dc.contributor.author |
Chronopoulou, EG |
en |
dc.contributor.author |
Labrou, NE |
en |
dc.date.accessioned |
2014-06-06T06:49:40Z |
|
dc.date.available |
2014-06-06T06:49:40Z |
|
dc.date.issued |
2009 |
en |
dc.identifier.issn |
18722083 |
en |
dc.identifier.uri |
http://dx.doi.org/10.2174/187220809789389135 |
en |
dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/4709 |
|
dc.subject |
1-chloro-2,4-dinitrobenzene |
en |
dc.subject |
CDNB |
en |
dc.subject |
G-site |
en |
dc.subject |
Glutathione |
en |
dc.subject |
Glutathione binding site |
en |
dc.subject |
Glutathione transferase |
en |
dc.subject |
GSH |
en |
dc.subject |
GST |
en |
dc.subject |
H-site |
en |
dc.subject |
Hydrophobic binding site |
en |
dc.subject.other |
canfosfamide |
en |
dc.subject.other |
enzyme inhibitor |
en |
dc.subject.other |
glutathione transferase |
en |
dc.subject.other |
glutathione transferase A1 |
en |
dc.subject.other |
glutathione transferase A3 3 enzyme inhibitor |
en |
dc.subject.other |
glutathione transferase P1 |
en |
dc.subject.other |
glutathione transferase P1 1 |
en |
dc.subject.other |
oxygen arylated diazeniumdiolate derivative |
en |
dc.subject.other |
prodrug |
en |
dc.subject.other |
sulfonamide |
en |
dc.subject.other |
unclassified drug |
en |
dc.subject.other |
biosensor |
en |
dc.subject.other |
biotechnology |
en |
dc.subject.other |
cancer diagnosis |
en |
dc.subject.other |
cancer resistance |
en |
dc.subject.other |
cancer therapy |
en |
dc.subject.other |
disease marker |
en |
dc.subject.other |
drug activation |
en |
dc.subject.other |
drug design |
en |
dc.subject.other |
drug detoxification |
en |
dc.subject.other |
drug mechanism |
en |
dc.subject.other |
drug structure |
en |
dc.subject.other |
enzyme activity |
en |
dc.subject.other |
enzyme analysis |
en |
dc.subject.other |
enzyme assay |
en |
dc.subject.other |
enzyme inhibition |
en |
dc.subject.other |
enzyme structure |
en |
dc.subject.other |
herbicide tolerance |
en |
dc.subject.other |
human |
en |
dc.subject.other |
liver function |
en |
dc.subject.other |
neoplasm |
en |
dc.subject.other |
nonhuman |
en |
dc.subject.other |
patent |
en |
dc.subject.other |
plant defense |
en |
dc.subject.other |
priority journal |
en |
dc.subject.other |
protein expression |
en |
dc.subject.other |
review |
en |
dc.subject.other |
transgenic plant |
en |
dc.subject.other |
Animals |
en |
dc.subject.other |
Biosensing Techniques |
en |
dc.subject.other |
Biotechnology |
en |
dc.subject.other |
Glutathione Transferase |
en |
dc.subject.other |
Herbicide Resistance |
en |
dc.subject.other |
Humans |
en |
dc.subject.other |
Medicine |
en |
dc.subject.other |
Plants, Genetically Modified |
en |
dc.title |
Glutathione transferases: Emerging multidisciplinary tools in red and green biotechnology |
en |
heal.type |
other |
en |
heal.identifier.primary |
10.2174/187220809789389135 |
en |
heal.publicationDate |
2009 |
en |
heal.abstract |
Cytosolic glutathione transferases (GSTs) are a diverse family of enzymes involved in a wide range of biological processes, many of which involve the conjugation of the tripeptide glutathione (GSH) to an electrophilic substrate. Detailed studies of GSTs are justified because of the considerable interest of these enzymes in medicine, agriculture and analytical biotechnology. For example, in medicine, GSTs are explored as molecular targets for the design of new anticancer drugs as a plausible means to sensitize drug-resistant tumors that overexpress GSTs. In agriculture, GSTs are exploited in the development of transgenic plants with increased resistance to biotic and abiotic stresses. Recently, selected isoenzymes of GSTs have found successful applications in the development of enzyme biosensors for the direct monitoring of environmental pollutants, such as herbicides and insecticides. This review article summarizes recent representative patents related to GSTs and their applications in biotechnology. © 2009 Bentham Science Publishers Ltd. |
en |
heal.journalName |
Recent Patents on Biotechnology |
en |
dc.identifier.issue |
3 |
en |
dc.identifier.volume |
3 |
en |
dc.identifier.doi |
10.2174/187220809789389135 |
en |
dc.identifier.spage |
211 |
en |
dc.identifier.epage |
223 |
en |