ArticleThe protein journal2011
Effect of homocysteine thiolactone on structure and aggregation propensity of bovine pancreatic insulin.
Article in The protein journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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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Who cites it
8 citing papers in PubMed, 28 citations in OpenAlex.
- Characterization of S-homocysteinylation of Human Insulin and Its Implications in Diabetes.The protein journal · 2025Article
- N-Homocysteinylation of lysine residues in α-Synuclein enhances aggregation propensity and cytotoxicity in SH-SY5Y cells.Scientific reports · 2025Article
- The modification of nisin with homocysteine thiolactone and its effect on antimicrobial activity.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2024Article
- Functionally active cross-linked protein oligomers formed by homocysteine thiolactone.Scientific reports · 2023Article
- The relationship between insulin resistance, adiponectin and C-reactive protein and vascular endothelial injury in diabetic patients with coronary heart disease.Experimental and therapeutic medicine · 2018Article
- Characterization of N-homocysteinylated albumin adducts.The protein journal · 2014Article
- N-homocysteinylation induces different structural and functional consequences on acidic and basic proteins.PloS one · 2014Article
- Existence of molten globule state in homocysteine-induced protein covalent modifications.PloS one · 2014Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Homocysteine thiolactone (HCTL) is a cyclic thioester of homocysteine, showing high reactivity toward lysine residues of proteins. In the present study the structural properties and aggregation propensity of bovine pancreatic insulin were studied in the presences of increasing concentration of HCTL (0-500 μM), using different spectroscopic techniques. As shown in this study, HCTL induces gross structural alterations and subsequently aggregation of insulin in a dose dependent manner. Also induction of insulin aggregation by HCTL occurs in a sequential process, where native protein with alpha-helical abundant structure gradually transforms into partially folded conformations with the significant amount of beta-sheet. Since C-terminal B-chain of insulin plays a critical role in stability of this protein, the structural alteration/aggregation induced by HCTL can be consequence of homocysteinylation of the only Lysine residue (Lys29) on its B-chain. This study may have important implications regarding the effect of HCTL on structure of insulin particularly in the pathological states linked to hyperhomocysteinemia.
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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.