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Possible Interaction: Glycine and Glutamic Acid




Glutamic Acid

Research Papers that Mention the Interaction

Substitution of the glycine at position 468 with an alanine or glutamic acid severely compromises protein activity and stability.
DNA repair  •  2006  |  View Paper
The glutamine-to-glutamic acid ratio and glycine were inversely correlated (i.e., LH > MHO > MUO) with HbA1c values.
Journal of proteome research  •  2014  |  View Paper
In contrast, substitution of Gly with Glu or β-Ala resulted in only a partial loss of stimulatory activity.
Journal of Pharmacology and Experimental Therapeutics  •  2003  |  View Paper
At 0.4m-carbodi-imide reagent all of the binding of Ca(2+) to protein was abolished and it was estimated that about 37% of the side-chain carboxyl groups of aspartic acid plus glutamic acid had been blocked by glycine.
The Biochemical journal  •  1971  |  View Paper
The responses to Glu , NMDA, and Asp were each potentiated when 1 microM glycine was coapplied.
Journal of neurophysiology  •  1992  |  View Paper
Microinjection of Gly 1 -2 min before microinjection of Glu in 7 sites reduced significantly (P less than 0.05) the decrease in HR elicited by Glu from 87.0 +/- 27.3 bpm to 17.7 +/- 7.2 bpm.
Brain Research  •  1991  |  View Paper
The addition of a combination of glycine and glutamic acid , urea, or a mixture of NEAA significantly improved growth, but diammonium citrate or other NEAA added singly did not give a significant response.
Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine  •  1967  |  View Paper
Their normal function requires a simultaneous involvement of glutamic acid (as an agonist) and glycine (as a coagonist).
Doklady Biochemistry and Biophysics  •  2004  |  View Paper
Substitution of glycine with glutamic acid at position 48 of the human immunodeficiency virus protease resulted in an enzyme with reduced activity on one of the protease processing sites in the viral Pol polyprotein precursor.
Virology  •  1995  |  View Paper
In addition it has been shown that site specific mutagenesis resulting in the substitution of Gly with Glu leads to a loss of viral infectivity.
Biochemical and biophysical research communications  •  1994  |  View Paper
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