Results 281 to 290 of about 27,386 (335)
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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
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2016
Carbonic anhydrases (CAs, EC 4.2.1.1) are metalloenzymes which catalyze the hydration of carbon dioxide to bicarbonate and protons. Many pathogenic bacteria encode such enzymes belonging to the α-, β-, and/or γ-CA families. In the last decade enzymes from Neisseria spp., Helicobacter pylori, Escherichia coli, Mycobacterium tuberculosis, Brucella spp ...
Capasso C., Supuran C. T.
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Carbonic anhydrases (CAs, EC 4.2.1.1) are metalloenzymes which catalyze the hydration of carbon dioxide to bicarbonate and protons. Many pathogenic bacteria encode such enzymes belonging to the α-, β-, and/or γ-CA families. In the last decade enzymes from Neisseria spp., Helicobacter pylori, Escherichia coli, Mycobacterium tuberculosis, Brucella spp ...
Capasso C., Supuran C. T.
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Future Medicinal Chemistry, 2018
Mammalian carbonic anhydrases (CAs; EC 4.2.1.1) of which 16 isoforms are known, are involved in important physiological functions. Their inhibition is exploited pharmacologically for the treatment of many diseases (glaucoma, edema, epilepsy, obesity, hypoxic tumors, neuropathic pain, etc.) but the activators were less investigated till recently.
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Mammalian carbonic anhydrases (CAs; EC 4.2.1.1) of which 16 isoforms are known, are involved in important physiological functions. Their inhibition is exploited pharmacologically for the treatment of many diseases (glaucoma, edema, epilepsy, obesity, hypoxic tumors, neuropathic pain, etc.) but the activators were less investigated till recently.
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2016
Carbonic anhydrases (CAs, EC 4.2.1.1) belonging to the α-, β-, and η-classes are present in many pathogenic protozoa, such as those belonging to the Trypanosoma, Leishmania, and Plasmodium genera. In the last years many such enzymes have been cloned, purified, and extensively characterized.
Supuran C. T., Capasso C.
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Carbonic anhydrases (CAs, EC 4.2.1.1) belonging to the α-, β-, and η-classes are present in many pathogenic protozoa, such as those belonging to the Trypanosoma, Leishmania, and Plasmodium genera. In the last years many such enzymes have been cloned, purified, and extensively characterized.
Supuran C. T., Capasso C.
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2000
Microalgae grown in ordinary air (0.04% CO2) show a much higher affinity for inorganic carbon (Ci) in photosynthesis than those grown with 2% to 5% CO2, although at saturating CO2 concentrations the maximum rate of photosynthesis is almost the same.
H, Fukuzawa, M, Tsuzuki, S, Miyachi
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Microalgae grown in ordinary air (0.04% CO2) show a much higher affinity for inorganic carbon (Ci) in photosynthesis than those grown with 2% to 5% CO2, although at saturating CO2 concentrations the maximum rate of photosynthesis is almost the same.
H, Fukuzawa, M, Tsuzuki, S, Miyachi
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Bioorganic & Medicinal Chemistry Letters, 2010
Carbonic anhydrases (CAs, EC 4.2.1.1) are widespread enzymes in all organisms, catalyzing CO2 hydration to bicarbonate and protons. Their inhibition is exploited clinically for decades for various classes of diuretics and systemically acting antiglaucoma agents.
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Carbonic anhydrases (CAs, EC 4.2.1.1) are widespread enzymes in all organisms, catalyzing CO2 hydration to bicarbonate and protons. Their inhibition is exploited clinically for decades for various classes of diuretics and systemically acting antiglaucoma agents.
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Nature, 1947
IN contrast to the wealth of information concerning carbonic anhydrase in the animal kingdom, there have been few reports of the occurrence of this enzyme in the plant kingdom1. It seemed desirable, therefore, briefly to describe the following observations made in the course of work on the enzyme in animal tissues.
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IN contrast to the wealth of information concerning carbonic anhydrase in the animal kingdom, there have been few reports of the occurrence of this enzyme in the plant kingdom1. It seemed desirable, therefore, briefly to describe the following observations made in the course of work on the enzyme in animal tissues.
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