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Saccharin Derivatives as Potential Inhibitors of Carbonic Anhydrases
, 2015 Jekaterīna Ivanova +3 more
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A subcellularly targeted photocaged inhibitor for mitochondrial carbonic anhydrase V.
Dalton TransMafy NN +6 more
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HUMAN CARBONIC ANHYDRASES AND CARBONIC ANHYDRASE DEFICIENCIES
Annual Review of Biochemistry, 1995Carbonic anhydrases (CAs I-VII) are products of a gene family that encodes seven isozymes and several homologous, CA- related proteins. All seven isozymes have been cloned, sequenced, and mapped, and the intron-exon organization of five genes established. They differ in subcellular localizations, being cytoplasmic (CA I, II, III, and VII), GPI-anchored
W S, Sly, P Y, Hu
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ChemInform, 2002
AbstractFor Abstract see ChemInform Abstract in Full Text.
SCOZZAFAVA, ANDREA +2 more
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AbstractFor Abstract see ChemInform Abstract in Full Text.
SCOZZAFAVA, ANDREA +2 more
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International Journal of Biochemistry, 1987
Some of the current studies of carbonic anhydrases are directed to the genetic mechanisms underlying their synthesis. Determination of the structure of their genes will probably most readily resolve the question of whether the membrane bound forms of the enzyme represent products of additional loci other than those of the three well-known soluble forms.
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Some of the current studies of carbonic anhydrases are directed to the genetic mechanisms underlying their synthesis. Determination of the structure of their genes will probably most readily resolve the question of whether the membrane bound forms of the enzyme represent products of additional loci other than those of the three well-known soluble forms.
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American Journal of Physiology-Renal Physiology, 1982
Carbonic anhydrase is a zinc metalloenzyme widely distributed throughout the tissues of the body. This enzyme exists in a number of isozymic forms in most mammalian species. Significant advances over the past decade have been made in characterizing the nature of renal carbonic anhydrase.
D C, Dobyan, R E, Bulger
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Carbonic anhydrase is a zinc metalloenzyme widely distributed throughout the tissues of the body. This enzyme exists in a number of isozymic forms in most mammalian species. Significant advances over the past decade have been made in characterizing the nature of renal carbonic anhydrase.
D C, Dobyan, R E, Bulger
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Novel Carbonic Anhydrase Inhibitors
Future Medicinal Chemistry, 2021Abstract
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2019
Among the seven different classes of carbonic anhydrases (CAs), the Ζ-class represents a very interesting one due to the biochemical peculiarity of CDCA1, which is the most investigated representative. In fact, CDCA1 is a cambialistic enzyme being able to naturally exchange Zn(II) with Cd(II) and vice versa, within its catalytic site.
Langella, E. +4 more
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Among the seven different classes of carbonic anhydrases (CAs), the Ζ-class represents a very interesting one due to the biochemical peculiarity of CDCA1, which is the most investigated representative. In fact, CDCA1 is a cambialistic enzyme being able to naturally exchange Zn(II) with Cd(II) and vice versa, within its catalytic site.
Langella, E. +4 more
openaire +2 more sources