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Showing 1-20 of 20 results for "N5131" within Papers
Mariana G Tarragó et al.
Cell metabolism, 27(5), 1081-1095 (2018-05-03)
Aging is characterized by the development of metabolic dysfunction and frailty. Recent studies show that a reduction in nicotinamide adenine dinucleotide (NAD+) is a key factor for the development of age-associated metabolic decline. We recently demonstrated that the NADase CD38
C Munshi et al.
Biochimica et biophysica acta, 1388(2), 428-436 (1998-12-22)
ADP-ribosyl cyclase is a multi-functional enzyme that catalyzes the formation of two Ca2+ signaling molecules, cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP). X-ray crystallography of three different crystal forms shows that it is a non-covalent dimer. Chemical
Measuring CD38 Hydrolase and Cyclase Activities: 1, N6-Ethenonicotinamide Adenine Dinucleotide (varepsilon-NAD) and Nicotinamide Guanine Dinucleotide (NGD) Fluorescence-based Methods
de Oliveira GC, et al.
Bio-protocol, 8(14) (2018)
Leonie Durnin et al.
The FEBS journal, 278(17), 3095-3108 (2011-07-12)
It is well established that the intracellular second messenger cADP-ribose (cADPR) activates Ca(2+) release from the sarcoplasmic reticulum through ryanodine receptors. CD38 is a multifunctional enzyme involved in the formation of cADPR in mammals. CD38 has also been reported to
Large-scale purification of Aplysia ADP-ribosylcyclase and measurement of its activity by fluorimetric assay.
H C Lee et al.
Methods in enzymology, 280, 331-340 (1997-01-01)
Decreased ADP-ribosyl cyclase activity in peripheral blood mononuclear cells from diabetic patients with nephropathy.
Ohtsuji M, Yagi K, Shintaku-Kubota M, et al.
EXS, 2008, 508-508 (2008)
ADP-ribosyl cyclase and GDP-ribosyl cyclase activities are not always equivalent: impact on the study of the physiological role of cyclic ADP-ribose.
Frances E Lund et al.
Analytical biochemistry, 346(2), 336-338 (2005-10-11)
Leanne T Breen et al.
American journal of physiology. Renal physiology, 290(2), F486-F495 (2005-09-29)
Endogenous nucleotides with extracellular functions may be involved in the complex neural control of human urinary bladder (HUB). Using HPLC techniques with fluorescence detection, we observed that in addition to ATP and its metabolites ADP, AMP and adenosine, electrical field
Lili Peng et al.
Biochimie, 93(9), 1601-1609 (2011-06-15)
The phosphodiesterases (PDEs) are a superfamily of enzymes that have multiple roles in extracellular nucleotide metabolism and in the regulation of nucleotide-based intercellular signaling. Here we describe for the first time the isolation and partial characterization of a novel phosphodiesterase
M E Migaud et al.
Biochemistry, 38(28), 9105-9114 (1999-07-22)
Readily synthesized nicotinamide adenine dinucleotide (NAD(+)) analogues have been used to investigate aspects of the cyclization of NAD(+) to cyclic adenosine 5'-O-diphosphate ribose (cADPR) catalyzed by the enzyme adenosine 5'-O-diphosphate (ADP) ribosyl cyclase and to produce the first potent inhibitors
Andrea Fabiano et al.
Visual neuroscience, 28(2), 121-128 (2011-01-29)
Cyclic ADP-ribose (cADPR) is a second messenger modulating intracellular calcium levels. We have previously described a cADPR-dependent calcium signaling pathway in bovine rod outer segments (ROS), where calcium ions play a pivotal role. ROS ADP-ribosyl cyclase (ADPR-cyclase) was localized in
M Liang et al.
Archives of biochemistry and biophysics, 371(2), 317-325 (1999-11-05)
Here we investigated whether cADPR and NAADP are synthesized in mitochondria. We found that ADPR-cyclase activity is present in mitochondria. In addition, we describe for the first time synthesis of NAADP in this intracellular organelle. ADPR-cyclase activities (V(MAX)) and NAADP
Transfer of mitochondria from astrocytes to neurons after stroke
Hayakawa K, et al.
Nature, 535(7613), 551-551 (2016)
L G Mészáros et al.
Biochemical and biophysical research communications, 234(1), 252-256 (1997-05-08)
Two types of ADP-ribosyl cyclase activity were distinguished in dog and rat cardiac muscles by measuring the enzymatic conversion of NGD (as an NAD analog) into the fluorescent product cyclic GDP-ribose in cardiac muscle subcellular fractions. Both types of activity
S L Oei et al.
FEBS letters, 397(1), 17-21 (1996-11-11)
Poly(ADP-ribosyl) transferase (pADPRT) catalyzes the transfer of the ADP-ribose moiety from NAD+ onto proteins as well as onto protein-bound ADP-ribose. As a result, protein-bound polymers of ADP-ribose are formed. pADPRT itself contains several acceptor sites for ADP-ribose polymers and may
TIR Domain Proteins Are an Ancient Family of NAD+-Consuming Enzymes
Essuman K, et al.
Current Biology, 28(3), 421-430 (2018)
Lutz Sternfeld et al.
The Journal of biological chemistry, 278(36), 33629-33636 (2003-06-17)
Cyclic ADP-ribose, a metabolite of NAD+ evokes Ca2+ release from intracellular stores in different cells. We have determined the activity of cADPr-producing enzymes (ADP-ribosyl cyclases) in different cellular fractions prepared from isolated pancreatic acinar cells by measuring the conversion of
Isabella Panfoli et al.
Investigative ophthalmology & visual science, 48(3), 978-984 (2007-02-28)
Calcium ions play a pivotal role in phototransduction. In this study, the presence and functional role of the adenosine diphosphoribosyl (ADPR)-cyclase-cyclic ADP-ribose (cADPR) system in bovine retinal rod outer segments (ROS) was investigated. A Ca(2+) release from osmotically intact ROS
L M Smyth et al.
Neuroscience, 139(4), 1467-1477 (2006-04-04)
Using high performance liquid chromatography fraction analysis we have recently established that numerous smooth muscle preparations, including the canine mesenteric artery and vein, release beta-nicotinamide adenine dinucleotide upon short-pulse electrical field stimulation in tetrodotoxin- and omega-conotoxin GVIA-sensitive manners [ Release
Claire Ceni et al.
The Biochemical journal, 395(2), 417-426 (2006-01-18)
cADPR (cADP-ribose), a metabolite of NAD+, is known to modulate intracellular calcium levels and to be involved in calcium-dependent processes, including synaptic transmission, plasticity and neuronal excitability. However, the enzyme that is responsible for producing cADPR in the cytoplasm of
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