نتایج جستجو برای: mg2

تعداد نتایج: 7906  

Journal: :Circulation research 1976
R J Solaro J S Shiner

Increases in free Mg2+ from 0.04 to 10.0 mM with constant pH 7.0 TO 0.10 M ionic strength, and 2 mM MgATP2- caused a rightward shift of the free Ca-relative ATPase relation for both cardiac skeletal myofibrils. The specific activity of cardiac myofibrillar ATPase over a wide range of free Ca2+ was, however, depressed in 0.04 vs. 1.0 mM Mg2+, whereas a similar decrease in free Mg2+ slightly enha...

Journal: :Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas 1999
D Falkenstein C A Ribeiro J F Figueiredo

High magnesium concentration inhibits the effect of arginine vasopressin (AVP) on smooth muscle contraction and platelet aggregation and also influences hepatocyte AVP receptor binding. The aim of this study was to determine the role of magnesium concentration [Mg2+] in AVP-stimulated water transport in the kidney collecting duct. The effect of low and high peritubular [Mg2+] on the AVP-stimula...

Journal: :Biochemical and biophysical research communications 2004
Shanti Kalipatnapu Md Jafurulla Nandhini Chandrasekaran Amitabha Chattopadhyay

The serotonin1A (5-HT1A) receptor is an important member of the superfamily of seven transmembrane domain G-protein coupled receptors (GPCRs). We report here that guanine nucleotide sensitivity of agonist binding to hippocampal 5-HT1A receptors is dependent on the concentration of Mg2+. Our results show that agonist binding to 5-HT1A receptors is relatively insensitive to guanine nucleotides in...

Journal: :The Biochemical journal 1997
M Fukuda T Kojima K Mikoshiba

Synaptotagmins are Ca2+-and phospholipid-binding proteins of synaptic vesicles that might function as Ca2+ receptors for neurotransmitter release via their first C2 (C2A) domain. Here we describe the effect of Mg2+ on phospholipid binding to the C2A domains of multiple synaptotagmins (II-VI), and demonstrate that only synaptotagmin III can bind negatively charged phospholipids [phosphatidylseri...

Journal: :Cell 1996
Eleonora García Véscovi Fernando C Soncini Eduardo A Groisman

Ions are not traditionally thought to act as first messengers in signal transduction cascades. However, while searching for genes regulated by the PhoP/PhoQ virulence regulatory system of Salmonella typhimurium, we recovered two loci whose expression is controlled by the concentration of Mg2+. To determine whether Mg2+ is the signal modulating the whole PhoP/PhoQ system, we evaluated the gene e...

Journal: :Nucleic acids research 2003
D Rey Banatao Russ B Altman Teri E Klein

Interactions with magnesium (Mg2+) ions are essential for RNA folding and function. The locations and function of bound Mg2+ ions are difficult to characterize both experimentally and computationally. In particular, the P456 domain of the Tetrahymena thermophila group I intron, and a 58 nt 23s rRNA from Escherichia coli have been important systems for studying the role of Mg2+ binding in RNA, b...

Journal: :Magnesium research 2008
Lusliany J Rondón Yves Rayssiguier Andrzej Mazur

Complex fermentable carbohydrates, such as inulin-type fructans have been shown to improve Mg2+ absorption in the hindgut and body stores. The mechanisms for this are not well understood. The newly identified transient receptor potential melastatin 6 and 7 (TRPM6 and TRPM7) channels have been shown to function in active epithelial Mg2+ transport in the apical membrane of epithelial cells, the k...

2002
JIN ZHANG MORDECAI P. BLAUSTEIN Mordecai P. Blaustein

Zhang, Jin, W. Gil Wier, and Mordecai P. Blaustein. Mg2 blocks myogenic tone but not K -induced constriction: role for SOCs in small arteries. Am J Physiol Heart Circ Physiol 283: H2692–H2705, 2002. First published August 15, 2002; 10.1152/ajpheart.00260.2002.—The effects of Mg2 and nifedipine (Nif) on vasoconstriction and Ca2 transients were studied in intact, pressurized rat mesenteric arteri...

Journal: :The Journal of biological chemistry 1989
M A Atkinson P K Lambooy E D Korn

The actin-activated Mg2+-ATPase of myosin II from Acanthamoeba castellanii is regulated by phosphorylation of 3 serine residues at the tip of the tail of each of its two heavy chains; only dephosphorylated myosin II is active, whereas the phosphorylated and dephosphorylated forms have identical Ca2+-ATPase activities and Mg2+-ATPase activities in the absence of F-actin. We have now chemically m...

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