New evidence for the diversity of mechanisms and protonated Schiff bases formed in the non-enzymatic covalent protein modification (NECPM) of HbA by the hydrate and aldehydic forms of acetaldehyde and glyceraldehyde-Reference-Cited by-同舟云学术

New evidence for the diversity of mechanisms and protonated Schiff bases formed in the non-enzymatic covalent protein modification (NECPM) of HbA by the hydrate and aldehydic forms of acetaldehyde and glyceraldehyde

Published:2019-01-01 Issue:1 Volume:5 Page:1584955
ISSN:2331-2025
Container-title:Cogent Biology
language:en
Short-container-title:Cogent Biology

Author:

Lewis Justin¹,Smith Brandy A.¹²,Oakes Heaton²,Holman R.W.¹,Rodnick Kenneth J.²

Affiliation:

1. Department of Chemistry, Idaho State University, Pocatello, ID 83209, USA

2. Department of Biological Sciences, Idaho State University, Pocatello, ID 83209, USA

Funder

National Institute of General Medical Sciences

Publisher

Informa UK Limited

Subject

General Earth and Planetary Sciences,General Environmental Science

Link

https://www.cogentoa.com/article/10.1080/23312025.2019.1584955.pdf

Reference23 articles.

1. PREDICTING AND CHARACTERIZING METAL-BINDING SITES USING SUPPORT VECTOR MACHINES

2. Biochemistry and molecular cell biology of diabetic complications

3. The initial noncovalent binding of glucose to human hemoglobin in nonenzymatic glycation

4. A new CE-ESI-MS method for the detection of stable hemoglobin acetaldehyde adducts, potential biomarkers of alcohol abuse

5. Improved Methods for the Measurement of Acetaldehyde Concentrations in Plasma and Red Blood Cells

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