Evidence map›Paper›PMID 17760510›Full record

ReviewAntioxidants & redox signaling2007

Molecular targeting of proteins by L-homocysteine: mechanistic implications for vascular disease.

Alla V Glushchenko, Donald W Jacobsen

Open access · greenAbstract readReview
In one paragraph

Review in Antioxidants & redox signaling, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.7field-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

32 citing papers in PubMed, 111 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Homocysteinylation of Fibrinogen: A Post-Translational Link to Thrombosis.International journal of molecular sciences · 2025
    Review
  5. Review
  6. Homocysteinylation and Sulfhydration in Diseases.Current neuropharmacology · 2022
    Review
  7. Article
  8. Blood Thiol Redox State in Chronic Kidney Disease.International journal of molecular sciences · 2022
    Review
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Role of homocysteinylation of ACE in endothelial dysfunction of arteries.American journal of physiology. Heart and circulatory physiology · 2015
    Article
  19. Impact of homocysteine-thiolactone on plasma fibrin networks.Journal of thrombosis and thrombolysis · 2014
    Article
  20. Review
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

2 authors at 1 institution in 1 country.

Alla V GlushchenkoDepartment of Cell Biology, Lerner Research Institute, Cleveland Clinic, Case Western Reserve University, Cleveland, Ohio 44195, USA.
Donald W Jacobsen
Case Western Reserve University · US

Funding

Homocysteine: Vascular Biochemistry and MetabolismR37HL052234 · NHLBI · CLEVELAND CLINIC LERNER COM-CWRU · PI JACOBSEN, DONALD WELDON · 2006 to 2010
$1.9M
NHLBI NIH HHS R37 HL052234
6 · The paper itself

Abstract

Hyperhomocysteinemia is an independent risk factor for cardiovascular disease, complications of pregnancy, cognitive impairment, and osteoporosis. That elevated homocysteine leads to vascular dysfunction may be the linking factor between these apparently unrelated pathologies. Although a growing body of evidence suggests that homocysteine plays a causal role in atherogenesis, specific mechanisms to explain the underlying pathogenesis have remained elusive. This review focuses on chemistry unique to the homocysteine molecule to explain its inherent cytotoxicity. Thus, the high pKa of the sulfhydryl group (pKa, 10.0) of homocysteine underlies its ability to form stable disulfide bonds with protein cysteine residues, and in the process, alters or impairs the function of the protein. Studies in this laboratory have identified albumin, fibronectin, transthyretin, and metallothionein as targets for homocysteinylation. In the case of albumin, the mechanism of targeting has been elucidated. Homocysteinylation of the cysteine residues of fibronectin impairs its ability to bind to fibrin. Homocysteinylation of the cysteine residues of metallothionein disrupts zinc binding by the protein and abrogates inherent superoxide dismutase activity. Thus, S-homocysteinylation of protein cysteine residues may explain mechanistically the cytotoxicity of elevated L-homocysteine.

Indexed as

AnimalsBlood ProteinsHomocysteineHumansMembrane ProteinsModels, BiologicalVascular DiseasesBlood ProteinsHomocysteineMembrane Proteins

Identifiers

PMID17760510
PMCPMC2855132
OpenAlexW2046438960

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.