PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
11853741-1	2002	The aim of the present work was to examine the relationship between proline metabolism and NAD kinase activity in greenbeans submitted to cold-shock.	Proline	68-75	NAD kinase	Homo sapiens	91-101
11853741-4	2002	Also, we found a close relationship between the Ca(2+)-CaM-dependent NAD kinase activity and proline metabolism, suggesting that the adaptive responses or acclimation of plants to cold stress are preceded by increased [Ca(2+)](cyt).	Proline	93-100	NAD kinase	Homo sapiens	69-79
34629356-2	2021	Nicotinamide adenine dinucleotide kinase (NAD kinase) catalyzes the phosphorylation of NAD+ to NADP+ in the presence of ATP (ATP-NAD kinase).	NAD	87-91	NAD kinase	Homo sapiens	0-40
8135539-2	1994	At first and in the unique but obligatory presence of NAD, the NAD kinase acts almost instantaneously as an oxido-reductase (probably coupled with the transformation of NAD to NADH).	NAD	54-57	NAD kinase	Homo sapiens	63-73
8135539-2	1994	At first and in the unique but obligatory presence of NAD, the NAD kinase acts almost instantaneously as an oxido-reductase (probably coupled with the transformation of NAD to NADH).	NAD	176-180	NAD kinase	Homo sapiens	63-73
8135539-4	1994	Final assays testing for the specificity of the phosphoryl donor revealed that not only ATP but also GTP, G6P, and even NADP could be the substrate; the efficiencies of these phosphoryl donors varied with the different isoforms of NAD kinase, evidenced in the different seeds tested, and compared with NAD kinase from heterotropically grown Euglena cells, and NAD kinase purified from chicken liver (from Sigma Chemical Co.).	NADP	120-124	NAD kinase	Homo sapiens	231-241
8135539-4	1994	Final assays testing for the specificity of the phosphoryl donor revealed that not only ATP but also GTP, G6P, and even NADP could be the substrate; the efficiencies of these phosphoryl donors varied with the different isoforms of NAD kinase, evidenced in the different seeds tested, and compared with NAD kinase from heterotropically grown Euglena cells, and NAD kinase purified from chicken liver (from Sigma Chemical Co.).	NADP	120-124	NAD kinase	Homo sapiens	302-312
8135539-4	1994	Final assays testing for the specificity of the phosphoryl donor revealed that not only ATP but also GTP, G6P, and even NADP could be the substrate; the efficiencies of these phosphoryl donors varied with the different isoforms of NAD kinase, evidenced in the different seeds tested, and compared with NAD kinase from heterotropically grown Euglena cells, and NAD kinase purified from chicken liver (from Sigma Chemical Co.).	NADP	120-124	NAD kinase	Homo sapiens	302-312
1337352-0	1992	A continuous spectrophotometric assay for the activation of plant NAD kinase by calmodulin, calcium(II), and europium(III) ions.	Calcium	92-99	NAD kinase	Homo sapiens	66-76
1337352-1	1992	A continuous spectrophotometric assay has been developed to quantify the calmodulin, calcium(II) ion, and europium(III) ion dependence of the activation of NAD kinase from pea seedlings.	Calcium	85-96	NAD kinase	Homo sapiens	156-166
1337352-3	1992	These results indicate that the binding of three calcium(II) ions is necessary for activation of plant NAD kinase.	Calcium	49-60	NAD kinase	Homo sapiens	103-113
2154300-4	1990	The calcium increase is responsible for the NADP change (via NAD kinase) and possibly the change in G6PD.	Calcium	4-11	NAD kinase	Homo sapiens	61-71
2154300-4	1990	The calcium increase is responsible for the NADP change (via NAD kinase) and possibly the change in G6PD.	NADP	44-48	NAD kinase	Homo sapiens	61-71
10333484-4	1999	Domain exchange mutants in which EF hand III or IV was replaced by EF hand I or II respectively (CaM1214 and CaM1232 respectively) showed a modest effect on PDE and NADK activation (50 to 100% of wild-type), but calmodulin methylation was abolished.	cam1214	97-104	NAD kinase	Homo sapiens	165-169
10333484-4	1999	Domain exchange mutants in which EF hand III or IV was replaced by EF hand I or II respectively (CaM1214 and CaM1232 respectively) showed a modest effect on PDE and NADK activation (50 to 100% of wild-type), but calmodulin methylation was abolished.	cam1232	109-116	NAD kinase	Homo sapiens	165-169
34133937-4	2021	However, de novo NADP+ is synthesized only through one known enzymatic reaction, catalyzed by NAD+ kinase (NADK).	NADP	17-22	NAD kinase	Homo sapiens	94-105
34133937-4	2021	However, de novo NADP+ is synthesized only through one known enzymatic reaction, catalyzed by NAD+ kinase (NADK).	NADP	17-22	NAD kinase	Homo sapiens	107-111
34133937-5	2021	In this study, we show that oncogenic KRAS promotes protein kinase C (PKC)-mediated NADK phosphorylation, leading to its hyperactivation, thus sustaining both NADP+ and NADPH levels in PDAC cells.	NADP	159-164	NAD kinase	Homo sapiens	84-88
34629356-7	2021	These pioneering findings, i.e., ATP/poly(P)-NAD kinase, NAD kinase gene, and human mitochondrial NAD kinase, have significantly enhanced research on the biochemistry, molecular biology, and evolutionary biology of NAD kinase, mitochondria, and poly(P), including some biotechnological knowledge applicable to NADP+ production.	NADP	310-315	NAD kinase	Homo sapiens	215-225
34629356-2	2021	Nicotinamide adenine dinucleotide kinase (NAD kinase) catalyzes the phosphorylation of NAD+ to NADP+ in the presence of ATP (ATP-NAD kinase).	NAD	87-91	NAD kinase	Homo sapiens	42-52
34629356-2	2021	Nicotinamide adenine dinucleotide kinase (NAD kinase) catalyzes the phosphorylation of NAD+ to NADP+ in the presence of ATP (ATP-NAD kinase).	NADP	95-100	NAD kinase	Homo sapiens	0-40
34629356-2	2021	Nicotinamide adenine dinucleotide kinase (NAD kinase) catalyzes the phosphorylation of NAD+ to NADP+ in the presence of ATP (ATP-NAD kinase).	NADP	95-100	NAD kinase	Homo sapiens	42-52
