Evidence map›Paper›PMID 31140034›Full record

ReviewThe protein journal2019

Exploring the Extended Biological Functions of the Human Copper Chaperone of Superoxide Dismutase 1.

Yan Ge, Lu Wang, Duanhua Li, Chen Zhao, Jinjun Li, Tao Liu

Abstract readReview
PubMed Publisher
In one paragraph

Review in The protein journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed, 1 pooled it
0.9field-weighted citation impact, top 28% 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

11 citing papers in PubMed, 1 synthesis or guideline pooled it, 19 citations in OpenAlex.

  1. Pooled it
  2. From hemocuprein to CSRP: the many faces of Cu/Zn superoxide dismutase.Metallomics : integrated biometal science · 2026
    Review
  3. Review
  4. Review
  5. Pathogenic RBiochemistry · 2024
    Article
  6. Review
  7. Article
  8. Biochemical Analysis ofACS infectious diseases · 2022
    Article
  9. Review
  10. Review
  11. 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 1 institution in 1 country.

Yan GeAntibiotics Research and Re-evaluation Key Laboratory of Sichuan Province, Sichuan Industrial Institute of Antibiotics, Chengdu University, No. 168 Huaguan Road, Chenghua District, Chengdu, 610052, China.ORCID 0000-0003-3158-2069
Lu WangAntibiotics Research and Re-evaluation Key Laboratory of Sichuan Province, Sichuan Industrial Institute of Antibiotics, Chengdu University, No. 168 Huaguan Road, Chenghua District, Chengdu, 610052, China. wanglu@cdu.edu.cn.
Duanhua LiAntibiotics Research and Re-evaluation Key Laboratory of Sichuan Province, Sichuan Industrial Institute of Antibiotics, Chengdu University, No. 168 Huaguan Road, Chenghua District, Chengdu, 610052, China.
Chen ZhaoAntibiotics Research and Re-evaluation Key Laboratory of Sichuan Province, Sichuan Industrial Institute of Antibiotics, Chengdu University, No. 168 Huaguan Road, Chenghua District, Chengdu, 610052, China.
Jinjun LiAntibiotics Research and Re-evaluation Key Laboratory of Sichuan Province, Sichuan Industrial Institute of Antibiotics, Chengdu University, No. 168 Huaguan Road, Chenghua District, Chengdu, 610052, China.
Tao LiuAntibiotics Research and Re-evaluation Key Laboratory of Sichuan Province, Sichuan Industrial Institute of Antibiotics, Chengdu University, No. 168 Huaguan Road, Chenghua District, Chengdu, 610052, China.
Chengdu University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human copper chaperone of SOD1 (designated as CCS) was discovered more than two decades ago. It is an important copper binding protein and a homolog of Saccharomyces cerevisiae LYS7. To date, no studies have systematically or specifically elaborated on the functional development of CCS. This review summarizes the essential information about CCS, such as its localization, 3D structure, and copper binding ability. An emphasis is placed on its interacting protein partners and its biological functions in vivo and in vitro. Three-dimensional structural analysis revealed that CCS is composed of three domains. Its primary molecular function is the delivery of copper to SOD1 and activation of SOD1. It has also been reported to bind to XIAP, Mia40, and X11α, and other proteins. Through these protein partners, CCS is implicated in several vital biological processes in vivo, such as copper homeostasis, apoptosis, angiogenesis and oxidative stress. This review is anticipated to assist scientists in systematically understanding the latest research developments of CCS for facilitating the development of new therapeutics targeting CCS in the future.

Indexed as

Adaptor Proteins, Signal TransducingCarcinogenesisCopperCopper Transporter 1Copper Transport ProteinsHumansMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMolecular ChaperonesNerve Tissue ProteinsSuperoxide Dismutase-1X-Linked Inhibitor of Apoptosis ProteinAdaptor Proteins, Signal TransducingAPBA1 protein, humanATOX1 protein, humanCCS protein, humanCHCHD4 protein, humanCopperCopper Transporter 1Copper Transport ProteinsMitochondrial Membrane Transport ProteinsMitochondrial Precursor Protein Import Complex ProteinsMolecular ChaperonesNerve Tissue ProteinsSLC31A1 protein, humanSOD1 protein, humanSuperoxide Dismutase-1XIAP protein, humanX-Linked Inhibitor of Apoptosis ProteinCCSCopperFunctionsSOD1

Identifiers

PMID31140034
OpenAlexW2947638834

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.