Explore: Glutaredoxin
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Books Results
Source: The Open Library
The Open Library Search Results
Search results from The Open Library
1Bacteriophage T4 thioredoxin structure at 2.8 Å resolution and a comparison between molecules belonging to the thioredoxin glutaredoxin family of proteins
By Ulf Sonnerstam
“Bacteriophage T4 thioredoxin structure at 2.8 Å resolution and a comparison between molecules belonging to the thioredoxin glutaredoxin family of proteins” Metadata:
- Title: ➤ Bacteriophage T4 thioredoxin structure at 2.8 Å resolution and a comparison between molecules belonging to the thioredoxin glutaredoxin family of proteins
- Author: Ulf Sonnerstam
- Language: English
- Number of Pages: Median: 5830
- Publisher: ➤ Dept. of Chemistry and Molecular Biology, Swedish University of Agricultural Sciences
- Publish Date: 1984
- Publish Location: Uppsala
“Bacteriophage T4 thioredoxin structure at 2.8 Å resolution and a comparison between molecules belonging to the thioredoxin glutaredoxin family of proteins” Subjects and Themes:
- Subjects: Thioredoxin - Glutaredoxin - Proteins
Edition Identifiers:
- The Open Library ID: OL57248195M
- Online Computer Library Center (OCLC) ID: 13598094
- All ISBNs: 9157621039 - 9789157621030
Access and General Info:
- First Year Published: 1984
- Is Full Text Available: No
- Is The Book Public: No
- Access Status: No_ebook
Online Marketplaces
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2Thioredoxin and glutaredoxin systems
By Arne Holmgren
“Thioredoxin and glutaredoxin systems” Metadata:
- Title: ➤ Thioredoxin and glutaredoxin systems
- Author: Arne Holmgren
- Language: English
- Number of Pages: Median: 411
- Publisher: Raven Press
- Publish Date: 1986
- Publish Location: New York
“Thioredoxin and glutaredoxin systems” Subjects and Themes:
- Subjects: ➤ Glutaredoxin - Congresses - Thioredoxin - Bacterial Proteins - Thioredoxins - Carbolic acid - Phenols - Biochemistry - Pharmacology
Edition Identifiers:
- The Open Library ID: OL2541961M
- Online Computer Library Center (OCLC) ID: 13062764
- Library of Congress Control Number (LCCN): 85023307
- All ISBNs: 9780881672022 - 0881672025
Access and General Info:
- First Year Published: 1986
- Is Full Text Available: No
- Is The Book Public: No
- Access Status: No_ebook
Online Marketplaces
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3Structural and functional studies on glutaredoxin and thioredoxin
By Matti J. Nikkola
“Structural and functional studies on glutaredoxin and thioredoxin” Metadata:
- Title: ➤ Structural and functional studies on glutaredoxin and thioredoxin
- Author: Matti J. Nikkola
- Language: English
- Publisher: ➤ Swedish University of Agricultural Sciences, Dept. of Molecular Biology
- Publish Date: 1991
- Publish Location: Uppsala
“Structural and functional studies on glutaredoxin and thioredoxin” Subjects and Themes:
- Subjects: Glutaredoxin - Thioredoxin
Edition Identifiers:
- The Open Library ID: OL18009565M
- Online Computer Library Center (OCLC) ID: 26118772
- All ISBNs: 9157645418 - 9789157645418
Access and General Info:
- First Year Published: 1991
- Is Full Text Available: No
- Is The Book Public: No
- Access Status: No_ebook
Online Marketplaces
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- Ebay: New & used books.
Wiki
Source: Wikipedia
Wikipedia Results
Search Results from Wikipedia
Glutaredoxin
Glutaredoxins (also known as Thioltransferase) are small redox enzymes of approximately one hundred amino-acid residues that use glutathione as a cofactor
Glutathione
electron donor. Other enzymes using glutathione as a substrate are glutaredoxins. These small oxidoreductases are involved in flower development, salicylic
GLRX
Glutaredoxin-1 is a protein that in humans is encoded by the GLRX gene. GLRX has been shown to interact with Wilson disease protein and ATP7A. GRCh38:
Glutaredoxin 2 (bacterial)
molecular biology, the glutaredoxin 2 family is a family of bacterial glutaredoxins. Unlike other glutaredoxins, glutaredoxin 2 (Grx2) cannot reduce ribonucleotide
Thioredoxin reductase
eukaryotes and one in animals. Bacterial TrxR also catalyzes the reduction of glutaredoxin like proteins known as NrdH. Both classes are flavoproteins which function
Arsenate reductase (glutaredoxin)
Arsenate reductase (glutaredoxin) (EC 1.20.4.1) is an enzyme that catalyzes the chemical reaction arsenate + glutaredoxin ⇌ {\displaystyle \rightleftharpoons
Oxoglutarate dehydrogenase complex
radicals, and can be undone after hydrogen peroxide consumption via glutaredoxin. Glutathionylation "protects" the lipoic acid of the E2 domain from undergoing
Chloride channel
conserved glutaredoxin monothiol motif, similar to the omega class GSTs. Al Khamici et al. demonstrated that CLIC proteins have glutaredoxin-like glutathione-dependent
Thioredoxin
similar to thioredoxins but with a sequence more akin to glutaredoxins. Unlike typical glutaredoxins, NrdH can accept electrons from thioredoxin reductase
List of enzymes
Category:EC 1.20.2 Category:EC 1.20.4 Arsenate reductase (glutaredoxin) EC 1.20.4.1 Glutaredoxin Category:EC 1.20.9 Category:EC 1.20.99 Category:EC 1.21