34629356-2	2021	Nicotinamide adenine dinucleotide kinase (NAD kinase) catalyzes the phosphorylation of NAD+ to NADP+ in the presence of ATP (ATP-NAD kinase).	Adenosine Triphosphate	120-123	NAD kinase	Homo sapiens	0-40
34629356-2	2021	Nicotinamide adenine dinucleotide kinase (NAD kinase) catalyzes the phosphorylation of NAD+ to NADP+ in the presence of ATP (ATP-NAD kinase).	Adenosine Triphosphate	120-123	NAD kinase	Homo sapiens	42-52
34629356-3	2021	Novel NAD kinase that explicitly phosphorylates NAD+ to NADP+ using poly(P), besides ATP (ATP/poly(P)-NAD kinase), was found in bacteria, in particular, Gram-positive bacteria, and the gene encoding ATP/poly(P)-NAD kinase was also newly identified in Mycobacterium tuberculosis H37Rv.	NAD	48-52	NAD kinase	Homo sapiens	6-16
34629356-3	2021	Novel NAD kinase that explicitly phosphorylates NAD+ to NADP+ using poly(P), besides ATP (ATP/poly(P)-NAD kinase), was found in bacteria, in particular, Gram-positive bacteria, and the gene encoding ATP/poly(P)-NAD kinase was also newly identified in Mycobacterium tuberculosis H37Rv.	NAD	48-52	NAD kinase	Homo sapiens	102-112
34629356-3	2021	Novel NAD kinase that explicitly phosphorylates NAD+ to NADP+ using poly(P), besides ATP (ATP/poly(P)-NAD kinase), was found in bacteria, in particular, Gram-positive bacteria, and the gene encoding ATP/poly(P)-NAD kinase was also newly identified in Mycobacterium tuberculosis H37Rv.	NADP	56-61	NAD kinase	Homo sapiens	6-16
34629356-3	2021	Novel NAD kinase that explicitly phosphorylates NAD+ to NADP+ using poly(P), besides ATP (ATP/poly(P)-NAD kinase), was found in bacteria, in particular, Gram-positive bacteria, and the gene encoding ATP/poly(P)-NAD kinase was also newly identified in Mycobacterium tuberculosis H37Rv.	NADP	56-61	NAD kinase	Homo sapiens	102-112
34629356-3	2021	Novel NAD kinase that explicitly phosphorylates NAD+ to NADP+ using poly(P), besides ATP (ATP/poly(P)-NAD kinase), was found in bacteria, in particular, Gram-positive bacteria, and the gene encoding ATP/poly(P)-NAD kinase was also newly identified in Mycobacterium tuberculosis H37Rv.	Adenosine Triphosphate	85-88	NAD kinase	Homo sapiens	6-16
34629356-3	2021	Novel NAD kinase that explicitly phosphorylates NAD+ to NADP+ using poly(P), besides ATP (ATP/poly(P)-NAD kinase), was found in bacteria, in particular, Gram-positive bacteria, and the gene encoding ATP/poly(P)-NAD kinase was also newly identified in Mycobacterium tuberculosis H37Rv.	Adenosine Triphosphate	85-88	NAD kinase	Homo sapiens	102-112
34629356-3	2021	Novel NAD kinase that explicitly phosphorylates NAD+ to NADP+ using poly(P), besides ATP (ATP/poly(P)-NAD kinase), was found in bacteria, in particular, Gram-positive bacteria, and the gene encoding ATP/poly(P)-NAD kinase was also newly identified in Mycobacterium tuberculosis H37Rv.	Adenosine Triphosphate	199-202	NAD kinase	Homo sapiens	6-16
34629356-3	2021	Novel NAD kinase that explicitly phosphorylates NAD+ to NADP+ using poly(P), besides ATP (ATP/poly(P)-NAD kinase), was found in bacteria, in particular, Gram-positive bacteria, and the gene encoding ATP/poly(P)-NAD kinase was also newly identified in Mycobacterium tuberculosis H37Rv.	Adenosine Triphosphate	199-202	NAD kinase	Homo sapiens	102-112
34629356-7	2021	These pioneering findings, i.e., ATP/poly(P)-NAD kinase, NAD kinase gene, and human mitochondrial NAD kinase, have significantly enhanced research on the biochemistry, molecular biology, and evolutionary biology of NAD kinase, mitochondria, and poly(P), including some biotechnological knowledge applicable to NADP+ production.	NADP	310-315	NAD kinase	Homo sapiens	33-55
34629356-7	2021	These pioneering findings, i.e., ATP/poly(P)-NAD kinase, NAD kinase gene, and human mitochondrial NAD kinase, have significantly enhanced research on the biochemistry, molecular biology, and evolutionary biology of NAD kinase, mitochondria, and poly(P), including some biotechnological knowledge applicable to NADP+ production.	NADP	310-315	NAD kinase	Homo sapiens	57-67
3007484-9	1986	In parallel experiments using the same agents on each enzyme, NAD kinase was the only enzyme of the three that was not activated by oleic acid and several other lipids or by limited trypsin digestion.	Oleic Acid	132-142	NAD kinase	Homo sapiens	62-72
6263156-0	1980	Calmodulin-activated plant microsomal Ca2+ uptake and purification of plant NAD kinase and other proteins by calmodulin-Sepharose chromatography.	Sepharose	120-129	NAD kinase	Homo sapiens	76-86
2982330-1	1985	NAD kinase from human neutrophils has been partially purified by sequential application of Red Agarose, ion-exchange, and gel-filtration chromatography.	Sepharose	95-102	NAD kinase	Homo sapiens	0-10
2982330-3	1985	NAD kinase activity is extremely sensitive to free calcium concentration, with half-maximal activity observed at free calcium concentrations of approximately 0.4 microM.	Calcium	51-58	NAD kinase	Homo sapiens	0-10
2982330-3	1985	NAD kinase activity is extremely sensitive to free calcium concentration, with half-maximal activity observed at free calcium concentrations of approximately 0.4 microM.	Calcium	118-125	NAD kinase	Homo sapiens	0-10
2982330-4	1985	In cellular extracts calcium-dependent activation of NAD kinase increases the maximum velocity of the reaction from 2- to 5-fold while not affecting Km values for NAD and ATP.	Calcium	21-28	NAD kinase	Homo sapiens	53-63
2982330-5	1985	The activity of the partially purified NAD kinase is stimulated 3.5-fold by the addition of calmodulin in the presence of calcium.	Calcium	122-129	NAD kinase	Homo sapiens	39-49
