Explore: Inteins
Discover books, insights, and more — all in one place.
Learn more about Inteins with top reads curated from trusted sources — all in one place.
AI-Generated Overview About “inteins”:
Books Results
Source: The Open Library
The Open Library Search Results
Search results from The Open Library
1Artificial nucleases
By Marlene Belfort, Victoria Derbyshire, Barry L. Stoddard and David W. Wood

“Artificial nucleases” Metadata:
- Title: Artificial nucleases
- Authors: Marlene BelfortVictoria DerbyshireBarry L. StoddardDavid W. Wood
- Language: English
- Number of Pages: Median: 5847
- Publisher: Springer-Verlag - Springer
- Publish Date: 1987 - 2004 - 2005
- Publish Location: New York - Berlin
“Artificial nucleases” Subjects and Themes:
- Subjects: ➤ Artificial nucleases - Nucleic acids - DNA - Protein engineering - Endonucleases - Molecular biology - Biomédecine - Sciences de la vie - Inteins - Enzymes
Edition Identifiers:
- The Open Library ID: OL9055387M - OL3693037M - OL19291347M
- Online Computer Library Center (OCLC) ID: 53183388 - 22321387 - 62143715
- Library of Congress Control Number (LCCN): 2005922928 - 87004883 - 2003066404
- All ISBNs: ➤ 9783540251064 - 9783540201120 - 9780387175959 - 3540251065 - 0387175954 - 3540201122
Access and General Info:
- First Year Published: 1987
- 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.
Online Borrowing:
Online Marketplaces
Find Artificial nucleases at online marketplaces:
- Amazon: Audiable, Kindle and printed editions.
- Ebay: New & used books.
Wiki
Source: Wikipedia
Wikipedia Results
Search Results from Wikipedia
Protein splicing
intein-coding segments inserted at different positions. For these and other reasons, inteins (or more properly, the gene segments coding for inteins)
Central dogma of molecular biology
most inteins contain a homing endonuclease or HEG domain which is capable of finding a copy of the parent gene that does not include the intein nucleotide
Thermolabile
easy: generating conditional mutations by using temperature-sensitive inteins that function within different temperature ranges". Genetics. 183 (1):
Bacteria
Reaban ME, Coetzee T, Dalgaard JZ (July 1995). "Prokaryotic introns and inteins: a panoply of form and function". Journal of Bacteriology. 177 (14): 3897–903
Asparagine peptide lyase
solved for the intein V type proton ATPase catalytic subunit (Saccharomyces cerevisiae), a member of family N9 and for several inteins from family N10
Protein primary structure
Intramolecular transesterification, resulting in a branched polypeptide. In inteins, the new ester bond is broken by an intramolecular attack by the soon-to-be
Homing endonuclease
genes within introns, as fusions with host proteins, or as self-splicing inteins. They catalyze the hydrolysis of genomic DNA within the cells that synthesize
Protein
Deproteination DNA-binding protein Macromolecule Index of protein-related articles Intein List of proteins Proteopathy Proteopedia Protein sequence space Protein
Peptide bond
proteolysis and, more generally, in N–O acyl exchange reactions such as those of inteins. When the functional group attacking the peptide bond is a thiol, hydroxyl
Splice
joining pieces of genetic material Protein splicing, a natural process where inteins are removed Splice (system call), a system call used to transfer data on