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Last Updated: 2 years ago

Possible Interaction: Alanine and Serine

supplement:

Alanine

supplement:

Serine

Research Papers that Mention the Interaction

Mutating serine 575 to an alanine blocked STIM1 phosphorylation, reduced basal STIM1 mobility, and rendered STIM1 insensitive to E2.
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.
Proceedings of the National Academy of Sciences of the United States of America  •  2001  |  View Paper
Substitution of serine 60 with alanine reduces incorporation of (32)P-orthophosphate substantially.
Gastroenterology  •  2001  |  View Paper
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.
Molecular immunology  •  1997  |  View Paper
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%.
The Journal of Biological Chemistry  •  1996  |  View Paper
Mutation of this serine residue to an alanine prevented chondroitin sulfate chain addition to the core protein.
Neurodegeneration : a journal for neurodegenerative disorders, neuroprotection, and neuroregeneration  •  1996  |  View Paper
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