Examples of 'phosphorylate' in a sentence
Meaning of "phosphorylate"
phosphorylate (verb): Phosphorylate is a biochemical term that describes the process of adding a phosphate group to a molecule, typically a protein, to modify its activity, function, or structure
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- to cause phosphorylation.
- to undergo phosphorylation.
How to use "phosphorylate" in a sentence
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phosphorylate
The tyrosine kinases phosphorylate tyrosine residues.
The kinases can be categorized into families by the substrates they phosphorylate.
These reagents are used to phosphorylate aliphatic alcohols.
Kinases phosphorylate proteins and phosphatases dephosphorylate proteins.
This activates the receptor to phosphorylate itself.
Activated receptors phosphorylate tyrosine residues on the receptors.
Immunoprecipitates of the receptor retain ability to phosphorylate the receptor.
Ribose or a phosphorylate derivative thereof.
The receptors dimerize and then cross phosphorylate one another.
It is preferred not to phosphorylate the original components of the fat globule.
The isoforms differ in their ability to interact with and phosphorylate their target substrates.
Protein kinases phosphorylate integrins and a host of other cellular proteins.
Certain protein kinases specifically phosphorylate particular substrates.
These dimers phosphorylate each other and enhance catalytic activity of the kinase.
Members of the raf family of kinases phosphorylate residues on mek.
See also
Activated ROCKs phosphorylate a number of substrates and play important roles in pivotal cellular functions.
Protein kinases are distinguished by their ability to phosphorylate substrates on discrete sequences.
PTKs can phosphorylate tyrosine residue on a protein.
It was initially identified as an enzyme able to phosphorylate and hence inhibit glycogen synthase.
The MAPKs phosphorylate many substrates including cytosolic proteins and ETS family of transcription factors.
The enzyme did not phosphorylate ribonucleosides.
Remember that ATP was a second messenger that kinases use in order to phosphorylate protein.
Kinase enzymes that specifically phosphorylate tyrosine amino acids are termed tyrosine kinases.
STAT activator phosphorylation requires phosphorylation of JAK to phosphorylate.
Protein kinases constitute enzymes that phosphorylate and thus activate other proteins.
Kinases phosphorylate substrates on serine / threonine or tyrosine amino acids.
Both enzymes have comparable substrate preferences and phosphorylate peptide substrates with similar kinetic constants.
The phosphorylated IKKβ then acts to phosphorylate IκBα to liberate the NF-κB.
Other kinases might therefore phosphorylate the Smads.
Protein kinases phosphorylate proteins on serine / threonine or tyrosine residues.
The kinase MEK is an example of kinases that phosphorylate tyrosine and threonine.
Activated MAP-kinases phosphorylate several transduction targets, including transcription factors.
A third possibility is that these kinases directly phosphorylate components of the Hh pathway.
Some protein kinases phosphorylate many different proteins, others phosphorylate only a single protein.
Another preferred biological activity is the ability to phosphorylate or modulate the phosphorylation of Gli.
These kinases phosphorylate downstream targets in a signal transduction cascade, eventually leading to cell cycle arrest.
The activated Akt protein has the ability to phosphorylate and activate several metabolic targets.
The increased cytosolic calcium binds to calmodulin, activating myosin light-chain kinase which phosphorylate myosin.
However NIK is unable to phosphorylate IkB directly.
CDKs phosphorylate their substrates on serines and threonines, so they are serine-threonine kinases.
PAK inhibitors may function to alter the ability of PAK to phosphorylate its substrates.
STAT is then able to phosphorylate and dimerize with another STAT.
In a feedback mechanism, these activated kinases phosphorylate the receptor.
Activated Wts can then go on to phosphorylate and inactivate the transcriptional coactivator Yorkie Yki.
The second group of kinases, called tyrosine kinases are phosphorylate tyrosine residues.
Specifically, tyrosine kinases phosphorylate proteins on the phenolic moiety of tyrosine residues.
These are evidently, but not the only candidate kinases that phosphorylate tau in vivo.
Deoxyribonucleoside kinases phosphorylate deoxyribonucleosides at the 5 ' position.
They constitute a family of seven mammalian serine-threonine protein kinases that phosphorylate agonist-bound receptor.
By contrast, lipid kinases phosphorylate a variety of lipid substrates.
