Evidence map›Paper›PMID 19240214›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2009

Three-dimensional structure of the human copper transporter hCTR1.

Christopher J De Feo, Stephen G Aller, Gnana S Siluvai, Ninian J Blackburn, Vinzenz M Unger

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 126 papers.

0numbers the graph read from it
0cells of the map it votes in
126citing papers in PubMed
20.5field-weighted citation impact, top 1% 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

126 citing papers in PubMed, 274 citations in OpenAlex.

  1. Review
  2. 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
  3. Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. The Role of Copper Overload in Modulating Neuropsychiatric Symptoms.International journal of molecular sciences · 2024
    Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. Study on Computer Screening and Drug Properties of Herbs Intervening in Copper Death.Computational and mathematical methods in medicine · 2023
    Article
  19. Article
  20. Article

66 more citing papers are in PubMed but not listed here.

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

5 authors at 2 institutions in 1 country.

Christopher J De FeoDepartment of Molecular Biophysics and Biochemistry, Yale University School of Medicine, 333 Cedar Street New Haven, CT 06510, USA.
Stephen G Aller
Gnana S Siluvai
Ninian J Blackburn
Vinzenz M Unger
Yale University · USOregon Health & Science University · US

Funding

Skill Development for Diverse Scientific Careers: A New Course Predoctoral Program in Cellular and Molecular BiologyT32GM007223 · NIGMS · YALE UNIVERSITY · PI BASERGA, SUSAN J · 1985 to 2019
$31.0M
The role of transferrin receptor 2 in iron homeostasisP01GM067166 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI LUTSENKO, SVETLANA · 2003 to 2013
$14.6M
Structure and Function of Copper TransportersR01GM071590 · NIGMS · YALE UNIVERSITY · PI UNGER, VINZENZ · 2005 to 2009
$1.3M
Structure-Function of the Human Copper Transporter hCTR1F31NS045550 · NINDS · YALE UNIVERSITY · PI ALLER, STEPHEN G · 2003 to 2005
$118k
Structure and Function of the Human Copper TransporterF31NS056825 · NINDS · YALE UNIVERSITY · PI DEFEO, CHRISTOPHER J · 2006 to 2007
$58k
NIGMS NIH HHS GM071590NIGMS NIH HHS P01 GM067166NIGMS NIH HHS R01 GM071590NIGMS NIH HHS T32 GM007223NIGMS NIH HHS T32 GM07223NINDS NIH HHS F31 NS045550NINDS NIH HHS F31 NS056825NINDS NIH HHS F31 NS56825
6 · The paper itself

Abstract

Copper uptake proteins (CTRs), mediate cellular acquisition of the essential metal copper in all eukaryotes. Here, we report the structure of the human CTR1 protein solved by electron crystallography to an in plane resolution of 7 A. Reminiscent of the design of traditional ion channels, trimeric hCTR1 creates a pore that stretches across the membrane bilayer at the interface between the subunits. Assignment of the helices identifies the second transmembrane helix as the key element lining the pore, and reveals how functionally important residues on this helix could participate in Cu(I)-coordination during transport. Aligned with and sealing both ends of the pore, extracellular and intracellular domains of hCTR1 appear to provide additional metal binding sites. Consistent with the existence of distinct metal binding sites, we demonstrate that hCTR1 stably binds 2 Cu(I)-ions through 3-coordinate Cu-S bonds, and that mutations in one of these putative binding sites results in a change of coordination chemistry.

Indexed as

Binding SitesCation Transport ProteinsCopperCopper Transporter 1Cryoelectron MicroscopyCrystallizationHumansMutationProtein ConformationCation Transport ProteinsCopperCopper Transporter 1SLC31A1 protein, human

Identifiers

PMID19240214
PMCPMC2647337
OpenAlexW2156644611

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.