Evidence map›Paper›PMID 20080717›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Homocystamides promote free-radical and oxidative damage to proteins.

Martha Sibrian-Vazquez, Jorge O Escobedo, Soojin Lim, George K Samoei, Robert M Strongin

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
7.4field-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

54 citing papers in PubMed, 147 citations in OpenAlex.

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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.

Martha Sibrian-VazquezDepartment of Chemistry, Portland State University, Portland, OR 97201, USA.
Jorge O Escobedo
Soojin Lim
George K Samoei
Robert M Strongin
California Institute of Technology · USPortland State University · US

Funding

Synthesis and Study of Novel Sensing AgentsR01EB002044 · NIBIB · PORTLAND STATE UNIVERSITY · PI STRONGIN, ROBERT M · 2003 to 2010
$1.6M
NIBIB NIH HHS R01 EB00204NIBIB NIH HHS R01 EB002044
6 · The paper itself

Abstract

Elevated levels of homocysteine are associated with several major diseases. However, it is not clear whether homocysteine is a marker or a causative agent. The majority (ca. 80%) of the homocysteine present in humans is protein bound. The study of the posttranslational modification of proteins by homocysteine and its cyclic congener, homocysteine thiolactone, is emerging as an area of great current interest for unraveling the ongoing "mediator/marker controversy" [Jacobsen DW (2009) Clin Chem 55:1-2]. Interestingly, many of the pathologies associated with homocysteine are also linked to oxidative stress. In the current study, chemical evidence for a causal relationship between homocysteine-bound proteins and oxidative damage is presented. For example, a reproducible increase in protein carbonyl functionality occurs as a consequence of the reaction of human serum albumin with homocysteine thiolactone. This occurs at physiological temperature upon exposure to air without any added oxidants or free-radical initiators. Alpha-amino acid carbon-centered radicals, well-known precursors of protein carbonyls, are shown to form via a hydrogen atom transfer process involving thiolactone-derived homocystamides. Model peptides in buffer as well as native proteins in human blood plasma additionally exhibit properties in keeping with the homocystamide-facilitated hydrogen atom transfer and resultant carbon-centered radicals.

Indexed as

Alzheimer DiseaseCardiovascular DiseasesCongenital AbnormalitiesFree RadicalsHomocysteineHumansHydrogen BondingKineticsLysineOsteoporosisOxidative StressProtein Processing, Post-TranslationalRenal InsufficiencySerum AlbuminFree RadicalsHomocysteineLysineSerum Albumin

Identifiers

PMID20080717
PMCPMC2818928
OpenAlexW2063037352

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.