threonine

More evidence is needed to rate the effectiveness of threonine for these uses.

But more evidence is needed to determine if threonine was actually at fault.

Threonine is changed in the body to a chemical called glycine.

Patients with a different amino acid, threonine, at position 164, had a much better outcome.

There is also some evidence that threonine might actually worsen lung function in these patients.

Threonine is an amino acid found in certain meats, nuts, and seeds.

Taking 6 grams of threonine daily seems to modestly decrease muscle contractions.

Threonine seems to be safe when doses of 2 grams to 4 grams daily are taken for up to 12 months.

Threonine (because its chemical structure is related to that of a sugar called threose), 12.

Serine and threonine, often earthly contaminants, were absent from the samples.

Phosphorylation on serine is the most common, followed by threonine.

It is inhibited by enzyme inhibitors that covalently bind the threonine.

Editing at this site would result in an amino acid change from a Threonine to an Alanine.

Enzymes involved in a typical biosynthesis of threonine include:

Serine and threonine are amino acids of similar composition.

The seeds are sufficiently nutritious, although they do lack some essential nutrients, notably lysine and threonine.

The structural feature that governs this autoinhibition is the Threonine 286 residue.

Threonine is an amino acid.

Neither a threonine, nor a serine at position 183 of subunit 1 contact the ligands.

Threonine is one of two amino acids out of the twenty with two chiral centers.

Threonine is metabolized in two ways:

Threonine also gives rise to isoleucine.

Phosphatases from the Cdc25 family dephosphorylate both the threonine and the tyrosine.

The threonine and glutamic-acid proteases were not described until 1995 and 2004, respectively.

Together with threonine, isoleucine is one of two common amino acids that have a chiral side chain.