PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10437804-0 1999 Hydrolysis of NADP+ by platelet CD38 in the absence of synthesis and degradation of cyclic ADP-ribose 2"-phosphate. NADP 14-19 CD38 molecule Homo sapiens 32-36 10437804-2 1999 In this work, we investigated the metabolism of NADP+ by CD38 expressed on human platelets. NADP 48-53 CD38 molecule Homo sapiens 57-61 9494110-9 1998 Altogether our results lead to the conclusion that CD38 is an authentic "classical" NAD(P)+ glycohydrolase (EC 3.2.2.6). NADP 84-90 CD38 molecule Homo sapiens 51-55 8530456-0 1995 ADP-ribosyl cyclase and CD38 catalyze the synthesis of a calcium-mobilizing metabolite from NADP. NADP 92-96 CD38 molecule Homo sapiens 24-28 8701086-16 1996 Both ADP-ribosyl cyclase and CD38 can catalyze the exchange of the nicotinamide group in NADP+ with nicotinic acid, leading to the formation of another Ca+2 mobilizing metabolite, nicotinic acid dinucleotide phosphate (NAADP). NADP 89-94 CD38 molecule Homo sapiens 29-33 8530456-3 1995 In this study, we show that both the cyclase and CD38 can also catalyze the exchange of the nicotinamide group of NADP+ with nicotine acid (NA). NADP 114-119 CD38 molecule Homo sapiens 49-53 8530456-10 1995 Under the same conditions, CD38 converts NADP+ to ADP-ribose 2"-phosphate instead, which is the hydrolysis product of cyclic ADP-ribose 2"-phosphate. NADP 41-46 CD38 molecule Homo sapiens 27-31 31672920-3 2019 Accordingly, for more than 20 years it has remained unresolved how CD38 can use cytosolic substrates such as NAD and NADP to produce messengers that target intracellular Ca2+-stores. NADP 117-121 CD38 molecule Homo sapiens 67-71 32717131-0 2020 Interleukin-8 drives CD38 to form NAADP from NADP+ and NAAD in the endolysosomes to mobilize Ca2+ and effect cell migration. NADP 45-50 CD38 molecule Homo sapiens 21-25 32717131-3 2020 We discovered that CD38 catalyzes synthesis of NAADP by exchanging the nicotinamide moiety of nicotinamide adenine dinucleotide phosphate (NADP+ ) for the NA group of nicotinic acid adenine dinucleotide (NAAD) inside endolysosomes of interleukin 8 (IL8)-treated lymphokine-activated killer (LAK) cells. NADP 94-137 CD38 molecule Homo sapiens 19-23 32717131-3 2020 We discovered that CD38 catalyzes synthesis of NAADP by exchanging the nicotinamide moiety of nicotinamide adenine dinucleotide phosphate (NADP+ ) for the NA group of nicotinic acid adenine dinucleotide (NAAD) inside endolysosomes of interleukin 8 (IL8)-treated lymphokine-activated killer (LAK) cells. NADP 139-144 CD38 molecule Homo sapiens 19-23 32717131-6 2020 Thus, the membrane organization of endolysosomal CD38, a signal-mediated transport system for NADP+ and luminal NAD+ biosynthetic enzymes integrate signals from a chemokine and cAMP to specify the spatiotemporal mobilization of Ca2+ to drive cell migration. NADP 94-99 CD38 molecule Homo sapiens 49-53 34896700-1 2022 CD38 is a single-pass transmembrane enzyme catalyzing the synthesis of two nucleotide second messengers, cyclic ADP-ribose (cADPR) from NAD and nicotinic acid adenine dinucleotide phosphate (NAADP) from NADP. NADP 203-207 CD38 molecule Homo sapiens 0-4 25447548-1 2015 CD38 catalyzes the synthesis of two structurally distinct messengers for Ca2+-mobilization, cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP), from cytosolic substrates, NAD and NADP, respectively. NADP 212-216 CD38 molecule Homo sapiens 0-4 29632067-3 2018 CD38 is the only enzyme known to catalyze NAADP synthesis from NADP and nicotinic acid. NADP 63-67 CD38 molecule Homo sapiens 0-4 29187364-1 2018 The NAD(P)+-hydrolyzing enzyme CD38 is activated in the heart during the process of ischemia and reperfusion, triggering NAD(P)(H) depletion. NADP 4-11 CD38 molecule Homo sapiens 31-35 29187364-9 2018 Marked NADP(H) depletion with loss of NO and increase in superoxide production occurred following hypoxia-reoxygenation that was prevented by CD38 inhibition or knockdown. NADP 7-14 CD38 molecule Homo sapiens 142-146 29187364-10 2018 Thus, endothelial cells have high expression of CD38 which is activated by hypoxia-reoxygenation triggering CD38-mediated NADP(H) depletion with loss of eNOS-mediated NO generation and increased eNOS uncoupling. NADP 122-126 CD38 molecule Homo sapiens 48-52 29187364-10 2018 Thus, endothelial cells have high expression of CD38 which is activated by hypoxia-reoxygenation triggering CD38-mediated NADP(H) depletion with loss of eNOS-mediated NO generation and increased eNOS uncoupling. NADP 122-126 CD38 molecule Homo sapiens 108-112 28108596-1 2017 We recently showed that ischemia/reperfusion (I/R) of the heart causes CD38 activation with resultant depletion of the cardiac NADP(H) pool, which is most marked in the endothelium. NADP 127-134 CD38 molecule Homo sapiens 71-75 16101292-4 2005 We show that the novel NAD(P)(+) catabolizing enzyme (NACE) expressed by schistosomes is structurally most closely related to the cyclases cloned from Aplysia but also shows significant homology with the mammalian cyclases, CD38 and CD157. NADP 23-32 CD38 molecule Homo sapiens 224-228 21641214-2 2011 It is involved in the conversion of NAD(P)(+) into cyclic ADP-ribose, NAADP(+) and ADP-ribose and the role of these metabolites in multiple Ca(2+) signaling pathways makes CD38 a novel potential pharmacological target. NADP 36-45 CD38 molecule Homo sapiens 172-176 18835239-1 2008 ADP-ribosyl cyclase and NAD+ glycohydrolase (CD38, E.C.3.2.2.5) efficiently catalyze the exchange of the nicotinamidyl moiety of NAD+, nicotinamide adenine dinucleotide phosphate (NADP+) or nicotinamide mononucleotide (NMN+) with an alternative base. NADP 135-178 CD38 molecule Homo sapiens 45-49 18835239-1 2008 ADP-ribosyl cyclase and NAD+ glycohydrolase (CD38, E.C.3.2.2.5) efficiently catalyze the exchange of the nicotinamidyl moiety of NAD+, nicotinamide adenine dinucleotide phosphate (NADP+) or nicotinamide mononucleotide (NMN+) with an alternative base. NADP 180-185 CD38 molecule Homo sapiens 45-49 22670756-0 2012 Expression of the human NAD(P)-metabolizing ectoenzyme CD38 compromises systemic acquired resistance in Arabidopsis. NADP 24-30 CD38 molecule Homo sapiens 55-59 22670756-7 2012 Using transgenic Arabidopsis plants expressing the human NAD(P)-metabolizing ectoenzyme CD38, we demonstrated that altering eNAD(P) concentration or signaling compromises biological induction of SAR. NADP 57-63 CD38 molecule Homo sapiens 88-92 18626062-2 2008 Expressed in distinct patterns in most tissues, CD38 (and CD157) cleaves NAD(+) and NADP(+), generating cyclic ADP ribose (cADPR), NAADP, and ADPR. NADP 84-91 CD38 molecule Homo sapiens 48-52