6309257-3	1983	The electrophoretically homogeneous preparations of NAD-kinase demonstrate a hyperbolic dependence of the NADP synthesis rate on substrate concentration and a loss of dependence of specific activity on the enzyme concentration.	NADP	106-110	NAD kinase	Homo sapiens	52-62
16659381-0	1975	Photoactivation of NAD Kinase through Phytochrome: Phosphate Donors and Cofactors.	Phosphates	51-60	NAD kinase	Homo sapiens	19-29
192196-1	1977	Pigeon liver NAD kinase was covalently coupled to the inside surfaces of nylon tubes, both directly to the nylon and via polyamine specers Km values and the inactivation energy of the reaction changed upon immobilization, but the pH-dependence remained unaltered.	Nylons	73-78	NAD kinase	Homo sapiens	13-23
192196-1	1977	Pigeon liver NAD kinase was covalently coupled to the inside surfaces of nylon tubes, both directly to the nylon and via polyamine specers Km values and the inactivation energy of the reaction changed upon immobilization, but the pH-dependence remained unaltered.	Nylons	107-112	NAD kinase	Homo sapiens	13-23
192196-1	1977	Pigeon liver NAD kinase was covalently coupled to the inside surfaces of nylon tubes, both directly to the nylon and via polyamine specers Km values and the inactivation energy of the reaction changed upon immobilization, but the pH-dependence remained unaltered.	Polyamines	121-130	NAD kinase	Homo sapiens	13-23
16659381-4	1975	Under red light, striking photoactivation of NAD kinase was obtained with ATP and subsequently CTP.In the presence of exogenous Mg(2+), which is required for NAD kinase activity, alpha-nitroso-beta-naphthol, cyanide, and dimethylglyoxime, strongly inhibited the activation by red light without affecting the level of NAD kinase in the dark.Of the divalent cations tested with the KCN-treated phytochrome preparation, only Co(2+) was effective for photoactivation of NAD kinase.	dimethylglyoxime	221-237	NAD kinase	Homo sapiens	45-55
16659381-4	1975	Under red light, striking photoactivation of NAD kinase was obtained with ATP and subsequently CTP.In the presence of exogenous Mg(2+), which is required for NAD kinase activity, alpha-nitroso-beta-naphthol, cyanide, and dimethylglyoxime, strongly inhibited the activation by red light without affecting the level of NAD kinase in the dark.Of the divalent cations tested with the KCN-treated phytochrome preparation, only Co(2+) was effective for photoactivation of NAD kinase.	Adenosine Triphosphate	74-77	NAD kinase	Homo sapiens	45-55
16659381-4	1975	Under red light, striking photoactivation of NAD kinase was obtained with ATP and subsequently CTP.In the presence of exogenous Mg(2+), which is required for NAD kinase activity, alpha-nitroso-beta-naphthol, cyanide, and dimethylglyoxime, strongly inhibited the activation by red light without affecting the level of NAD kinase in the dark.Of the divalent cations tested with the KCN-treated phytochrome preparation, only Co(2+) was effective for photoactivation of NAD kinase.	Cytidine Triphosphate	95-98	NAD kinase	Homo sapiens	45-55
16659381-4	1975	Under red light, striking photoactivation of NAD kinase was obtained with ATP and subsequently CTP.In the presence of exogenous Mg(2+), which is required for NAD kinase activity, alpha-nitroso-beta-naphthol, cyanide, and dimethylglyoxime, strongly inhibited the activation by red light without affecting the level of NAD kinase in the dark.Of the divalent cations tested with the KCN-treated phytochrome preparation, only Co(2+) was effective for photoactivation of NAD kinase.	Potassium Cyanide	380-383	NAD kinase	Homo sapiens	45-55
16659381-4	1975	Under red light, striking photoactivation of NAD kinase was obtained with ATP and subsequently CTP.In the presence of exogenous Mg(2+), which is required for NAD kinase activity, alpha-nitroso-beta-naphthol, cyanide, and dimethylglyoxime, strongly inhibited the activation by red light without affecting the level of NAD kinase in the dark.Of the divalent cations tested with the KCN-treated phytochrome preparation, only Co(2+) was effective for photoactivation of NAD kinase.	Cyanides	208-215	NAD kinase	Homo sapiens	45-55
16659381-4	1975	Under red light, striking photoactivation of NAD kinase was obtained with ATP and subsequently CTP.In the presence of exogenous Mg(2+), which is required for NAD kinase activity, alpha-nitroso-beta-naphthol, cyanide, and dimethylglyoxime, strongly inhibited the activation by red light without affecting the level of NAD kinase in the dark.Of the divalent cations tested with the KCN-treated phytochrome preparation, only Co(2+) was effective for photoactivation of NAD kinase.	Cobalt(2+)	422-428	NAD kinase	Homo sapiens	45-55
237854-8	1975	The results indicate that NAD-+-kinase activity may play a significant part in the control of pentose-shunt oxidation in thyroid follicle cells.	Pentoses	94-101	NAD kinase	Homo sapiens	26-38
16659381-5	1975	Even when Mg(2+), an essential component of NAD kinase, was added to the assay system, the further addition of Co(2+) was required for the activation of NAD kinase by Pfr.	magnesium ion	10-16	NAD kinase	Homo sapiens	44-54
16659381-5	1975	Even when Mg(2+), an essential component of NAD kinase, was added to the assay system, the further addition of Co(2+) was required for the activation of NAD kinase by Pfr.	magnesium ion	10-16	NAD kinase	Homo sapiens	153-163
16659381-5	1975	Even when Mg(2+), an essential component of NAD kinase, was added to the assay system, the further addition of Co(2+) was required for the activation of NAD kinase by Pfr.	Cobalt(2+)	111-117	NAD kinase	Homo sapiens	44-54
16659381-5	1975	Even when Mg(2+), an essential component of NAD kinase, was added to the assay system, the further addition of Co(2+) was required for the activation of NAD kinase by Pfr.	Cobalt(2+)	111-117	NAD kinase	Homo sapiens	153-163
