國立虎尾科技大學 |

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

紀錄類型:	書目-語言資料,印刷品 : Monograph/item
正題名/作者:	Carbonic Anhydrase as Drug Target/ edited by Daumantas Matulis.
其他題名:	Thermodynamics and Structure of Inhibitor Binding /
其他作者:	Matulis, Daumantas.
面頁冊數:	XXVI, 353 p. 169 illus., 107 illus. in color.online resource. :
Contained By:	Springer Nature eBook
標題:	Molecular biology. -
電子資源:	https://doi.org/10.1007/978-3-030-12780-0
ISBN:	9783030127800

Carbonic Anhydrase as Drug Target = Thermodynamics and Structure of Inhibitor Binding /
Carbonic Anhydrase as Drug TargetThermodynamics and Structure of Inhibitor Binding /[electronic resource] :edited by Daumantas Matulis. - 1st ed. 2019. - XXVI, 353 p. 169 illus., 107 illus. in color.online resource.

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.

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. .

ISBN: 9783030127800

Standard No.: 10.1007/978-3-030-12780-0doiSubjects--Topical Terms:

583443
Molecular biology.

LC Class. No.: QH506

Dewey Class. No.: 611.01816

Carbonic Anhydrase as Drug Target = Thermodynamics and Structure of Inhibitor Binding /
LDR:03214nam a22003975i 4500 001 1005191
003 DE-He213
005 20200703104525.0
007 cr nn 008mamaa
008 210106s2019 gw | s |||| 0|eng d
020 $a 9783030127800 $9 978-3-030-12780-0
024 7 $a 10.1007/978-3-030-12780-0 $2 doi
035 $a 978-3-030-12780-0
050 4 $a QH506
072 7 $a MBGR $2 bicssc
072 7 $a SCI049000 $2 bisacsh
072 7 $a MBGR $2 thema
072 7 $a PSD $2 thema
082 0 4 $a 611.01816 $2 23
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
347 $a text file $b PDF $2 rda
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. $3 583443
650 0 $a Medical biochemistry. $3 1254555
650 0 $a Proteins . $3 1253493
650 0 $a Medicinal chemistry. $3 1253747
650 0 $a Pharmaceutical technology. $3 557391
650 1 4 $a Molecular Medicine. $3 668353
650 2 4 $a Medical Biochemistry. $3 668897
650 2 4 $a Protein-Ligand Interactions. $3 882815
650 2 4 $a Medicinal Chemistry. $3 668872
650 2 4 $a Pharmaceutical Sciences/Technology. $3 768561
700 1 $a Matulis, Daumantas. $4 edt $4 http://id.loc.gov/vocabulary/relators/edt $3 1226667
710 2 $a SpringerLink (Online service) $3 593884
773 0 $t Springer Nature eBook
776 0 8 $i Printed edition: $z 9783030127787
776 0 8 $i Printed edition: $z 9783030127794
856 4 0 $u https://doi.org/10.1007/978-3-030-12780-0
912 $a ZDB-2-SBL
912 $a ZDB-2-SXB
950 $a Biomedical and Life Sciences (SpringerNature-11642)
950 $a Biomedical and Life Sciences (R0) (SpringerNature-43708)