Results 171 to 180 of about 10,542 (222)
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A new function for CD38/ADP-ribosyl cyclase in nuclear Ca2+ homeostasis

Nature Cell Biology, 1999
Nucleoplasmic calcium ions (Ca2+) influence nuclear functions as critical as gene transcription, apoptosis, DNA repair, topoisomerase activation and polymerase unfolding. Although both inositol trisphosphate receptors and ryanodine receptors, types of Ca2+ channel, are present in the nuclear membrane, their role in the homeostasis of nuclear Ca2 ...
O. Adebanjo   +17 more
semanticscholar   +3 more sources

Crystallization of ADP‐ribosyl cyclase from Aplysia californica

Proteins: Structure, Function, and Genetics, 1996
ADP-ribosyl cyclase synthesizes the secondary messenger cyclic ADP-ribose from NAD+. Diffraction quality crystals of the enzyme from ovotestes of Aplysia californica have been obtained. Crystallographic analysis of this enzyme will yield insight into the mode of binding of the novel cyclic nucleotide and the mechanism by which NAD+ is cyclized.
Lee, HC   +3 more
openaire   +3 more sources

ADP-Ribosyl Cyclase in Rat Salivary Glands

Biochemical and Biophysical Research Communications, 2000
Both the Ca(2+)-releasing mechanism induced by cyclic ADP-ribose (cADPR) and the ADP-ribosyl cyclase (ADPRC) activity that converts NAD(+) to cADPR were observed in a variety of cell types. We studied the ADPRC activity in rat major salivary glands that include parotid gland (PG), submandiblar gland (SMG), and sublingual gland (SLG).
W, Masuda, T, Noguchi
openaire   +2 more sources

Cyclic ADP-ribose as a second messenger revisited from a new aspect of signal transduction from receptors to ADP-ribosyl cyclase.

Pharmacology and Therapeutics, 2001
H. Higashida   +7 more
semanticscholar   +3 more sources

Role of kidney ADP-ribosyl cyclase in diabetic nephropathy

American Journal of Physiology-Renal Physiology, 2009
The role of ADP-ribosyl cyclases (ADPR-cyclases) in diabetic nephropathy was investigated. ADPR-cyclases synthesize cADP-ribose (cADPR), a Ca2+-mobilizing second messenger, and are stimulated by G protein-coupled receptors. We have previously reported that ADPR-cyclases can be activated by ANG II and showed that a specific kidney ADPR-cyclase inhibitor,
Seon-Young, Kim   +4 more
openaire   +2 more sources

ADP ribosyl-cyclases (CD38/CD157), social skills and friendship

Psychoneuroendocrinology, 2017
Why some individuals seek social engagement while others shy away has profound implications for normal and pathological human behavior. Evidence suggests that oxytocin (OT), the paramount human social hormone, and CD38 that governs OT release, contribute to individual differences in social skills from intense social involvement to extreme avoidance ...
Anne Chonga   +8 more
openaire   +3 more sources

Chemo-enzymatic synthesis of NPN cofactor taking advantage of ADP-ribosyl cyclase and LarC cyclometallase promiscuous activities.

Bioorganic chemistry (Print)
The nickel-pincer nucleotide cofactor (NPN) is a widespread organometallic cofactor required for lactate racemase (LarA) and for α-hydroxy acid racemases and epimerases of the LarA superfamily.
Timothé Vucko   +4 more
semanticscholar   +1 more source

The homo-dimeric form of ADP-ribosyl cyclase in solution

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1998
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 cross-linking and dynamic light scattering were used in
Bloomfield, VA   +4 more
openaire   +4 more sources

Purification and Characterization of ADP-Ribosyl Cyclase from Euglena gracilis

Journal of Biochemistry, 1999
ADP-ribosyl cyclase, which catalyzes the conversion from NAD+ to cyclic adenosine diphosphoribose (cADPR), is proposed to participate in cell cycle regulation in Euglena gracilis. This enzyme, which was found as a membrane-bound protein, was purified almost the homogeneity after solubilization with deoxycholate, and found to be a monomeric protein with
W, Masuda   +5 more
openaire   +2 more sources

GTP stabilization of adenylate cyclase activated and ADP-ribosylated by choleragen

Biochemical and Biophysical Research Communications, 1981
Abstract Choleragen activates adenylate cyclase in human skin fibroblasts by catalyzing the ADP-ribosylation of the 42,000 and 47,000 dalton guanyl nucleotide-binding regulatory components (G) of adenylate cyclase. The ADP-ribose linkage to 42,000 and 47,000 dalton proteins was stable at 30°C for 1 h with or without GTP, whereas GTP was required to ...
S, Nakaya   +5 more
openaire   +2 more sources

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