| dc.contributor.author |
Labrou, NE |
en |
| dc.contributor.author |
Papageorgiou, AC |
en |
| dc.contributor.author |
Avramis, VI |
en |
| dc.date.accessioned |
2014-06-06T06:50:43Z |
|
| dc.date.available |
2014-06-06T06:50:43Z |
|
| dc.date.issued |
2010 |
en |
| dc.identifier.issn |
09298673 |
en |
| dc.identifier.uri |
http://dx.doi.org/10.2174/092986710791299920 |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/5135 |
|
| dc.subject |
Acute lymphoblastic leukemia |
en |
| dc.subject |
Catalytic mechanism protein crystallography |
en |
| dc.subject |
L-asparaginase |
en |
| dc.subject |
Protein drug |
en |
| dc.subject.other |
agarose |
en |
| dc.subject.other |
amino acid |
en |
| dc.subject.other |
ammonia |
en |
| dc.subject.other |
antineoplastic agent |
en |
| dc.subject.other |
asparaginase macrogol |
en |
| dc.subject.other |
asparagine |
en |
| dc.subject.other |
bleomycin |
en |
| dc.subject.other |
cisplatin |
en |
| dc.subject.other |
corticosteroid |
en |
| dc.subject.other |
cyclophosphamide |
en |
| dc.subject.other |
cytosine |
en |
| dc.subject.other |
doxorubicin |
en |
| dc.subject.other |
enzyme antibody |
en |
| dc.subject.other |
glutaminase |
en |
| dc.subject.other |
liposome |
en |
| dc.subject.other |
methotrexate |
en |
| dc.subject.other |
monomer |
en |
| dc.subject.other |
polyacrylamide |
en |
| dc.subject.other |
vincristine |
en |
| dc.subject.other |
acute lymphoblastic leukemia |
en |
| dc.subject.other |
anaphylactic shock |
en |
| dc.subject.other |
anaphylaxis |
en |
| dc.subject.other |
blood clotting disorder |
en |
| dc.subject.other |
catalysis |
en |
| dc.subject.other |
clinical trial |
en |
| dc.subject.other |
disease severity |
en |
| dc.subject.other |
drug activity |
en |
| dc.subject.other |
drug efficacy |
en |
| dc.subject.other |
drug formulation |
en |
| dc.subject.other |
drug half life |
en |
| dc.subject.other |
drug hydrolysis |
en |
| dc.subject.other |
drug hypersensitivity |
en |
| dc.subject.other |
drug information |
en |
| dc.subject.other |
drug structure |
en |
| dc.subject.other |
drug synthesis |
en |
| dc.subject.other |
erratum |
en |
| dc.subject.other |
Erwinia |
en |
| dc.subject.other |
Escherichia coli |
en |
| dc.subject.other |
gene sequence |
en |
| dc.subject.other |
human |
en |
| dc.subject.other |
hydrolysis |
en |
| dc.subject.other |
hyperlipidemia |
en |
| dc.subject.other |
immune response |
en |
| dc.subject.other |
lymphoma |
en |
| dc.subject.other |
microcapsule |
en |
| dc.subject.other |
pancreatitis |
en |
| dc.subject.other |
protein engineering |
en |
| dc.subject.other |
site directed mutagenesis |
en |
| dc.subject.other |
treatment response |
en |
| dc.subject.other |
Asparaginase |
en |
| dc.subject.other |
Catalytic Domain |
en |
| dc.subject.other |
Clinical Trials as Topic |
en |
| dc.subject.other |
Humans |
en |
| dc.subject.other |
Precursor Cell Lymphoblastic Leukemia-Lymphoma |
en |
| dc.subject.other |
Protein Engineering |
en |
| dc.subject.other |
Protein Structure, Tertiary |
en |
| dc.subject.other |
Structure-Activity Relationship |
en |
| dc.title |
Structure-function relationships and clinical applications of L-Asparaginases |
en |
| heal.type |
other |
en |
| heal.identifier.primary |
10.2174/092986710791299920 |
en |
| heal.publicationDate |
2010 |
en |
| heal.abstract |
L-Asparaginase (L-ASNase, EC 3.5.1.1) catalyzes the hydrolysis of the non-essential amino acid L-Asn to LAsp and ammonia and is widely used for the treatment of haematopoetic diseases such as acute lymphoblastic leukaemia (ALL) and lymphomas. Therapeutic forms of L-ASNase come from different biological sources (primarily E. coli and Erwinia chrysanthemi). It is well established that the various preparations have different biochemical pharmacology properties,and different tendency to induce side-effects. This is due to different structural, physicochemical and kinetic properties of L-ASNases from the various biological sources. Understanding these properties of various L-ASNases would allow a better decipherment of their catalytic and therapeutic features, thus enabling more accurate predictions of the behaviour of these enzymes under a variety of therapeutic conditions. In addition, detailed understanding of the catalytic mechanism of L-ASNases might permit the design of new forms of L-ASNases with optimal biochemical properties for clinical applications. In this paper we review the available biochemical and pharmacokinetic information of the therapeutic forms of bacterial L-ASNases, and focus on a detailed description of structure, function and clinical applications of these enzymes © 2010 Bentham Science Publishers Ltd. |
en |
| heal.journalName |
Current Medicinal Chemistry |
en |
| dc.identifier.issue |
20 |
en |
| dc.identifier.volume |
17 |
en |
| dc.identifier.doi |
10.2174/092986710791299920 |
en |
| dc.identifier.spage |
2183 |
en |
| dc.identifier.epage |
2195 |
en |