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The Journal of Biological Chemistry • 2013 | View Paper
“Significance A common variant of histidine-rich Ca-binding protein (HRC), where an alanine replaces a serine at amino acid 96, can increase the risk of dying from severe heart disease.”
Proceedings of the National Academy of Sciences • 2017 | View Paper
“Mutation of Ser to Ala reduced the strength of interaction with the chemical transition state specifically, as shown by vanadate-ADP and beryllium fluoride-ADP trapping experiments.”
Journal of Biological Chemistry • 2004 | View Paper
“Mutation of serine to other amino acids with varying side chains: alanine , methionine, leucine, aspartic acid, asparagine, and arginine also resulted in significant activation, indicating a serine-specific inhibitory effect.”
“Substitution of the serines by alanine impeded the access of MAL to GEMs and changed its distribution from a perinuclear distribution to an ER pattern.”
Biochemical and biophysical research communications • 1999 | View Paper
“Substitution of one Ala by Ser in the N-terminal flank had pronounced effect and peptide A2SA-75-81-A4 proved to be more effective than the native 20-mer sequence in the hybridoma as well as in the LN cell proliferation assays.”
“Simultaneous mutation of these four serines to alanines decreases the rate of agonist-induced uncoupling and the rate of agonist-induced internalization.”
Biochemical Society transactions • 1997 | View Paper
“Mutational analysis of three serine residues upstream of the di-leucine motif revealed that mutation of serine 139 to an alanine reduces the initial internalization rate by 50%.”