ArticleBiochemical and biophysical research communications2011
Ribose sugars generate internal glycation cross-links in horse heart myoglobin.
Article in Biochemical and biophysical research communications, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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.
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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.
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Who cites it
9 citing papers in PubMed, 31 citations in OpenAlex.
- Anhydrous microwave synthesis as efficient method for obtaining model advanced glycation end-products.Frontiers in molecular biosciences · 2024Article
- Ribose Intake as Food Integrator: Is It a Really Convenient Practice?Biomolecules · 2022Review
- Identification of the Protein Glycation Sites in Human Myoglobin as Rapidly Induced by d-Ribose.Molecules (Basel, Switzerland) · 2021Article
- D-ribose and pathogenesis of Alzheimer's disease.Molecular biology reports · 2020Review
- Formation of Pentosidine Cross-Linking in Myoglobin by Glyoxal: Detection of Fluorescent Advanced Glycation End Product.Journal of fluorescence · 2017Article
- Article
- Structural and functional alterations of myoglobin by glucose-protein interactions.Journal of molecular modeling · 2014Article
- In vitro study on structural alteration of myoglobin by methylglyoxal.The protein journal · 2013Article
- Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Glycation of horse heart metmyoglobin with d-ribose 5-phosphate (R5P), d-2-deoxyribose 5-phosphate (dR5P), and d-ribose with inorganic phosphate at 37°C generates an altered protein (Myo-X) with increased SDS-PAGE mobility. The novel protein product has been observed only for reactions with the protein myoglobin and it is not evident with other common sugars reacted over a 1 week period. Myo-X is first observed at 1-2 days at 37°C along with a second form that is consistent in mass with that of myoglobin attached to several sugars. MALDI mass spectrometry and other techniques show no evidence of the cleavage of a peptide from the myoglobin chain. Apomyoglobin in reaction with R5P also exhibited this protein form suggesting its occurrence was not heme-related. While significant amounts of O(2)(-) and H(2)O(2) are generated during the R5P glycation reaction, they do not appear to play roles in the formation of the new form. The modification is likely due to an internal cross-link formed during a glycation reaction involving the N-terminus and an internal amine group; most likely the neighboring Lys133. The study shows the unique nature of these common pentose sugars in spontaneous glycation reactions with proteins.
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Registered trials
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.