239-2	1975	NAD kinase was purified from pigeon liver by an improved procedure which included chromatography on phosphocellulose.	phosphocellulose	100-116	NAD kinase	Homo sapiens	0-10
239-6	1975	The significance of the kinetics and of the type of inhibition produced by NADPH is discussed in terms of the regulation of NAD kinase activity in vivo.	NADP	75-80	NAD kinase	Homo sapiens	124-134
164088-5	1975	Adenylate kinase and NAD" kinase show no activity when ATP is replaced by the nucleotide-triphosphate-analogue.	Adenosine Triphosphate	55-58	NAD kinase	Homo sapiens	21-32
164088-5	1975	Adenylate kinase and NAD" kinase show no activity when ATP is replaced by the nucleotide-triphosphate-analogue.	nucleotide-triphosphate	78-101	NAD kinase	Homo sapiens	21-32
4664937-4	1972	It is shown that if the residual errors are weighted by a procedure described elsewhere (Ottaway, 1971b, 1973), the percentage error of the computed velocity is distributed evenly over a plot which contains a 100-fold variation in the concentration of one substrate and a 500-fold variation in the concentration of Mg(2+), and in which the velocity of the reaction (that catalysed by NAD kinase) varies over a 60-fold range.	Magnesium	315-317	NAD kinase	Homo sapiens	384-394
4340475-0	1972	Kinetic studies of the interaction of pigeon-liver NAD kinase with adenine nucleotides and divalent cations.	Adenine Nucleotides	67-86	NAD kinase	Homo sapiens	51-61
33011272-1	2020	NAD kinase (NADK) is required for the de novo synthesis of NADP+ from NAD+.	NADP	59-64	NAD kinase	Homo sapiens	0-10
33321420-4	2021	We have employed recombinant human NAD kinase expressed in E. coli as an enzymatic reagent to convert readily available synthetic NAD derivatives to NADP analogs, which were subsequently transformed into NAADP derivatives using enzyme catalyzed pyridine base exchange.	NADP	149-153	NAD kinase	Homo sapiens	35-45
33321420-4	2021	We have employed recombinant human NAD kinase expressed in E. coli as an enzymatic reagent to convert readily available synthetic NAD derivatives to NADP analogs, which were subsequently transformed into NAADP derivatives using enzyme catalyzed pyridine base exchange.	NAADP	204-209	NAD kinase	Homo sapiens	35-45
33321420-4	2021	We have employed recombinant human NAD kinase expressed in E. coli as an enzymatic reagent to convert readily available synthetic NAD derivatives to NADP analogs, which were subsequently transformed into NAADP derivatives using enzyme catalyzed pyridine base exchange.	pyridine	245-253	NAD kinase	Homo sapiens	35-45
33011272-1	2020	NAD kinase (NADK) is required for the de novo synthesis of NADP+ from NAD+.	NADP	59-64	NAD kinase	Homo sapiens	12-16
33011272-1	2020	NAD kinase (NADK) is required for the de novo synthesis of NADP+ from NAD+.	NAD	70-74	NAD kinase	Homo sapiens	0-10
33011272-1	2020	NAD kinase (NADK) is required for the de novo synthesis of NADP+ from NAD+.	NAD	70-74	NAD kinase	Homo sapiens	12-16
33011272-6	2020	This was mirrored by a rapid reduction in NAD+ levels, suggesting that NADK had been activated.	NAD	42-46	NAD kinase	Homo sapiens	71-75
33011272-11	2020	Activation of NADK by PKC in phagocytic cells could be critical for the rapid provision of sufficient levels of superoxide for host defence against invading microorganisms.	Superoxides	112-122	NAD kinase	Homo sapiens	14-18
30846598-0	2019	Direct stimulation of NADP+ synthesis through Akt-mediated phosphorylation of NAD kinase.	NADP	22-27	NAD kinase	Homo sapiens	78-88
31275331-3	2019	NADK is a key enzyme for NADP (including NADP+ and NADPH) biosynthesis by phosphorylating NAD (including NAD+ and NADH) and therefore, maintains the balance between NAD pool and NADP pool through an allosteric regulation mode.	NADP	25-29	NAD kinase	Homo sapiens	0-4
31275331-3	2019	NADK is a key enzyme for NADP (including NADP+ and NADPH) biosynthesis by phosphorylating NAD (including NAD+ and NADH) and therefore, maintains the balance between NAD pool and NADP pool through an allosteric regulation mode.	NADP	41-46	NAD kinase	Homo sapiens	0-4
31275331-3	2019	NADK is a key enzyme for NADP (including NADP+ and NADPH) biosynthesis by phosphorylating NAD (including NAD+ and NADH) and therefore, maintains the balance between NAD pool and NADP pool through an allosteric regulation mode.	NADP	51-56	NAD kinase	Homo sapiens	0-4
31275331-3	2019	NADK is a key enzyme for NADP (including NADP+ and NADPH) biosynthesis by phosphorylating NAD (including NAD+ and NADH) and therefore, maintains the balance between NAD pool and NADP pool through an allosteric regulation mode.	NAD	105-109	NAD kinase	Homo sapiens	0-4
31275331-3	2019	NADK is a key enzyme for NADP (including NADP+ and NADPH) biosynthesis by phosphorylating NAD (including NAD+ and NADH) and therefore, maintains the balance between NAD pool and NADP pool through an allosteric regulation mode.	NAD	114-118	NAD kinase	Homo sapiens	0-4
31275331-3	2019	NADK is a key enzyme for NADP (including NADP+ and NADPH) biosynthesis by phosphorylating NAD (including NAD+ and NADH) and therefore, maintains the balance between NAD pool and NADP pool through an allosteric regulation mode.	NAD	25-28	NAD kinase	Homo sapiens	0-4
31275331-3	2019	NADK is a key enzyme for NADP (including NADP+ and NADPH) biosynthesis by phosphorylating NAD (including NAD+ and NADH) and therefore, maintains the balance between NAD pool and NADP pool through an allosteric regulation mode.	NADP	41-45	NAD kinase	Homo sapiens	0-4
31275331-4	2019	In addition, the two respective derivatives from NAD+ (substrate of NADK) and NADP+ (product of NADK), cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP), have been considered to be the important messengers for intracellular Ca2+ homeostasis which could finally influence the combination between CaM and NADK, forming a feedback regulation mechanism.	NAD	49-53	NAD kinase	Homo sapiens	68-72
