Examples of 'threonine residues' in a sentence
Meaning of "threonine residues"
threonine residues - Threonine residues refer to the particular amino acid threonine in a chain of amino acids within a protein. The term is often used in biochemistry and molecular biology to describe specific components or structures within proteins
How to use "threonine residues" in a sentence
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threonine residues
The RAF protein kinase phosphorylates protein targets on serine or threonine residues.
These repeats contain serine and threonine residues that are phosphorylated in actively transcribing RNA polymerase.
The results obtained demonstrated that Orchestin is phophorylated on serine and threonine residues.
Generally, threonine residues are preferred.
We have not determined whether the Gst Lck is phosphorylated on serine or threonine residues.
There may be e.g. several threonine residues that are glycosylated in a statistical manner.
PKC is a multifunctional protein kinase which phosphorylates serine and threonine residues in many target proteins.
In addition, threonine residues undergo phosphorylation through the action of a threonine kinase.
O-glycans are linked to hydroxyl groups of serine or threonine residues.
However, it is not all serine and threonine residues which are O-glycosylated in a protein.
Constitutive phosphorylation occurs on tyrosine, serine and threonine residues.
The O-linked are attached vía serine or threonine residues and consist of short linear chains.
Said flexible linker preferably comprises glycine, serine and threonine residues.
O-glycans are linked vía serine or threonine residues to the protein.
Surprisingly, the majority of activating phosphorylation appears to take place on serine and threonine residues.
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O-linked glycosylation takes place at serine or threonine residues Tanner et al ., Biochim.
Said flexible linker essentially comprises glycine, serine and threonine residues.
The flexible polypeptide linker essentially comprises glycine, serine and threonine residues.
Dual-specificity protein phosphatases remove phosphate groups from phosphorylated tyrosine and serine / threonine residues.
A serine / threonine protein kinase catalyzes the addition of phosphate onto proteins on serine and threonine residues.
In addition mannose could be O-glycosidic linked to serine or threonine residues.
The TRPM7 kinase moiety phosphorylates serine and threonine residues.
However, this method is limited to polypeptides with N-terminal serine or threonine residues.
In vivo, protein kinase C exhibits a preference for the phosphorylation of serine or threonine residues.
In the case of RAC-PK, the phosphorylating agent advantageously targets serine and threonine residues.
ERK 's are serine / threonine kinases that are activated when phosphorylated on tyrosine and threonine residues.
Biosynthetically, the Lan and meLan residues originate from cysteine, serine and threonine residues.
Interacting with phosphorylated serine, tyrosine, or threonine residues.
O-glycosylation occurs in the side chains of serine and / or threonine residues.
To affect O-linked glycosylation of a polypeptide, one would modify serine and / or threonine residues.
Abstract, Protein kinase A ( PKA ) are enzymes which catalyze the phosphorylation of serine or threonine residues.
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Glycine is synthesized vía serine or threonine by serine hydroxymethyltransferase
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