Explore: Cysteine Endopeptidases
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AI-Generated Overview About “cysteine-endopeptidases”:
Books Results
Source: The Open Library
The Open Library Search Results
Search results from The Open Library
1Lysosomal cysteine proteases
By Heidrun Kirschke, Alan J. Barrett and Neil D. Rawlings

“Lysosomal cysteine proteases” Metadata:
- Title: Lysosomal cysteine proteases
- Authors: Heidrun KirschkeAlan J. BarrettNeil D. Rawlings
- Language: English
- Number of Pages: Median: 138
- Publisher: ➤ Oxford University Press, USA - Oxford University Press
- Publish Date: 1997 - 1998
- Publish Location: New York - Oxford
“Lysosomal cysteine proteases” Subjects and Themes:
- Subjects: ➤ Cysteine proteinases - Lysosomes - Cysteine Proteases - Cysteine Endopeptidases - Lysosom - Cysteine proteinase - Enzimas - Cysteinproteasen
Edition Identifiers:
- The Open Library ID: OL7399942M - OL699375M
- Online Computer Library Center (OCLC) ID: 504052109
- Library of Congress Control Number (LCCN): 97047140
- All ISBNs: 0198502494 - 9780198502494
Access and General Info:
- First Year Published: 1997
- Is Full Text Available: Yes
- Is The Book Public: No
- Access Status: Borrowable
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.
Online Borrowing:
- Borrowing from Open Library: Borrowing link
- Borrowing from Archive.org: Borrowing link
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2Design of caspase inhibitors as potential clinical agents
By Tom O'Brien and Steven D. Linton

“Design of caspase inhibitors as potential clinical agents” Metadata:
- Title: ➤ Design of caspase inhibitors as potential clinical agents
- Authors: Tom O'BrienSteven D. Linton
- Language: English
- Number of Pages: Median: 312
- Publisher: ➤ Taylor & Francis - CRC Press - Taylor & Francis Group - CRC
- Publish Date: 2008 - 2009 - 2019
- Publish Location: Boca Raton
“Design of caspase inhibitors as potential clinical agents” Subjects and Themes:
- Subjects: ➤ Cysteine proteinases - Caspases - Apoptosis - Therapeutic use - Physiology - Antagonists & inhibitors - Inhibitors - Chemistry - General - Science / Chemistry / General - Life Sciences - Biochemistry - Life Sciences - Cytology - Science - Science/Mathematics - Enzyme inhibitors - Caspase Inhibitors - Cysteine Endopeptidases - Cysteine Proteinase Inhibitors - Peptidases à cystéine - Inhibiteurs - Apoptose
Edition Identifiers:
- The Open Library ID: ➤ OL34595214M - OL33680446M - OL33667768M - OL33442914M - OL11816474M - OL19889543M
- Online Computer Library Center (OCLC) ID: 282762315
- Library of Congress Control Number (LCCN): 2008025506
- All ISBNs: ➤ 1420045415 - 9781420045406 - 9780367386573 - 0367386577 - 1420045407 - 9780429149474 - 1281863157 - 9781420045413 - 9781281863157 - 0429149476
Access and General Info:
- First Year Published: 2008
- Is Full Text Available: No
- Is The Book Public: No
- Access Status: No_ebook
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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3Ubiquitin-proteasome protocols
By Cam Patterson

“Ubiquitin-proteasome protocols” Metadata:
- Title: Ubiquitin-proteasome protocols
- Author: Cam Patterson
- Language: English
- Number of Pages: Median: 381
- Publisher: Humana Press
- Publish Date: 2004 - 2005 - 2010
- Publish Location: Totowa, NJ - Totowa, N.J
“Ubiquitin-proteasome protocols” Subjects and Themes:
- Subjects: ➤ Proteolytic enzymes - Laboratory manuals - Ubiquitin - Life Sciences - Biochemistry - SCIENCE - Cysteine Endopeptidases - Multienzyme Complexes - Metabolism
Edition Identifiers:
- The Open Library ID: OL17152551M - OL48612039M - OL22623697M - OL34453169M
- Online Computer Library Center (OCLC) ID: 56066486
- Library of Congress Control Number (LCCN): 2004017480
- All ISBNs: ➤ 9781588292520 - 9781592598953 - 1617374539 - 9781617374531 - 1592598951 - 1588292525
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:
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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4Proteolytic enzymes
By Alan J. Barrett

“Proteolytic enzymes” Metadata:
- Title: Proteolytic enzymes
- Author: Alan J. Barrett
- Language: English
- Number of Pages: Median: 765
- Publisher: ➤ Academic Press - Elsevier Science & Technology Books
- Publish Date: 1994 - 1995
“Proteolytic enzymes” Subjects and Themes:
- Subjects: ➤ Peptidasen - Enzymes - Serinproteinasen - Proteolytic enzymes - Cysteine endopeptidases - Proteolyse - Enzymologia - Cysteine - Serine endopeptidases - Peptidases a serine - Peptidases - Peptide hydrolases - Serine - Podre·czniki laboratoryjne - Proteasen - Classification - Cysteinproteasen - Peptidases a cysteine - Peptydazy - Peptidase - Serine Proteases - Cysteine Proteases
Edition Identifiers:
- The Open Library ID: OL34527869M - OL7326259M - OL9280907M - OL34527831M
- Online Computer Library Center (OCLC) ID: 31473281
- All ISBNs: ➤ 0121821455 - 0080883575 - 0080883613 - 9780121821456 - 9780080883571 - 9780080883618
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.
Online Borrowing:
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5Development of synthetic peptide substrates for the poliovirus 3C proteinase
By Jeffrey Robert Weidner
“Development of synthetic peptide substrates for the poliovirus 3C proteinase” Metadata:
- Title: ➤ Development of synthetic peptide substrates for the poliovirus 3C proteinase
- Author: Jeffrey Robert Weidner
- Language: English
- Number of Pages: Median: 130
- Publisher: Gainesville, FL
- Publish Date: 1989
“Development of synthetic peptide substrates for the poliovirus 3C proteinase” Subjects and Themes:
- Subjects: Research - Cysteine Endopeptidases - Endopeptidases - Polioviruses - Chromatography, High Pressure Liquid.
Edition Identifiers:
- The Open Library ID: OL58803695M
Access and General Info:
- First Year Published: 1989
- Is Full Text Available: Yes
- Is The Book Public: Yes
- Access Status: Public
Online Access
Online Borrowing:
- Borrowing from Open Library: Borrowing link
- Borrowing from Archive.org: Borrowing link
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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