Examples of 'cathepsin' in a sentence
Meaning of "cathepsin"
cathepsin: a type of enzyme found in cells that is involved in cellular processes and functions
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- Any of a family of proteases primarily active within lysosomes.
How to use "cathepsin" in a sentence
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cathepsin
The cathepsin cleavage sequences are shown in underline.
The dipeptide then is a recognition site for cathepsin.
The cathepsin gene expression may be age related.
A peptide linker may be cleavable by a cathepsin.
The molecular mechanisms of cathepsin activity are not completely understood.
The first piece was immediately processed for cathepsin activities.
Cathepsin d is an aspartyl endopeptidase involved in many pathological processes when overexpressed.
Compounds and compositions as cathepsin s inhibitors.
For these reasons cathepsin d is considered an important target for chemotherapeutic intervention.
Proline derivatives as cathepsin inhibitors.
The above data leads to methods of making specific inhibitors of a given cathepsin.
Inhibiting the production of cathepsin is a possible novel therapeutic approach to pain.
Another aspect of the present disclosure is directed to inhibiting cathepsin activity.
The molecular mechanism of cathepsin activity has not been fully explained.
Another aspect of the present invention is directed to inhibiting cathepsin activity.
See also
The cathepsin protease is cleared by Blue chromatography.
Cleavage of the peptidic substrate by cathepsin D causes an increase in the fluorescence intensity.
Cathepsin A is an enzyme that is classified both as a cathepsin and a carboxypeptidase.
A few products were also tested in respect of the inhibition of the cathepsin D activity.
Cathepsin D has been suggested to be an independent marker of prognosis in breast cancer.
The epoxysuccinic acid derivative of the invention is also effective as a cathepsin B inhibitor.
Cathepsin B has been proposed as a potentially effective biomarker for a variety of cancers.
Another preferred combination is a compound of the present invention and a cathepsin K inhibitor.
Cathepsin K levels have also been demonstrated to be elevated in chondroclasts of osteoarthritic synovium.
A class of the embodiment is the method wherein the cathepsin activity is cathepsin K activity.
Cathepsin K is believed to play a causative role in diseases of excessive bone or cartilage loss.
This example illustrates that inhibition of cathepsin S altered the immune response to tetanus toxoid.
Cathepsin B is a lysosomal cysteine protease normally involved in proenzyme processing and protein turnover.
Ang II can also directly be generated from angiotensinogen by enzymes like tonin and cathepsin.
Local release of this cathepsin may contribute to the osteolysis in Gaucher disease.
Lysosomes fusión into nascent phagosomes brings proteases including cathepsin and triggers Rhodamine conversion.
A newer highly potent cathepsin K inhibitor named relacatib is presently being studied in experimental animals.
Monocytes contain the intracellular serine proteases elastase and cathepsin G and secrete small amounts of metalloproteinases.
Cathepsin L is a major lysosomal protease and is responsible for bulk turnover of intracellular protein.
The crystal structure of cathepsin K has been resolved.
The cathepsin G recognition site is adjacent to a natural trypsin and chymotrypsin recognition site.
In still another embodiment the polypeptide is cathepsin G.
Effect of pCU vector on cathepsin B and uPAR protein levels in total cell extracts.
Suppression of immune response via inhibition of cathepsin S.
Cathepsin B has also been implicated in the progression of various human tumors including ovarian cancer.
There are a number of cathepsin S inhibitors reported in the literature.
Cathepsin D was not detected in sound gullet cells.
There are some natural Cathepsin inhibitors.
The lysosomal protease cathepsin D increased markedly in brown adipocytes during differentiation in primary cultures.
Simeprevir is not a clinically relevant inhibitor of cathepsin A enzyme activity.
The cathepsin G recognition site is adjacent to naturally occurring trypsin and chymotrypsin recognition sites.
Both results indicate a direct role of cathepsin K in cartilage erosion.
In addition cathepsin G release can result in damage to the cell wall and other tissue.
This represents a block in the degradation of Ii due to inhibition of cathepsin S.
Other cathepsin K inhibitors are in various stages of development.
