Explore: Cathepsin

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Source: The Open Library

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1Tissue proteinases

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“Tissue proteinases” Metadata:

  • Title: Tissue proteinases
  • Author: ➤  
  • Language: English
  • Number of Pages: Median: 353
  • Publisher: ➤  North-Holland; New York, American Elsevier
  • Publish Date:
  • Publish Location: Amsterdam

“Tissue proteinases” Subjects and Themes:

Edition Identifiers:

Access and General Info:

  • First Year Published: 1971
  • Is Full Text Available: Yes
  • Is The Book Public: No
  • Access Status: Borrowable

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2Tissue proteinases

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“Tissue proteinases” Metadata:

  • Title: Tissue proteinases
  • Author: ➤  
  • Language: English
  • Number of Pages: Median: 353
  • Publisher: ➤  American Elsevier Pub. Co. - American Elsevier Pub. Co - North-Holland Pub. Co.
  • Publish Date:
  • Publish Location: New York - Amsterdam

“Tissue proteinases” Subjects and Themes:

Edition Identifiers:

Access and General Info:

  • First Year Published: 1971
  • Is Full Text Available: No
  • Is The Book Public: No
  • Access Status: No_ebook

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3Changes in cathepsin D Activity and concomitant studies of macromolecular components in the early sea urchin development

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“Changes in cathepsin D Activity and concomitant studies of macromolecular components in the early sea urchin development” Metadata:

  • Title: ➤  Changes in cathepsin D Activity and concomitant studies of macromolecular components in the early sea urchin development
  • Author:
  • Language: English
  • Number of Pages: Median: 377
  • Publisher: Almqvist Wiksell
  • Publish Date:
  • Publish Location: Stockholm

“Changes in cathepsin D Activity and concomitant studies of macromolecular components in the early sea urchin development” Subjects and Themes:

Edition Identifiers:

Access and General Info:

  • First Year Published: 1968
  • Is Full Text Available: No
  • Is The Book Public: No
  • Access Status: No_ebook

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4Partial purification of cathepsins from salmon muscle

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“Partial purification of cathepsins from salmon muscle” Metadata:

  • Title: ➤  Partial purification of cathepsins from salmon muscle
  • Author:
  • Language: English
  • Number of Pages: Median: 50
  • Publish Date:

“Partial purification of cathepsins from salmon muscle” Subjects and Themes:

Edition Identifiers:

Access and General Info:

  • First Year Published: 1965
  • Is Full Text Available: No
  • Is The Book Public: No
  • Access Status: No_ebook

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Wiki

Source: Wikipedia

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Cathepsin

turnover. Cathepsin A (serine protease) Cathepsin B (cysteine protease) Cathepsin C (cysteine protease) Cathepsin D (aspartyl protease) Cathepsin E (aspartyl

Cathepsin E

non-pepsin proteinase, cathepsin D-like acid proteinase, cathepsin E-like acid proteinase, cathepsin D-type proteinase) is an enzyme. Cathepsin E is a protease

Cathepsin L2

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. The protein is a human cysteine

Cathepsin X

Cathepsin X (EC 3.4.18.1, cathepsin B2, cysteine-type carboxypeptidase, cathepsin IV, cathepsin Z, acid carboxypeptidase, lysosomal carboxypeptidase B)

Osteoclast

cathepsin K. Studies on cathepsin L knockout mice have been mixed, with a report of reduced trabecular bone in homozygous and heterozygous cathepsin L

Cathepsin A

Cathepsin A is an enzyme that is classified both as a cathepsin and a carboxypeptidase. In humans, it is encoded by the CTSA gene. The enzyme is also

Cathepsin C

Cathepsin C (CTSC) also known as dipeptidyl peptidase I (DPP-I) is a lysosomal exo-cysteine protease belonging to the peptidase C1 protein family, a subgroup

Cathepsin L1

Cathepsin L1 is a protein that in humans is encoded by the CTSL1 gene. The protein is a cysteine cathepsin, a lysosomal cysteine protease that plays a

Cathepsin D

Cathepsin D is a protein that in humans is encoded by the CTSD gene. This gene encodes a lysosomal aspartyl protease composed of a protein dimer of disulfide-linked

Pycnodysostosis

disease of the bone caused by a mutation in the gene that codes the enzyme cathepsin K. It is also known as PKND and PYCD. The disease was first described