Examples of 'tyrosine residues' in a sentence
Meaning of "tyrosine residues"
tyrosine residues: Tyrosine residues are specific amino acid units that can be found in proteins. They play a key role in various biological processes, including signal transduction, enzyme catalysis, and protein structure stabilization
How to use "tyrosine residues" in a sentence
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tyrosine residues
The tyrosine kinases phosphorylate tyrosine residues.
Cytoplasmic tyrosine residues are circled.
Protein phosphorylation is implicated in angiogenesis especially at tyrosine residues.
Activated receptors phosphorylate tyrosine residues on the receptors.
Several proteins were thus shown to be phosphorylated at one or more tyrosine residues.
No tryptophan or tyrosine residues were present.
In specific embodiments these are surface exposed tyrosine residues.
Peptides containing tyrosine residues are used by this strain to produce tyramine.
Tyrosine kinases catalyze the phosphorylation of tyrosine residues in proteins.
Neither does it contain any tyrosine residues which might be involved in phosphorylation.
This process can occur to molecules such as tyrosine residues.
The reaction of nitrous acid with tyrosine residues was examined by spectrophotometry.
Human growth hormone molecules contain eight tyrosine residues.
The phosphorylation of tyrosine residues plays an important role in these two very important processes.
One of the modification reactions known is a sulfated reaction of tyrosine residues.
See also
An atelocollagen having three or less tyrosine residues per molecule is more preferable.
Monitoring the ability of said phosphatase domain to dephosphorylate phosphorylated tyrosine residues.
The binding of signaling proteins to these phosphorylated tyrosine residues leads to further downstream signaling.
Exposure of nitrogen dioxide to tyrosine hydroxylase results in the nitration of its tyrosine residues.
The above enzymes catalyze the phosphorylation of specific tyrosine residues to form tyrosine phosphorylated residues.
Tyrosine residues identified are examined for their predicted proximity and positional flexibility toward each other.
It is just casein that comprises iodinated tyrosine residues in its composition.
Phosphorylation of tyrosine residues was measured by ELISA using an antiphosphotyrosine MAb.
This nitronium intermediate again is able to nitrate protein derived tyrosine residues.
Lysine residues provide recognition sites for trypsin and tyrosine residues provide recognition sites for chymotripsin.
One consequence of this kinase activation is the autophosphorylation of EGFR on tyrosine residues.
The detection of phosphorylation of tyrosine residues by Western blotting was as follows.
Interaction of a neurotrophin ligand with trks induces phosphorylation of specific tyrosine residues on the receptor.
The detection of phosphorylation of tyrosine residues was carried out by Western blotting.
Receptor binding of IGFI results in autophosphorylation of tyrosine residues.
Tyrosine residues were conjugated to PEG chains for attachment of radioiodine or stable iodine moieties.
The protein is found in various tissues and many of its tyrosine residues are sulphated.
The corresponding tyrosine residues in the cytoplasmic domain of human KIT can be readily determined.
Additional peptide immunogens may be generated by replacing tyrosine residues with sulfated tyrosine residues.
The phenylalanine or tyrosine residues which occur at invariant positions are required for DNA binding.
IRSs are activated by insulin receptor tyrosine kinase that phosphorylates tyrosine residues of IRSs.
In the follicular lumen, tyrosine residues become iodinated.
Protein kinases phosphorylate proteins on serine / threonine or tyrosine residues.
Most preferably, both tyrosine residues can be replaced.
In another embodiment, the tyrosine enhancer is a polymer containing tyrosine residues.
Thus, nitrosylation of tyrosine residues is likely to occur in these situations.
The EGFR becomes phosphorylated on tyrosine residues.
Likewise, one or more tyrosine residues can be replaced by phenylalanine residues.
The second group of kinases, called tyrosine kinases are phosphorylate tyrosine residues.
In addition, one or more tyrosine residues can be replaced by phenyalanine residues.
Specifically, tyrosine kinases phosphorylate proteins on the phenolic moiety of tyrosine residues.
Additionally, tyrosine residues are crucial to this mechanism in acting as stabilizing hydrogen acceptors.
In addition, signaling can be terminated by dephosphorylation of the tyrosine residues by tyrosine phosphatases.
Likewise, one or more tyrosine residues can be replaced by phenylalanine residues as well.
Process according to claim 1, wherein the peptide contains one or more tyrosine residues.
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Examples of using Tyrosine
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Tyrosine must be determined in hydrolysates of unoxidised samples
The protein possesses tyrosine kinase activity
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