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  2. Papain-like protease - Wikipedia

    en.wikipedia.org/wiki/Papain-like_protease

    [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 ...

  3. Cathepsin - Wikipedia

    en.wikipedia.org/wiki/Cathepsin

    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 injury [5] Alzheimer's disease [6] Arthritis [7]

  4. Cathepsin L1 - Wikipedia

    en.wikipedia.org/wiki/Cathepsin_L1

    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 .

  5. Cathepsin L - Wikipedia

    en.wikipedia.org/wiki/Cathepsin_L

    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

  6. Carboxypeptidase - Wikipedia

    en.wikipedia.org/wiki/Carboxypeptidase

    Carboxypeptidase A, from bovine pancreas. A carboxypeptidase (EC number 3.4.16 - 3.4.18) is a protease enzyme that hydrolyzes (cleaves) a peptide bond at the carboxy-terminal (C-terminal) end of a protein or peptide.

  7. Cysteine protease - Wikipedia

    en.wikipedia.org/wiki/Cysteine_protease

    The activity of cysteine proteases is regulated by a few general mechanisms, which includes the production of zymogens, selective expression, pH modification, cellular compartmentalization, and regulation of their enzymatic activity by endogenous inhibitors, which seemingly is the most efficient mechanism associated with the regulation of the ...

  8. Serine protease - Wikipedia

    en.wikipedia.org/wiki/Serine_protease

    This may have different consequences, depending on the normal function of the serine protease. For example, mutations in protein C can lead to protein C deficiency and predisposing to thrombosis . Also, some proteases play a vital role in host cell-virus fusion activation by priming virus's Spike protein to show the protein named "fusion ...

  9. Cathepsin L2 - Wikipedia

    en.wikipedia.org/wiki/Cathepsin_L2

    1515 13039 Ensembl ENSG00000136943 ENSMUSG00000021477 UniProt O60911 P06797 RefSeq (mRNA) NM_001333 NM_001201575 NM_009984 RefSeq (protein) NP_001188504 NP_001324 NP_034114 Location (UCSC) Chr 9: 97.03 – 97.16 Mb Chr 13: 64.51 – 64.52 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Cathepsin L2 (EC 3.4.22.43, also known as cathepsin V or cathepsin U) is a protein encoded in ...