31275331-4	2019	In addition, the two respective derivatives from NAD+ (substrate of NADK) and NADP+ (product of NADK), cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP), have been considered to be the important messengers for intracellular Ca2+ homeostasis which could finally influence the combination between CaM and NADK, forming a feedback regulation mechanism.	NAD	49-53	NAD kinase	Homo sapiens	96-100
31275331-4	2019	In addition, the two respective derivatives from NAD+ (substrate of NADK) and NADP+ (product of NADK), cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP), have been considered to be the important messengers for intracellular Ca2+ homeostasis which could finally influence the combination between CaM and NADK, forming a feedback regulation mechanism.	NAD	49-53	NAD kinase	Homo sapiens	96-100
31275331-4	2019	In addition, the two respective derivatives from NAD+ (substrate of NADK) and NADP+ (product of NADK), cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP), have been considered to be the important messengers for intracellular Ca2+ homeostasis which could finally influence the combination between CaM and NADK, forming a feedback regulation mechanism.	NADP	78-83	NAD kinase	Homo sapiens	96-100
31275331-4	2019	In addition, the two respective derivatives from NAD+ (substrate of NADK) and NADP+ (product of NADK), cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP), have been considered to be the important messengers for intracellular Ca2+ homeostasis which could finally influence the combination between CaM and NADK, forming a feedback regulation mechanism.	NADP	78-83	NAD kinase	Homo sapiens	96-100
31275331-4	2019	In addition, the two respective derivatives from NAD+ (substrate of NADK) and NADP+ (product of NADK), cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP), have been considered to be the important messengers for intracellular Ca2+ homeostasis which could finally influence the combination between CaM and NADK, forming a feedback regulation mechanism.	Cyclic ADP-Ribose	103-120	NAD kinase	Homo sapiens	68-72
31275331-4	2019	In addition, the two respective derivatives from NAD+ (substrate of NADK) and NADP+ (product of NADK), cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP), have been considered to be the important messengers for intracellular Ca2+ homeostasis which could finally influence the combination between CaM and NADK, forming a feedback regulation mechanism.	NAADP	133-178	NAD kinase	Homo sapiens	68-72
31275331-4	2019	In addition, the two respective derivatives from NAD+ (substrate of NADK) and NADP+ (product of NADK), cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP), have been considered to be the important messengers for intracellular Ca2+ homeostasis which could finally influence the combination between CaM and NADK, forming a feedback regulation mechanism.	NAADP	133-178	NAD kinase	Homo sapiens	96-100
31275331-4	2019	In addition, the two respective derivatives from NAD+ (substrate of NADK) and NADP+ (product of NADK), cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP), have been considered to be the important messengers for intracellular Ca2+ homeostasis which could finally influence the combination between CaM and NADK, forming a feedback regulation mechanism.	NAADP	133-178	NAD kinase	Homo sapiens	96-100
33654713-3	2020	Conventional in vitro NAD kinase assay has been useful to evaluate enzyme activity; however, recent reports revealed a dynamics of NADP pool (the sum of NADP+ and NADPH) under fluctuating light condition, indicating that the rate of NADP synthesis is not always determined by NAD kinase activity.	NADP	131-135	NAD kinase	Homo sapiens	22-32
33654713-3	2020	Conventional in vitro NAD kinase assay has been useful to evaluate enzyme activity; however, recent reports revealed a dynamics of NADP pool (the sum of NADP+ and NADPH) under fluctuating light condition, indicating that the rate of NADP synthesis is not always determined by NAD kinase activity.	NADP	131-135	NAD kinase	Homo sapiens	276-286
33654713-4	2020	Here, we developed a novel method for the estimation of chloroplastic NAD kinase activity by quantifying the changes in the NADP amounts in response to illumination.	NADP	124-128	NAD kinase	Homo sapiens	70-80
30846598-3	2019	Akt phosphorylates NAD kinase (NADK), the sole cytosolic enzyme that catalyzes the synthesis of NADP+ from NAD+ (the oxidized form of NADH), on three serine residues (Ser44, Ser46, and Ser48) within an amino-terminal domain.	NADP	96-101	NAD kinase	Homo sapiens	19-29
30846598-3	2019	Akt phosphorylates NAD kinase (NADK), the sole cytosolic enzyme that catalyzes the synthesis of NADP+ from NAD+ (the oxidized form of NADH), on three serine residues (Ser44, Ser46, and Ser48) within an amino-terminal domain.	NADP	96-101	NAD kinase	Homo sapiens	31-35
30846598-3	2019	Akt phosphorylates NAD kinase (NADK), the sole cytosolic enzyme that catalyzes the synthesis of NADP+ from NAD+ (the oxidized form of NADH), on three serine residues (Ser44, Ser46, and Ser48) within an amino-terminal domain.	NAD	107-111	NAD kinase	Homo sapiens	19-29
30846598-3	2019	Akt phosphorylates NAD kinase (NADK), the sole cytosolic enzyme that catalyzes the synthesis of NADP+ from NAD+ (the oxidized form of NADH), on three serine residues (Ser44, Ser46, and Ser48) within an amino-terminal domain.	NAD	107-111	NAD kinase	Homo sapiens	31-35
30846598-3	2019	Akt phosphorylates NAD kinase (NADK), the sole cytosolic enzyme that catalyzes the synthesis of NADP+ from NAD+ (the oxidized form of NADH), on three serine residues (Ser44, Ser46, and Ser48) within an amino-terminal domain.	NAD	134-138	NAD kinase	Homo sapiens	19-29
