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The cysteine cathepsins have attracted significant research effort as drug targets. [1] [2] Cancer, Cathepsin D is a mitogen and "it attenuates the anti-tumor immune response of decaying chemokines to inhibit the function of dendritic cells". Cathepsins B and L are involved in matrix degradation and cell invasion. [3] Stroke [4] Traumatic brain ...
Cathepsin L1 is a protein that in humans is encoded by the CTSL1 gene. [ 3 ] [ 4 ] [ 5 ] The protein is a cysteine cathepsin , a lysosomal cysteine protease that plays a major role in intracellular protein catabolism .
[3] [10] [9] Many papain-like protease enzymes function as monomers, though a few, such as cathepsin C (Dipeptidyl-peptidase I), are homotetramers. The mature monomer structure is characteristically divided into two lobes or subdomains, known as the L-domain ( N-terminal ) and the R-domain ( C-terminal ), where the active site is located ...
Cathepsin L may refer to: Cathepsin L1 , a human protease enzyme encoded by the CTSL gene and known for its role in viral entry Cathepsin L2 , a human protease enzyme encoded by the CTSV gene and also known as cathepsin V
Cathepsin L2 (EC 3.4.22.43, also known as cathepsin V or cathepsin U) is a protein encoded in humans by the CTSV gene. [5] [6] [7] [8]The protein is a human cysteine cathepsin, a lysosomal cysteine protease with endopeptidase activity.
Animal Production Science is an international peer-reviewed scientific journal for agriculture and animal science and published by CSIRO Publishing.Research articles in the journal focus on improving livestock and food production, and on the social and economic issues that influence primary producers.
Serine proteases are inhibited by a diverse group of inhibitors, including synthetic chemical inhibitors for research or therapeutic purposes, and also natural proteinaceous inhibitors. One family of natural inhibitors called "serpins" (abbreviated from serine protease inhibitors ) can form a covalent bond with the serine protease, inhibiting ...
The very long (251-amino acid residues) proregion of the cathepsin F precursor contains a C-terminal domain similar to the pro-segment of Cathepsin L-like enzymes, a 50-residue flexible linker peptide, and an N-terminal domain predicted to adopt a cystatin-like fold. The cathepsin F proregion is unique within the papain family cysteine ...