ArticleBioscience reports2016
The influence of glycation on a high pressure denaturation of ubiquitin.
Article in Bioscience reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed, 4 citations in OpenAlex.
- Attempting to synthesize lasso peptides using high pressure.PloS one · 2020Article
- Maillard Proteomics: Opening New Pages.International journal of molecular sciences · 2017Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The combination of deuterium-hydrogen exchange (DHX) and mass spectrometry (MS) can be used for studying a high pressure denaturation (HPD) of proteins. Herein we present the results of investigations of the influence of glycation on the HPD of ubiquitin. Application of various values of pressure causes different degrees of protein unfolding, resulting in molecules with a different number of protons available for exchange with deuterons. The dependence of this number on pressure gives information on the denaturation state of a protein. On the basis of the obtained results we can conclude that increasing number of fructosamine moieties in ubiquitin decreases the pressure required for its denaturation. It suggests that glycation moderately decreases the protein stability. The present study is the first example of application of hydrogen-deuterium exchange as a method of investigating the influence of posttranslational modification of protein on the HPD.
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