Carbonic Anhydrase as Drug Target Thermodynamics and Structure of Inhibitor Binding /

This book offers deep insights into the thermodynamics and molecular structures of the twelve catalytically active isoforms of human carbonic anhydrase (CA) with a particular focus on inhibitor binding for drug design. X-ray crystallographic structures in combination with enzyme kinetic testing prov...

Πλήρης περιγραφή

Λεπτομέρειες βιβλιογραφικής εγγραφής
Συγγραφή απο Οργανισμό/Αρχή: SpringerLink (Online service)
Άλλοι συγγραφείς: Matulis, Daumantas (Επιμελητής έκδοσης, http://id.loc.gov/vocabulary/relators/edt)
Μορφή: Ηλεκτρονική πηγή Ηλ. βιβλίο
Γλώσσα:English
Έκδοση: Cham : Springer International Publishing : Imprint: Springer, 2019.
Έκδοση:1st ed. 2019.
Θέματα:
Διαθέσιμο Online:Full Text via HEAL-Link
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245 1 0 |a Carbonic Anhydrase as Drug Target  |h [electronic resource] :  |b Thermodynamics and Structure of Inhibitor Binding /  |c edited by Daumantas Matulis. 
250 |a 1st ed. 2019. 
264 1 |a Cham :  |b Springer International Publishing :  |b Imprint: Springer,  |c 2019. 
300 |a XXVI, 353 p. 169 illus., 107 illus. in color.  |b online resource. 
336 |a text  |b txt  |2 rdacontent 
337 |a computer  |b c  |2 rdamedia 
338 |a online resource  |b cr  |2 rdacarrier 
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505 0 |a Final ToC tbd. 1) Description of human carbonic anhydrases (12 catalytically active human isoforms; isoforms as drug targets, enzymatic activity, catalytic mechanism, thermodynamics of protonation of the water molecule in the active site) -- 2) Thermal stabilities of all isoform CA catalytic domains -- Thermodynamics of inhibitor binding to CAs (incl. intrinsic thermodynamics - not mentioned important subject in most CA literature) -- 3) Comparison of methods to determine inhibitor binding to CAs (ITC, FTSA, enzymatic activity assays) -- 4) Chemical synthesis of CA inhibitors -- 5) X-ray crystallographic structures of CAs and their complexes with inhibitors -- 6) Antibodies against CAs. 
520 |a This book offers deep insights into the thermodynamics and molecular structures of the twelve catalytically active isoforms of human carbonic anhydrase (CA) with a particular focus on inhibitor binding for drug design. X-ray crystallographic structures in combination with enzyme kinetic testing provide information on the interaction of CAs and their inhibitors, knowledge which is crucial for rational drug design. CAs are zinc carrying enzymes that catalyse the reversible interconversion of carbon dioxide and bicarbonate and are involved in numerous cellular processes. They are therefore a common target for drugs. The suppression of CA activities through inhibitory compounds has found application for example in diuretics and in glaucoma therapy. In this book methods used to determine binding thermodynamics of inhibitory compounds (Isothermal titration calorimetry, Fluorescent thermal shift assay/differential scanning fluorimetry and others) will be compared in detail. Also types and chemical synthesis of CA inhibitors, the use of antibodies against CAs as well as inhibitor application in animals are discussed. . 
650 0 |a Molecular biology. 
650 0 |a Medical biochemistry. 
650 0 |a Proteins . 
650 0 |a Medicinal chemistry. 
650 0 |a Pharmaceutical technology. 
650 1 4 |a Molecular Medicine.  |0 http://scigraph.springernature.com/things/product-market-codes/B1700X 
650 2 4 |a Medical Biochemistry.  |0 http://scigraph.springernature.com/things/product-market-codes/H35005 
650 2 4 |a Protein-Ligand Interactions.  |0 http://scigraph.springernature.com/things/product-market-codes/L14060 
650 2 4 |a Medicinal Chemistry.  |0 http://scigraph.springernature.com/things/product-market-codes/C28000 
650 2 4 |a Pharmaceutical Sciences/Technology.  |0 http://scigraph.springernature.com/things/product-market-codes/B21010 
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776 0 8 |i Printed edition:  |z 9783030127794 
856 4 0 |u https://doi.org/10.1007/978-3-030-12780-0  |z Full Text via HEAL-Link 
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950 |a Biomedical and Life Sciences (Springer-11642)