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|a 904406986
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|a 9780444632630
|q (electronic bk.)
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|a 0444632638
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|z 9780444632586
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|z (OCoLC)904406986
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|a 572.79
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|a Carbonic anhydrases as biocatalysts :
|b from theory to medical and industrial applications /
|c edited by Claudiu T. Supuran, Giuseppina De Simone.
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|a Amsterdam :
|b Elsevier,
|c [2015]
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|c �2015
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|a 1 online resource :
|b illustrations (some color)
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|a text
|b txt
|2 rdacontent
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|b c
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|a online resource
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|a Includes bibliographical references and index.
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|a Online resource; title from PDF title page (EBSCO, viewed January 21, 2015).
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|a Carbonic anhydrases (CAs, EC 4.2.1.1) are ubiquitous metalloenzymes, present throughout most living organisms and encoded by five evolutionarily unrelated gene families. The Carbonic Anhydrases as Biocatalysts: From Theory to Medical and Industrial Applications presents information on the growing interest in the study of this enzyme family and their applications to both medicine and biotechnology.
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|a Cover; Title Page; Copyright Page; Table of contents; List of Contributors; Preface; Part 1 -- Introduction; Chapter 1 -- Carbonic Anhydrases: An Overview; 1.1 -- Carbonic anhydrase families; 1.2 -- Catalytic features; 1.3 -- CA inhibition and activation; 1.4 -- Biomedical applications of the CAs; 1.5 -- Biotechnological applications of the CAs; References; Part 2 -- Carbonic Anhydrasesas Drug Targets; Chapter 2 -- Human Carbonic Anhydrases: Catalytic Properties, Structural Features, and Tissue Distribution; 2.1 -- Introduction; 2.2 -- hCAs' structural features; 2.3 -- hCAs' catalytic features.
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|a 2.4 -- hCAs' tissue distribution and their role as drug targetsReferences; Chapter 3 -- Carbonic Anhydrase I; 3.1 -- Introduction; 3.2 -- Structure of CA I; 3.3 -- Tissue localization and physiological functions; 3.4 -- CA I as pharmacological target; 3.5 -- CA I inhibitors; 3.6 -- CA I activators; 3.7 -- Conclusions and perspectives; Acknowledgment; References; Chapter 4 -- Carbonic Anhydrase II as Target for Drug Design; 4.1 -- Introduction; 4.2 -- Biochemical properties, genetic relationship with the other cytosolic isoforms, and 3D structure of hCA II; 4.3 -- hCA II inhibitors.
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|a 4.4 -- Antiglaucoma agents4.4.1 -- First-generation inhibitors; 4.4.2 -- Second-generation inhibitors: topically acting sulfonamides; 4.4.3 -- Third-generation inhibitors; 4.4.4 -- Dithiocarbamates and xanthates as topically acting antiglaucoma CAIs targeting hCA II; 4.5 -- Diuretics with CA inhibitory properties; 4.6 -- Agents for the management of altitude sickness; 4.7 -- Various pharmacological actions connected with CA II inhibition: serendipity or off-targeting with impressive efficacy?; 4.8 -- CA II inhibitors in the management of tumors?
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|a 4.9 -- New strategies to design CA II-selective inhibitors4.10 -- CA II activation; 4.11 -- Conclusions; References; Chapter 5 -- Carbonic Anhydrase III; 5.1 -- Introduction; 5.2 -- Discovery of CA III; 5.3 -- Physiological role of CA III; 5.4 -- Molecular characterization of CA III; 5.5 -- Catalytic properties and proton transfer of CA III; 5.6 -- CA III as a biomarker: role in disease states; 5.7 -- CA III as a drug target; Acknowledgment; References; Chapter 6 -- Carbonic Anhydrase IV; 6.1 -- Introduction; 6.2 -- Genomic organization and chromosomal localization of human CA IV.
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|a 6.3 -- Cloning and molecular characterization of human CA IV6.4 -- Structure/function: the role of disulfide bonds; 6.5 -- Characterization of catalytic properties of human CA IV and its inhibition by sulfonamide inhibitors; 6.6 -- Expression of CA IV in different tissues; 6.7 -- Physiological functions of CA IV; 6.7.1 -- Kidney function; 6.7.2 -- Neuronal function; 6.7.3 -- Eye function; 6.7.4 -- Skeletal and cardiac muscle function; 6.7.5 -- CA IV functions in metabolons; 6.7.6 -- The role of CA IV in the taste of carbonation; 6.7.7 -- Disease-causing mutations in CA IV; 6.7.8 -- Kidney disease.
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|a 6.7.9 -- Environmental factors contributing to RP-17 associated with CA IV mutations.
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|a Carbonic anhydrase.
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650 |
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|a Carbonic anhydrase
|x Therapeutic use.
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650 |
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|a Enzymes.
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650 |
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0 |
|a Enzymes
|x Therapeutic use.
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650 |
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|a Biotechnology.
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650 |
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2 |
|a Carbonic Anhydrases
|0 (DNLM)D002256
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650 |
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2 |
|a Enzymes
|0 (DNLM)D004798
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650 |
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2 |
|a Biotechnology
|0 (DNLM)D001709
|
650 |
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|a Anhydrase carbonique.
|0 (CaQQLa)201-0088394
|
650 |
|
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|a Anhydrase carbonique
|0 (CaQQLa)201-0088394
|x Emploi en th�erapeutique.
|0 (CaQQLa)201-0373975
|
650 |
|
6 |
|a Enzymes.
|0 (CaQQLa)201-0002557
|
650 |
|
6 |
|a Enzymes
|0 (CaQQLa)201-0002557
|x Emploi en th�erapeutique.
|0 (CaQQLa)201-0373975
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650 |
|
6 |
|a Biotechnologie.
|0 (CaQQLa)201-0004007
|
650 |
|
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|a enzyme.
|2 aat
|0 (CStmoGRI)aat300212647
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650 |
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|a bioengineering.
|2 aat
|0 (CStmoGRI)aat300250623
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650 |
|
7 |
|a SCIENCE
|x Life Sciences
|x Biochemistry.
|2 bisacsh
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650 |
|
7 |
|a Biotechnology
|2 fast
|0 (OCoLC)fst00832729
|
650 |
|
7 |
|a Carbonic anhydrase
|2 fast
|0 (OCoLC)fst00846939
|
650 |
|
7 |
|a Enzymes
|2 fast
|0 (OCoLC)fst00913605
|
650 |
|
7 |
|a Enzymes
|x Therapeutic use
|2 fast
|0 (OCoLC)fst00913631
|
700 |
1 |
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|a Supuran, Claudiu T.,
|d 1962-
|e editor.
|
700 |
1 |
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|a Simone, Giuseppina De,
|e editor.
|
776 |
0 |
8 |
|i Print version:
|a Supuran, Claudiu T.
|t Carbonic Anhydrases as Biocatalysts : From Theory to Medical and Industrial Applications.
|d Burlington : Elsevier Science, �2015
|z 9780444632586
|
856 |
4 |
0 |
|u https://sciencedirect.uam.elogim.com/science/book/9780444632586
|z Texto completo
|