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Source: The Open Library

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1Lysosomal cysteine proteases

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Book's cover

“Lysosomal cysteine proteases” Metadata:

  • Title: Lysosomal cysteine proteases
  • Authors:
  • Language: English
  • Number of Pages: Median: 138
  • Publisher: ➤  Oxford University Press, USA - Oxford University Press
  • Publish Date:
  • Publish Location: New York - Oxford

“Lysosomal cysteine proteases” Subjects and Themes:

Edition Identifiers:

Access and General Info:

  • First Year Published: 1997
  • Is Full Text Available: Yes
  • Is The Book Public: No
  • Access Status: Borrowable

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2Design of caspase inhibitors as potential clinical agents

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Book's cover

“Design of caspase inhibitors as potential clinical agents” Metadata:

  • Title: ➤  Design of caspase inhibitors as potential clinical agents
  • Authors:
  • Language: English
  • Number of Pages: Median: 312
  • Publisher: ➤  Taylor & Francis - CRC Press - Taylor & Francis Group - CRC
  • Publish Date:
  • Publish Location: Boca Raton

“Design of caspase inhibitors as potential clinical agents” Subjects and Themes:

Edition Identifiers:

Access and General Info:

  • First Year Published: 2008
  • Is Full Text Available: No
  • Is The Book Public: No
  • Access Status: No_ebook

Online Access

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    3Ubiquitin-proteasome protocols

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    Book's cover

    “Ubiquitin-proteasome protocols” Metadata:

    • Title: Ubiquitin-proteasome protocols
    • Author:
    • Language: English
    • Number of Pages: Median: 381
    • Publisher: Humana Press
    • Publish Date:
    • Publish Location: Totowa, NJ - Totowa, N.J

    “Ubiquitin-proteasome protocols” Subjects and Themes:

    Edition Identifiers:

    Access and General Info:

    • First Year Published: 2004
    • Is Full Text Available: No
    • Is The Book Public: No
    • Access Status: Unclassified

    Online Access

    Downloads Are Not Available:

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      4Proteolytic enzymes

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      Book's cover

      “Proteolytic enzymes” Metadata:

      • Title: Proteolytic enzymes
      • Author:
      • Language: English
      • Number of Pages: Median: 765
      • Publisher: ➤  Academic Press - Elsevier Science & Technology Books
      • Publish Date:

      “Proteolytic enzymes” Subjects and Themes:

      Edition Identifiers:

      Access and General Info:

      • First Year Published: 1994
      • Is Full Text Available: Yes
      • Is The Book Public: No
      • Access Status: Printdisabled

      Online Access

      Downloads Are Not Available:

      The book is not public therefore the download links will not allow the download of the entire book, however, borrowing the book online is available.

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        5Development of synthetic peptide substrates for the poliovirus 3C proteinase

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        “Development of synthetic peptide substrates for the poliovirus 3C proteinase” Metadata:

        • Title: ➤  Development of synthetic peptide substrates for the poliovirus 3C proteinase
        • Author:
        • Language: English
        • Number of Pages: Median: 130
        • Publisher: Gainesville, FL
        • Publish Date:

        “Development of synthetic peptide substrates for the poliovirus 3C proteinase” Subjects and Themes:

        Edition Identifiers:

        Access and General Info:

        • First Year Published: 1989
        • Is Full Text Available: Yes
        • Is The Book Public: Yes
        • Access Status: Public

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          Wiki

          Source: Wikipedia

          Wikipedia Results

          Search Results from Wikipedia

          Cysteine

          Cysteine (/ˈsɪstɪiːn/; symbol Cys or C) is a semiessential proteinogenic amino acid with the formula HS−CH2−CH(NH2)−COOH. The thiol side chain in cysteine

          Cysteine protease

          peptidases and their inhibitors: Cysteine Peptidases Archived 2017-04-04 at the Wayback Machine Cysteine+endopeptidases at the U.S. National Library of

          Ficain

          related cysteine endopeptidases produced from any species of the genus Ficus, before the terminology was restricted to a specific cysteine endopeptidase enzyme

          Asparagine endopeptidase

          thiol group of a cysteine residue as a nucleophile (hence also called cysteine protease). It is also known as asparaginyl endopeptidase, citvac, proteinase

          Coeliac disease

          ingestion of a combination of enzymes (prolyl endopeptidase and a barley glutamine-specific cysteine endopeptidase (EP-B2)) that degrade the putative 33-mer

          Papain

          of activities, including endopeptidases, aminopeptidases, dipeptidyl peptidases and enzymes with both exo- and endopeptidase activity. Members of the

          Actinidain

          bonds, also known as a peptidase (3.4). The .22 represents the cysteine endopeptidases and then the .14 is actinidain’s unique identifier within that

          Papain-like protease

          Papain-like proteases (or papain-like (cysteine) peptidases; abbreviated PLP or PLCP) are a large protein family of cysteine protease enzymes that share structural

          Matrix metalloproteinase

          are metalloproteinases that are calcium-dependent zinc-containing endopeptidases; other family members are adamalysins, serralysins, and astacins. The

          Metalloproteinase

          metalloproteinases: Exopeptidases, metalloexopeptidases (EC number: 3.4.17). Endopeptidases, metalloendopeptidases (3.4.24). Well known metalloendopeptidases include