نتائج البحث - "PHOSPHODIESTERASES"

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دورية أكاديمية

A rapid method for screening inhibitor effects: determination of I50 and its standard deviation.

المؤلفون: Job D, Cochet C, Dhien A, Chambaz EM

المصدر: Analytical biochemistry [Anal Biochem] 1978 Jan; Vol. 84 (1), pp. 68-77.

نوع المنشور: Journal Article

بيانات الدورية: Publisher: Elsevier Country of Publication: United States NLM ID: 0370535 Publication Model: Print Cited Medium: Print ISSN: 0003-2697 (Print) Linking ISSN: 00032697 NLM ISO Abbreviation: Anal Biochem Subsets: MEDLINE

مواضيع طبية MeSH: Enzyme Inhibitors* , Kinetics*, 3',5'-Cyclic-AMP Phosphodiesterases/antagonists & inhibitors ; Dose-Response Relationship, Drug ; Phosphodiesterase Inhibitors ; Statistics as Topic

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Sex-specific effects of daily tadalafil on diabetic heart kinetics in RECOGITO, a randomized, double-blind, placebo-controlled trial

المصدر: Science translational medicine. 14(649)

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74f5e4057b15a357d90f5b0413d7f5ec
https://pubmed.ncbi.nlm.nih.gov/35704597

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تقرير

Novel methods for physical mapping of the human genome applied to the long arm of chromosome 5

المساهمون: McClelland, M

وصف الملف: Medium: ED; Size: Pages: (17 p)

URL الوصول: http://www.osti.gov/scitech/servlets/purl/7206400

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Homogeneous single-label cGMP detection platform for the functional study of nitric oxide-sensitive (soluble) guanylyl cyclases and cGMP-specific phosphodiesterases

المؤلفون: Kopra, Kari, Sharina, Iraida, Martin, Emil, Härmä, Harri

المصدر: Scientific Reports, Vol 10, Iss 1, Pp 1-11 (2020)
Scientific Reports

URL الوصول: https://explore.openaire.eu/search/publication?articleId=pmid_dedup__::34b93c484bdc8d408f3bdda5b9553cb7
http://link.springer.com/article/10.1038/s41598-020-74611-x

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Structure of PDE3A-SLFN12 complex reveals requirements for activation of SLFN12 RNase

المصدر: 'Nature Communications ', vol: 12, pages: 4375-1-4375-16 (2021)
Nature Communications, Vol 12, Iss 1, Pp 1-16 (2021)
Nature Communications

مصطلحات موضوعية: Protein Conformation, alpha-Helical, Cell death, 0301 basic medicine, Cancer therapy, Cell Survival, RNase P, Science, General Physics and Astronomy, Plasma protein binding, Mass Spectrometry, Article, General Biochemistry, Genetics and Molecular Biology, 03 medical and health sciences, 0302 clinical medicine, Protein structure, Multienzyme Complexes, Cryoelectron microscopy, Catalytic Domain, Tetrahydroisoquinolines, Endoribonucleases, Humans, X-ray crystallography, Multidisciplinary, Calorimetry, Differential Scanning, Chemistry, HEK 293 cells, Intracellular Signaling Peptides and Proteins, Phosphodiesterase, General Chemistry, Heterotetramer, Adenosine Monophosphate, Cyclic Nucleotide Phosphodiesterases, Type 3, Recombinant Proteins, Cell biology, Pyridazines, Kinetics, HEK293 Cells, 030104 developmental biology, Structural biology, 030220 oncology & carcinogenesis, Mutation, Cancer cell, Protein Multimerization, HeLa Cells, Protein Binding

وصف الملف: application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6cfd121cbb4144ac667f5c20f822fddc
https://doi.org/10.1038/s41467-021-24495-w

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6

Selective changes in cytosolic β-adrenergic cAMP signals and L-type Calcium Channel regulation by Phosphodiesterases during cardiac hypertrophy

المؤلفون: Aniella Abi-Gerges, Liliana R. V. Castro, Jérôme Leroy, Valérie Domergue, Grégoire Vandecasteele, Rodolphe Fischmeister

المساهمون: Signalisation et physiopathologie cardiovasculaire (CARPAT), Institut National de la Santé et de la Recherche Médicale (INSERM)-Université Paris-Saclay

المصدر: Journal of Molecular and Cellular Cardiology
Journal of Molecular and Cellular Cardiology, Elsevier, 2021, 150, pp.109-121. ⟨10.1016/j.yjmcc.2020.10.011⟩

مصطلحات موضوعية: 0301 basic medicine, Male, medicine.medical_specialty, Calcium Channels, L-Type, Heart Ventricles, Phosphodiesterase 3, Stimulation, Cardiomegaly, 030204 cardiovascular system & hematology, Models, Biological, 03 medical and health sciences, 0302 clinical medicine, Cytosol, [SDV.MHEP.CSC]Life Sciences [q-bio]/Human health and pathology/Cardiology and cardiovascular system, Isoprenaline, Internal medicine, Receptors, Adrenergic, beta, medicine, Cyclic AMP, Animals, L-type calcium channel, Myocytes, Cardiac, Rats, Wistar, Receptor, Molecular Biology, chemistry.chemical_classification, Chemistry, Phosphodiesterase, Cyclic Nucleotide Phosphodiesterases, Type 3, Cyclic Nucleotide Phosphodiesterases, Type 4, Kinetics, 030104 developmental biology, Enzyme, Endocrinology, Phenotype, Phosphodiesterase 4 Inhibitors, Cardiology and Cardiovascular Medicine, medicine.drug

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f48ceafd4d8b7a8a4221c16aa494e9a7
https://pubmed.ncbi.nlm.nih.gov/33184031

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Molecular Dissection of Escherichia coli CpdB: Roles of the N Domain in Catalysis and Phosphate Inhibition, and of the C Domain in Substrate Specificity and Adenosine Inhibition

المؤلفون: Joaquim Rui Rodrigues, María Jesús Costas, José Carlos Cameselle, Alicia Cabezas, Iralis López-Villamizar, José Canales, João Meireles Ribeiro, Rosa María Pinto

المصدر: International Journal of Molecular Sciences
Volume 22
Issue 4
International Journal of Molecular Sciences, Vol 22, Iss 1977, p 1977 (2021)

مصطلحات موضوعية: Models, Molecular, 0301 basic medicine, Adenosine, substrate specificity, medicine.disease_cause, cyclic dinucleotide, lcsh:Chemistry, Catalytic Domain, lcsh:QH301-705.5, Spectroscopy, chemistry.chemical_classification, Cyclic nucleotide phosphodiesterase, Escherichia coli Proteins, Hydrolysis, protein domain, General Medicine, Computer Science Applications, substrate-binding site, Biochemistry, 2',3'-Cyclic-Nucleotide Phosphodiesterases, inhibitor sensitivity, medicine.drug, truncated protein, Protein domain, point mutant, Catalysis, Article, Phosphates, Inorganic Chemistry, Structure-Activity Relationship, 03 medical and health sciences, Protein Domains, Nucleotidase, Escherichia coli, medicine, Point Mutation, Histidine, Physical and Theoretical Chemistry, Binding site, Molecular Biology, pathogen–host interaction, Binding Sites, 030102 biochemistry & molecular biology, Organic Chemistry, Periplasmic space, catalytic site, Kinetics, 030104 developmental biology, Enzyme, lcsh:Biology (General), lcsh:QD1-999, chemistry, Biocatalysis, extracytoplasmic phosphodiesterase