PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 10331647-3 1999 ATP, produced by glucose metabolism, competes with cADPR for the binding site, Lys-129, of CD38, resulting in the inhibition of the hydrolysis of cADPR and thereby causing cADPR accumulation in beta-cells. Adenosine Triphosphate 0-3 CD38 molecule Homo sapiens 91-95 10553576-3 1999 ATP, produced by glucose metabolism, competes with cADPR for the binding site, Lys-129, of CD38, resulting in the inhibition of the hydrolysis of cADPR and thereby causing cADPR accumulation in beta-cells. Adenosine Triphosphate 0-3 CD38 molecule Homo sapiens 91-95 9211326-0 1997 Synthesis and hydrolysis of cyclic ADP-ribose by human leukocyte antigen CD38: inhibition of hydrolysis by ATP and physiological significance. Adenosine Triphosphate 107-110 CD38 molecule Homo sapiens 73-77 9020087-0 1997 Lysine 129 of CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase) participates in the binding of ATP to inhibit the cyclic ADP-ribose hydrolase. Adenosine Triphosphate 100-103 CD38 molecule Homo sapiens 14-18 9020087-1 1997 CD38 catalyzes not only the formation of cyclic ADP-ribose (cADPR) from NAD+ but also the hydrolysis of cADPR to ADP-ribose (ADPR), and ATP inhibits the hydrolysis (Takasawa, S., Tohgo, A., Noguchi, N., Koguma, T., Nata, K., Sugimoto, T., Yonekura, H., and Okamoto, H. (1993) J. Biol. Adenosine Triphosphate 136-139 CD38 molecule Homo sapiens 0-4 9020087-4 1997 In the present study, using purified recombinant CD38, we showed that the cADPR hydrolase activity of CD38 was inhibited by ATP in a competitive manner with cADPR. Adenosine Triphosphate 124-127 CD38 molecule Homo sapiens 49-53 9020087-4 1997 In the present study, using purified recombinant CD38, we showed that the cADPR hydrolase activity of CD38 was inhibited by ATP in a competitive manner with cADPR. Adenosine Triphosphate 124-127 CD38 molecule Homo sapiens 102-106 9020087-5 1997 To identify the binding site for ATP and/or cADPR, we labeled the purified CD38 with FSBA. Adenosine Triphosphate 33-36 CD38 molecule Homo sapiens 75-79 9020087-10 1997 These results indicate that Lys-129 of CD38 participates in cADPR binding and that ATP competes with cADPR for the binding site, resulting in the inhibition of the cADPR hydrolase activity of CD38. Adenosine Triphosphate 83-86 CD38 molecule Homo sapiens 192-196 31636635-2 2019 There, high extracellular levels of nucleotides, mainly NAD+ and ATP, are catabolized by different ectonucleotidases, which can be divided in two families according to substrate specificity: on one side those that metabolize NAD+, including CD38, CD157, and CD203a; on the other, those that convert ATP, namely CD39 (and other ENTPDases) and CD73. Adenosine Triphosphate 65-68 CD38 molecule Homo sapiens 241-245 32319590-6 2020 Further experiments using an ATP test kit and lactate test kit revealed that CD38 promotes glucose consumption, increases lactate accumulation and increases ATP production. Adenosine Triphosphate 29-32 CD38 molecule Homo sapiens 77-81 32319590-6 2020 Further experiments using an ATP test kit and lactate test kit revealed that CD38 promotes glucose consumption, increases lactate accumulation and increases ATP production. Adenosine Triphosphate 157-160 CD38 molecule Homo sapiens 77-81 31636635-2 2019 There, high extracellular levels of nucleotides, mainly NAD+ and ATP, are catabolized by different ectonucleotidases, which can be divided in two families according to substrate specificity: on one side those that metabolize NAD+, including CD38, CD157, and CD203a; on the other, those that convert ATP, namely CD39 (and other ENTPDases) and CD73. Adenosine Triphosphate 299-302 CD38 molecule Homo sapiens 241-245 30535454-9 2019 Additionally, cell metabolism assays demonstrated that CD38 increased the concentration of ATP, lactic acid, cyclic adenosine monophosphate and human ADP/acrp30 concentration in NPC cells. Adenosine Triphosphate 91-94 CD38 molecule Homo sapiens 55-59 28373875-2 2017 One set of ectoenzymes-CD39, CD38, CD203a, and CD73-leads to the generation of adenosine (ADO) by metabolizing ATP and NAD+. Adenosine Triphosphate 111-114 CD38 molecule Homo sapiens 29-33 24713601-0 2014 CD38 mediates the intracellular ATP levels and cell survival of C6 glioma cells. Adenosine Triphosphate 32-35 CD38 molecule Homo sapiens 0-4 24713601-3 2014 In this study, we applied CD38 small interfering RNA (siRNA) to determine the effects of decreased CD38 on the intracellular ATP levels and survival of C6 glioma cells. Adenosine Triphosphate 125-128 CD38 molecule Homo sapiens 99-103 24713601-4 2014 Our study showed that both CD38 siRNA and 8-bromo-cADPR - a ryanodine receptor antagonist - can lead to a significant increase in the intracellular ATP levels of C6 glioma cells. Adenosine Triphosphate 148-151 CD38 molecule Homo sapiens 27-31 24713601-7 2014 In summary, our study has provided novel evidence suggesting that CD38 mediates both the intracellular ATP levels and the survival of C6 glioma cells, suggesting that CD38 may become a therapeutic target for gliomas. Adenosine Triphosphate 103-106 CD38 molecule Homo sapiens 66-70 24713601-7 2014 In summary, our study has provided novel evidence suggesting that CD38 mediates both the intracellular ATP levels and the survival of C6 glioma cells, suggesting that CD38 may become a therapeutic target for gliomas. Adenosine Triphosphate 103-106 CD38 molecule Homo sapiens 167-171 29958894-3 2019 Among the host responses to the release of ATP, NAD+ and related small molecules is their breakdown on behalf of a panel of leukocyte ectonucleotidases - CD38, CD39, CD73, CD157, CD203a and CD203c -, whose activities are concatenated to form two nucleotide-catabolizing channels defined as the canonical and non-canonical adenosinergic pathways. Adenosine Triphosphate 43-46 CD38 molecule Homo sapiens 154-158