Results 171 to 180 of about 44,336 (211)

Cyclic nucleotide phosphodiesterases

Journal of Allergy and Clinical Immunology, 2001
Cyclic nucleotide second messengers (cAMP and cGMP) play a central role in signal transduction and regulation of physiologic responses. Their intracellular levels are controlled by the complex superfamily of cyclic nucleotide phosphodiesterase (PDE) enzymes. Continuing advances in our understanding of the molecular pharmacology of these enzymes has led
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Cyclic Nucleotide Phosphodiesterase Assay Technology

Current Protocols in Pharmacology, 2010
AbstractBecause of their critical role in modulating cellular cyclic nucleotide levels, phosphodiesterases (PDEs) are involved in many disease‐related signaling pathways. The PDE family is large and diverse, with members having different tissue distribution, sub‐cellular localizations, and substrate specificities.
S J, MacKenzie, S F, Hastings, C, Wells
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Cyclic nucleotide phosphodiesterase from Tetrahymena

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1973
Abstract The existence of multiple molecular forms of a cyclic nucleotide phosphodiesterase in Tetrahymena pyriformis is shown.
S, Ramanathan, S C, Chou
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Hormonal Regulation of Cyclic Nucleotide Phosphodiesterases*

Endocrine Reviews, 1991
I. Introduction ACOMPLEX array of signals from the extracellular environment regulate many cell processes, including the entry and exit from the mitotic cycle and the induction and maintenance of differentiation (1–3). Cells elaborate these external stimuli via receptors, transducers, and second messengers (4, 5) which control intricate circuits that ...
CONTI M, JIN SLC, MONACO, Lucia, REPASKE DR, SWINNEN JV   +4 more
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Crystallization of Cyclic Nucleotide Phosphodiesterases

2005
Selective inhibitors of cyclic nucleotide phosphodiesterases (PDEs) have been widely studied as therapeutic agents for the treatment of various human diseases. Three-dimensional structures are essential for the design of highly selective inhibitors, but their availability is limited by the speed of crystallization.
Hengming, Ke, Qing, Huai, Robert X, Xu
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Cyclic nucleotide phosphodiesterases in uterine development

Molecular and Cellular Endocrinology, 1975
Activities of cyclic nucleotide phosphodiesterase were studied in rat uterus as a function of age, DNA and protein content. Linear kinetics were observed for uterine homogenate cyclic GMP (cGMP) phosphodiesterase activity, but anomalous double-reciprocal plots, suggestive of multiple enzyme forms, were observed for cyclic AMP (cAMP) hydrolysis, cAMP ...
G M, Stancel, W J, Thompson, S J, Strada
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Calmodulin-dependent cyclic nucleotide phosphodiesterase (PDE1)

Cellular and Molecular Life Sciences, 1999
Ca2+/calmodulin-dependent cyclic nucleotide phosphodiesterase (PDE1) is one of the key enzymes involved in the complex interactions between the cyclic nucleotide and Ca2+ second messenger systems. Currently, three genes encode PDE1, and alternate splicing of these genes gives rise to functionally different isozymes which exhibit distinct catalytic and ...
R, Kakkar, R V, Raju, R K, Sharma
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Cyclic nucleotide phosphodiesterase in pea seedlings

Biochimica et Biophysica Acta (BBA) - Enzymology, 1972
Abstract An enzyme from pea seedlings that hydrolyzes both 2′,3′-cyclic nucleoside monophosphate and 3′,5′-cyclic nucleoside monophosphate has been partially purified from pea seedlings. It has a molecular weight of 350 000 and has optimal activity at pH 5.4–6.0. It is insensitive to methylxanthines and imidazole. It catalyzes the formation of 3′-AMP
P P, Lin, J E, Varner
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Cyclic Nucleotides and Phosphodiesterases in Platelets

Thrombosis and Haemostasis, 1999
IntroductionIt is now almost 30 years since the discovery that prostaglandin E1 (PGE1) inhibits platelet responses to aggregating agents, together with finding that the effects of this compound are mediated by adenosine 3′, 5′-cyclic monophosphate (cAMP) initiated interest in the physiological and pharmacological regulation of platelet function by ...
R J, Haslam, N T, Dickinson, E K, Jang
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Cyclic nucleotide phosphodiesterase of Chlamydomonas reinhardtii

Biochimica et Biophysica Acta (BBA) - Enzymology, 1974
Abstract Cyclic nucleotide phosphodiesterase (EC 3.1.4.17) activity was characterized in crude and (NH4)2SO4-fractionated extracts of the green alga Chlamydomonas reinhardtii. With cyclic AMP as substrate, the formation of 5′-AMP was optimal at pH 8.5 and required the presence of a sulfhydryl reagent and a divalent cation, Mg2+ and Mn2+ being the ...
U, Fischer, N, Amrhein
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