Why major nonenzymatic glycation sites of human serum albumin are preferred to other residues? [4]

Medical Hypotheses

Volumn 64, Issue 4, 2005, Pages 881-

  Marashi, Sayed Amir ^a   Safarian, Shahrokh ^a   Moosavi Movahedi, Ali A ^a  

^a UNIVERSITY OF TEHRAN   (Iran)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; GLUCOSE; HUMAN SERUM ALBUMIN; LIGAND; LYSINE;

ALBUMIN BLOOD LEVEL; CIRCULATION; COVALENT BOND; DIABETES MELLITUS; DRUG BINDING SITE; GLUCOSE BLOOD LEVEL; GLYCATION; HYPERGLYCEMIA; LETTER; NUCLEOTIDE BINDING SITE; PREDICTION; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN STRUCTURE; REPRODUCIBILITY; SURFACE PROPERTY;

EID: 13444262215     PISSN: 03069877     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mehy.2004.11.007     Document Type: Letter

References (4)

1. D.C. Carter, and J.X. Ho Structure of serum albumin Adv Protein Chem 45 1994 153 201
2. N. Iberg, and R. Fluckiger Nonenzymatic glycosylation of albumin in vivo. Identification of multiple glycosylated sites J Biol Chem 261 1986 13542 13545
3. L. Willard, A. Ranjan, and H. Zhang VADAR: a web server for quantitative evaluation of protein structure quality Nucleic Acids Res 31 2003 3316 3319 Available from: http://www.pence.ca/ftp/vadar/vadar.html/
4. A. Mohamadi-Nejad, A.A. Moosavi-Movahedi, G.H. Hakimelahi, and N. Sheibani Thermodynamic analysis of human serum albumin interactions with glucose: insights into the diabetic range of glucose concentration Int J Biochem Cell Biol 34 2002 1115 1124