it
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  12. [Genotype-phenotype relationship and genetics study of 115 cases with Wilson's disease].Zhonghua gan zang bing za zhi = Zhonghua ganzangbing zazhi = Chinese journal of hepatology · 2024
    Article
  13. Article
  14. Review
  15. The biology of mammalian multi-copper ferroxidases.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023
    Review
  16. Article
  17. Copper homeostasis and cuproptosis in health and disease.Signal transduction and targeted therapy · 2022
    Review
  18. Review
  19. 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.

Svetlana LutsenkoDepartment of Biochemistry and Molecular Biology, Oregon Health & Science University, Portland, OR 97239, USA. lutsenko@ohsu.edu
Erik S LeShane
Ujwal Shinde
Oregon Health & Science University · US

Funding

Molecular Mechanisms of ATP-dependent Copper TransportersR01DK071865 · NIDDK · OREGON HEALTH & SCIENCE UNIVERSITY · PI SVETLANA LUTSENKO · 2005 to 2026
$7.9M
TRAINING PROGRAM IN MOLECULAR HEMATOLOGYT32HL007781 · NHLBI · OREGON HEALTH & SCIENCE UNIVERSITY · PI BAGBY, GROVER CARLTON · 1993 to 2012
$5.1M
NHLBI NIH HHS 5-T32-HL007781NHLBI NIH HHS T32 HL007781NIDDK NIH HHS R01 DK071865
6 · The paper itself

Abstract

Copper is essential for cell metabolism as a cofactor of key metabolic enzymes. The biosynthetic incorporation of copper into secreted and plasma membrane-bound proteins requires activity of the copper-transporting ATPases (Cu-ATPases) ATP7A and ATP7B. The Cu-ATPases also export excess copper from the cell and thus critically contribute to the homeostatic control of copper. The trafficking of Cu-ATPases from the trans-Golgi network to endocytic vesicles in response to various signals allows for the balance between the biosynthetic and copper exporting functions of these transporters. Although significant progress has been made towards understanding the biochemical characteristics of human Cu-ATPase, the mechanisms that control their function and intracellular localization remain poorly understood. In this review, we summarize current information on structural features and functional properties of ATP7A and ATP7B. We also describe sequence motifs unique for each Cu-ATPase and speculate about their role in regulating ATP7A and ATP7B activity and trafficking.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceCation Transport ProteinsCopperCopper-Transporting ATPasesCopper Transport ProteinsHumansMetallochaperonesMolecular ChaperonesMolecular Sequence DataProtein Structure, TertiaryAdenosine TriphosphatasesATOX1 protein, humanATP7A protein, humanATP7B protein, humanCation Transport ProteinsCopperCopper-Transporting ATPasesCopper Transport ProteinsMetallochaperonesMolecular Chaperones

Identifiers

PMID17562324
PMCPMC2025638
OpenAlexW2058274420

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.