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Last Updated: 2 months ago

Possible Interaction: Alanine and Threonine

supplement:

Alanine

supplement:

Threonine

Research Papers that Mention the Interaction

The substitutions of these threonines with alanines decreased Pax6 transactivation, whereas substitutions to glutamic acids increased transactivation in mimicry of phosphorylation.
Journal of Biological Chemistry  •  2006  |  View Paper
Replacement of Thr with Ala at amino acid 366 or 367 caused a modest enhancement of K-RTA transactivation activity in a luciferase reporter assay and a cell model for KSHV reactivation.
Journal of Biomedical Science  •  2012  |  View Paper
Substitution of alanine for threonine at this position reduced early viral propagation, an effect apparently unrelated to NS1 antagonizing host interferon responses or activating phosphoinositide 3-kinase signaling.
Virology  •  2009  |  View Paper
Mutation of any one of these Ser or Thr residues to Ala caused reductions in the receptor phosphorylation state, the number and pattern of phosphopeptides observed in tryptic maps, and ANP-dependent guanylyl cyclase activity.
Molecular and Cellular Biology  •  1998  |  View Paper
The replacement of threonine 334 with alanine resulted in a marked augmentation of catalytic activity.
Blood  •  1996  |  View Paper
Mutation of either threonine or tryptophan to alanine resulted in a lowering of the activity of the R*basal similar to the Rg.
Molecular Pharmacology  •  2009  |  View Paper
Each substitution of threonine to alanine changes the energy barrier of the closing process by approximately 0.5 kcal/mol.
Molecular pharmacology  •  1998  |  View Paper
Substitution of the respective threonine by alanine in the rod photoreceptor and olfactory channels decreases the cGMP sensitivity of channel activation 30-fold but little affects activation by cAMP.
Proceedings of the National Academy of Sciences of the United States of America  •  1991  |  View Paper
Substitution of alanine with the hydrophilic residue threonine at position 117 likely disrupts this hydrophobic channel and may decrease the availability of the catalytic site to substrates, thereby diminishing the catalytic efficiency of C57BL/6-derived catalase.
Nucleic acids research  •  1990  |  View Paper
Furthermore L-alanine inhibits enzymic activities towards serine and threonine to different extent.
The International journal of biochemistry  •  1980  |  View Paper
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