30846598-3	2019	Akt phosphorylates NAD kinase (NADK), the sole cytosolic enzyme that catalyzes the synthesis of NADP+ from NAD+ (the oxidized form of NADH), on three serine residues (Ser44, Ser46, and Ser48) within an amino-terminal domain.	NAD	134-138	NAD kinase	Homo sapiens	31-35
30846598-3	2019	Akt phosphorylates NAD kinase (NADK), the sole cytosolic enzyme that catalyzes the synthesis of NADP+ from NAD+ (the oxidized form of NADH), on three serine residues (Ser44, Ser46, and Ser48) within an amino-terminal domain.	Serine	150-156	NAD kinase	Homo sapiens	19-29
30846598-3	2019	Akt phosphorylates NAD kinase (NADK), the sole cytosolic enzyme that catalyzes the synthesis of NADP+ from NAD+ (the oxidized form of NADH), on three serine residues (Ser44, Ser46, and Ser48) within an amino-terminal domain.	Serine	150-156	NAD kinase	Homo sapiens	31-35
30846598-4	2019	This phosphorylation stimulates NADK activity both in cells and directly in vitro, thereby increasing NADP+ production.	NADP	102-107	NAD kinase	Homo sapiens	32-36
30846598-6	2019	These data indicate that Akt-mediated phosphorylation of NADK stimulates its activity to increase NADP+ production through relief of an autoinhibitory function inherent to its amino terminus.	NADP	98-103	NAD kinase	Homo sapiens	57-61
26219913-1	2015	NAD(+) kinase (NADK) is the only known cytosolic enzyme that converts NAD(+) to NADP(+), which is subsequently reduced to NADPH.	NAD	0-6	NAD kinase	Homo sapiens	15-19
27582489-1	2016	NAD+ kinase (NADK) catalyzes the phosphorylation of nicotinamide adenine dinucleotide (NAD+) to nicotinamide adenine dinucleotide phosphate (NADP+) using ATP as the phosphate donor.	NAD	52-85	NAD kinase	Homo sapiens	0-11
27582489-1	2016	NAD+ kinase (NADK) catalyzes the phosphorylation of nicotinamide adenine dinucleotide (NAD+) to nicotinamide adenine dinucleotide phosphate (NADP+) using ATP as the phosphate donor.	NAD	52-85	NAD kinase	Homo sapiens	13-17
27582489-1	2016	NAD+ kinase (NADK) catalyzes the phosphorylation of nicotinamide adenine dinucleotide (NAD+) to nicotinamide adenine dinucleotide phosphate (NADP+) using ATP as the phosphate donor.	NAD	52-85	NAD kinase	Homo sapiens	0-3
27582489-1	2016	NAD+ kinase (NADK) catalyzes the phosphorylation of nicotinamide adenine dinucleotide (NAD+) to nicotinamide adenine dinucleotide phosphate (NADP+) using ATP as the phosphate donor.	NADP	96-139	NAD kinase	Homo sapiens	0-11
27582489-1	2016	NAD+ kinase (NADK) catalyzes the phosphorylation of nicotinamide adenine dinucleotide (NAD+) to nicotinamide adenine dinucleotide phosphate (NADP+) using ATP as the phosphate donor.	NADP	96-139	NAD kinase	Homo sapiens	13-17
27582489-1	2016	NAD+ kinase (NADK) catalyzes the phosphorylation of nicotinamide adenine dinucleotide (NAD+) to nicotinamide adenine dinucleotide phosphate (NADP+) using ATP as the phosphate donor.	NADP	96-139	NAD kinase	Homo sapiens	0-3
27582489-1	2016	NAD+ kinase (NADK) catalyzes the phosphorylation of nicotinamide adenine dinucleotide (NAD+) to nicotinamide adenine dinucleotide phosphate (NADP+) using ATP as the phosphate donor.	NADP	141-146	NAD kinase	Homo sapiens	0-11
27582489-1	2016	NAD+ kinase (NADK) catalyzes the phosphorylation of nicotinamide adenine dinucleotide (NAD+) to nicotinamide adenine dinucleotide phosphate (NADP+) using ATP as the phosphate donor.	NADP	141-146	NAD kinase	Homo sapiens	13-17
27582489-1	2016	NAD+ kinase (NADK) catalyzes the phosphorylation of nicotinamide adenine dinucleotide (NAD+) to nicotinamide adenine dinucleotide phosphate (NADP+) using ATP as the phosphate donor.	NADP	141-146	NAD kinase	Homo sapiens	0-3
27582489-1	2016	NAD+ kinase (NADK) catalyzes the phosphorylation of nicotinamide adenine dinucleotide (NAD+) to nicotinamide adenine dinucleotide phosphate (NADP+) using ATP as the phosphate donor.	Adenosine Triphosphate	154-157	NAD kinase	Homo sapiens	0-11
27582489-1	2016	NAD+ kinase (NADK) catalyzes the phosphorylation of nicotinamide adenine dinucleotide (NAD+) to nicotinamide adenine dinucleotide phosphate (NADP+) using ATP as the phosphate donor.	Adenosine Triphosphate	154-157	NAD kinase	Homo sapiens	13-17
27582489-1	2016	NAD+ kinase (NADK) catalyzes the phosphorylation of nicotinamide adenine dinucleotide (NAD+) to nicotinamide adenine dinucleotide phosphate (NADP+) using ATP as the phosphate donor.	Adenosine Triphosphate	154-157	NAD kinase	Homo sapiens	0-3
27582489-1	2016	NAD+ kinase (NADK) catalyzes the phosphorylation of nicotinamide adenine dinucleotide (NAD+) to nicotinamide adenine dinucleotide phosphate (NADP+) using ATP as the phosphate donor.	Phosphates	130-139	NAD kinase	Homo sapiens	0-11
27582489-1	2016	NAD+ kinase (NADK) catalyzes the phosphorylation of nicotinamide adenine dinucleotide (NAD+) to nicotinamide adenine dinucleotide phosphate (NADP+) using ATP as the phosphate donor.	Phosphates	130-139	NAD kinase	Homo sapiens	13-17
27582489-1	2016	NAD+ kinase (NADK) catalyzes the phosphorylation of nicotinamide adenine dinucleotide (NAD+) to nicotinamide adenine dinucleotide phosphate (NADP+) using ATP as the phosphate donor.	Phosphates	130-139	NAD kinase	Homo sapiens	0-3
27582489-6	2016	Given its key role in metabolism and regulation of ROS, it is not surprising that several recent studies, including in vitro and in vivo assays of tumor growth and querying of patient samples, have identified NADK as a potential therapeutic target for the treatment of cancer.	Reactive Oxygen Species	51-54	NAD kinase	Homo sapiens	209-213
27582489-7	2016	In this review, we will discuss the experimental evidence justifying further exploration of NADK as a clinically relevant drug target and describe our studies with a lead compound, thionicotinamide, an NADK inhibitor prodrug.	thionicotinamide	181-197	NAD kinase	Homo sapiens	92-96
27582489-7	2016	In this review, we will discuss the experimental evidence justifying further exploration of NADK as a clinically relevant drug target and describe our studies with a lead compound, thionicotinamide, an NADK inhibitor prodrug.	thionicotinamide	181-197	NAD kinase	Homo sapiens	202-206
26806015-4	2016	This approach reveals oncogenic activity for rare gene aberrations in genes including NAD Kinase (NADK), which regulates NADP(H) homeostasis and cellular redox state.	NADP	121-128	NAD kinase	Homo sapiens	86-96
26806015-4	2016	This approach reveals oncogenic activity for rare gene aberrations in genes including NAD Kinase (NADK), which regulates NADP(H) homeostasis and cellular redox state.	NADP	121-128	NAD kinase	Homo sapiens	98-102
26806015-5	2016	We further validate mutant NADK, whose expression provides gain-of-function enzymatic activity leading to a reduction in cellular reactive oxygen species and tumorigenesis, and show that depletion of wild-type NADK in PDAC cell lines attenuates cancer cell growth in vitro and in vivo.	Reactive Oxygen Species	130-153	NAD kinase	Homo sapiens	27-31
26219913-1	2015	NAD(+) kinase (NADK) is the only known cytosolic enzyme that converts NAD(+) to NADP(+), which is subsequently reduced to NADPH.	NADP	80-87	NAD kinase	Homo sapiens	0-13
26219913-1	2015	NAD(+) kinase (NADK) is the only known cytosolic enzyme that converts NAD(+) to NADP(+), which is subsequently reduced to NADPH.	NADP	80-87	NAD kinase	Homo sapiens	15-19
26219913-1	2015	NAD(+) kinase (NADK) is the only known cytosolic enzyme that converts NAD(+) to NADP(+), which is subsequently reduced to NADPH.	NADP	122-127	NAD kinase	Homo sapiens	0-13
26219913-1	2015	NAD(+) kinase (NADK) is the only known cytosolic enzyme that converts NAD(+) to NADP(+), which is subsequently reduced to NADPH.	NADP	122-127	NAD kinase	Homo sapiens	15-19
26219913-4	2015	In vitro and in vivo inhibition of NADK with either small-hairpin RNA or thionicotinamide inhibited proliferation.	thionicotinamide	73-89	NAD kinase	Homo sapiens	35-39
26219913-6	2015	NADK inhibitors alone or in combination with drugs that increase ROS-mediated stress may represent an efficacious antitumor combination and should be explored further.	Reactive Oxygen Species	65-68	NAD kinase	Homo sapiens	0-4
25641397-5	2015	The NAD kinase (NADK) is the sole NADP biosynthetic enzyme.	NADP	34-38	NAD kinase	Homo sapiens	4-14
25641397-5	2015	The NAD kinase (NADK) is the sole NADP biosynthetic enzyme.	NADP	34-38	NAD kinase	Homo sapiens	16-20
23212377-1	2012	NAD kinase is the sole NADP(+) biosynthetic enzyme.	NADP	23-30	NAD kinase	Homo sapiens	0-10
23616928-13	2013	Identification of MNADK immediately suggests a model in which NADK and MNADK are responsible for de novo synthesis of NADP(+) in cytosol and mitochondria, respectively, and therefore provides novel insights into understanding the sources and mechanisms of mitochondrial NADP(+) and NADH production in human cells.	NADP	118-125	NAD kinase	Homo sapiens	19-23
23616928-13	2013	Identification of MNADK immediately suggests a model in which NADK and MNADK are responsible for de novo synthesis of NADP(+) in cytosol and mitochondria, respectively, and therefore provides novel insights into understanding the sources and mechanisms of mitochondrial NADP(+) and NADH production in human cells.	NADP	270-277	NAD kinase	Homo sapiens	19-23
23616928-13	2013	Identification of MNADK immediately suggests a model in which NADK and MNADK are responsible for de novo synthesis of NADP(+) in cytosol and mitochondria, respectively, and therefore provides novel insights into understanding the sources and mechanisms of mitochondrial NADP(+) and NADH production in human cells.	NAD	282-286	NAD kinase	Homo sapiens	19-23
24022322-0	2013	Conferring the ability to utilize inorganic polyphosphate on ATP-specific NAD kinase.	inorganic polyphosphate	34-57	NAD kinase	Homo sapiens	74-84
24022322-1	2013	NAD kinase (NADK) is a crucial enzyme for production of NADP+.	NADP	56-61	NAD kinase	Homo sapiens	0-10
24022322-1	2013	NAD kinase (NADK) is a crucial enzyme for production of NADP+.	NADP	56-61	NAD kinase	Homo sapiens	12-16
24022322-2	2013	ATP-specific NADK prefers ATP to inorganic polyphosphate [poly(P)] as a phosphoryl donor, whereas poly(P)/ATP-NADK utilizes both ATP and poly(P), and is employed in industrial mass production of NADP+.	Adenosine Triphosphate	0-3	NAD kinase	Homo sapiens	13-17
24022322-2	2013	ATP-specific NADK prefers ATP to inorganic polyphosphate [poly(P)] as a phosphoryl donor, whereas poly(P)/ATP-NADK utilizes both ATP and poly(P), and is employed in industrial mass production of NADP+.	Adenosine Triphosphate	0-3	NAD kinase	Homo sapiens	110-114
24022322-2	2013	ATP-specific NADK prefers ATP to inorganic polyphosphate [poly(P)] as a phosphoryl donor, whereas poly(P)/ATP-NADK utilizes both ATP and poly(P), and is employed in industrial mass production of NADP+.	Adenosine Triphosphate	26-29	NAD kinase	Homo sapiens	13-17
24022322-2	2013	ATP-specific NADK prefers ATP to inorganic polyphosphate [poly(P)] as a phosphoryl donor, whereas poly(P)/ATP-NADK utilizes both ATP and poly(P), and is employed in industrial mass production of NADP+.	Polyphosphates	43-56	NAD kinase	Homo sapiens	13-17
24022322-2	2013	ATP-specific NADK prefers ATP to inorganic polyphosphate [poly(P)] as a phosphoryl donor, whereas poly(P)/ATP-NADK utilizes both ATP and poly(P), and is employed in industrial mass production of NADP+.	Adenosine Triphosphate	26-29	NAD kinase	Homo sapiens	13-17
24022322-2	2013	ATP-specific NADK prefers ATP to inorganic polyphosphate [poly(P)] as a phosphoryl donor, whereas poly(P)/ATP-NADK utilizes both ATP and poly(P), and is employed in industrial mass production of NADP+.	NADP	195-200	NAD kinase	Homo sapiens	13-17
24022322-2	2013	ATP-specific NADK prefers ATP to inorganic polyphosphate [poly(P)] as a phosphoryl donor, whereas poly(P)/ATP-NADK utilizes both ATP and poly(P), and is employed in industrial mass production of NADP+.	NADP	195-200	NAD kinase	Homo sapiens	110-114
24022322-5	2013	We also demonstrate that a poly(P)/ATP-NADK created through this method is suitable for the poly(P)-dependent mass production of NADP+.	Adenosine Triphosphate	35-38	NAD kinase	Homo sapiens	39-43
24022322-5	2013	We also demonstrate that a poly(P)/ATP-NADK created through this method is suitable for the poly(P)-dependent mass production of NADP+.	NADP	129-134	NAD kinase	Homo sapiens	39-43
23777333-11	2013	Mechanistically, enhanced superoxide production in neutrophils was associated with increases in levels of NAD(+) and NADP(+), as well as activation of NAD(+) kinase.	Superoxides	26-36	NAD kinase	Homo sapiens	151-164
22954684-6	2012	Studies of the mechanism by which BR lowers DHFR showed that BR, through its metabolite BAD, reduced NADP and NADPH cellular levels by inhibiting nicotinamide adenine dinucleotide kinase (NADK).	3-(1-deoxyribofuranosyl)benzamide	34-36	NAD kinase	Homo sapiens	146-186
22954684-6	2012	Studies of the mechanism by which BR lowers DHFR showed that BR, through its metabolite BAD, reduced NADP and NADPH cellular levels by inhibiting nicotinamide adenine dinucleotide kinase (NADK).	3-(1-deoxyribofuranosyl)benzamide	34-36	NAD kinase	Homo sapiens	188-192
22954684-6	2012	Studies of the mechanism by which BR lowers DHFR showed that BR, through its metabolite BAD, reduced NADP and NADPH cellular levels by inhibiting nicotinamide adenine dinucleotide kinase (NADK).	3-(1-deoxyribofuranosyl)benzamide	61-63	NAD kinase	Homo sapiens	146-186
22954684-6	2012	Studies of the mechanism by which BR lowers DHFR showed that BR, through its metabolite BAD, reduced NADP and NADPH cellular levels by inhibiting nicotinamide adenine dinucleotide kinase (NADK).	3-(1-deoxyribofuranosyl)benzamide	61-63	NAD kinase	Homo sapiens	188-192
22954684-6	2012	Studies of the mechanism by which BR lowers DHFR showed that BR, through its metabolite BAD, reduced NADP and NADPH cellular levels by inhibiting nicotinamide adenine dinucleotide kinase (NADK).	NADP	101-105	NAD kinase	Homo sapiens	146-186
22954684-6	2012	Studies of the mechanism by which BR lowers DHFR showed that BR, through its metabolite BAD, reduced NADP and NADPH cellular levels by inhibiting nicotinamide adenine dinucleotide kinase (NADK).	NADP	101-105	NAD kinase	Homo sapiens	188-192
22954684-6	2012	Studies of the mechanism by which BR lowers DHFR showed that BR, through its metabolite BAD, reduced NADP and NADPH cellular levels by inhibiting nicotinamide adenine dinucleotide kinase (NADK).	NADP	110-115	NAD kinase	Homo sapiens	146-186
22954684-6	2012	Studies of the mechanism by which BR lowers DHFR showed that BR, through its metabolite BAD, reduced NADP and NADPH cellular levels by inhibiting nicotinamide adenine dinucleotide kinase (NADK).	NADP	110-115	NAD kinase	Homo sapiens	188-192
23212377-3	2012	Here we present evidence demonstrating that a human protein of unknown function, C5orf33, is a human mitochondrial NAD kinase; this protein likely represents the missing source of human mitochondrial NADP(+).	NADP	200-204	NAD kinase	Homo sapiens	115-125
21526340-0	2011	NADPH regulates human NAD kinase, a NADP+-biosynthetic enzyme.	NADP	0-5	NAD kinase	Homo sapiens	22-32
21526340-0	2011	NADPH regulates human NAD kinase, a NADP+-biosynthetic enzyme.	NADP	36-41	NAD kinase	Homo sapiens	22-32
21526340-1	2011	NAD kinase (NADK, EC 2.7.1.23) is the sole NADP(+)-biosynthetic enzyme that catalyzes phosphorylation of NAD(+) to yield NADP(+) using ATP as a phosphoryl donor, and thus, plays a vital role in the cell and represents a potentially powerful antimicrobial drug target.	NADP	43-50	NAD kinase	Homo sapiens	0-10
21526340-1	2011	NAD kinase (NADK, EC 2.7.1.23) is the sole NADP(+)-biosynthetic enzyme that catalyzes phosphorylation of NAD(+) to yield NADP(+) using ATP as a phosphoryl donor, and thus, plays a vital role in the cell and represents a potentially powerful antimicrobial drug target.	NADP	43-50	NAD kinase	Homo sapiens	12-16
21526340-1	2011	NAD kinase (NADK, EC 2.7.1.23) is the sole NADP(+)-biosynthetic enzyme that catalyzes phosphorylation of NAD(+) to yield NADP(+) using ATP as a phosphoryl donor, and thus, plays a vital role in the cell and represents a potentially powerful antimicrobial drug target.	NAD	105-111	NAD kinase	Homo sapiens	0-10
21526340-1	2011	NAD kinase (NADK, EC 2.7.1.23) is the sole NADP(+)-biosynthetic enzyme that catalyzes phosphorylation of NAD(+) to yield NADP(+) using ATP as a phosphoryl donor, and thus, plays a vital role in the cell and represents a potentially powerful antimicrobial drug target.	NAD	105-111	NAD kinase	Homo sapiens	12-16
21526340-1	2011	NAD kinase (NADK, EC 2.7.1.23) is the sole NADP(+)-biosynthetic enzyme that catalyzes phosphorylation of NAD(+) to yield NADP(+) using ATP as a phosphoryl donor, and thus, plays a vital role in the cell and represents a potentially powerful antimicrobial drug target.	NADP	121-128	NAD kinase	Homo sapiens	0-10
21526340-1	2011	NAD kinase (NADK, EC 2.7.1.23) is the sole NADP(+)-biosynthetic enzyme that catalyzes phosphorylation of NAD(+) to yield NADP(+) using ATP as a phosphoryl donor, and thus, plays a vital role in the cell and represents a potentially powerful antimicrobial drug target.	NADP	121-128	NAD kinase	Homo sapiens	12-16
21526340-1	2011	NAD kinase (NADK, EC 2.7.1.23) is the sole NADP(+)-biosynthetic enzyme that catalyzes phosphorylation of NAD(+) to yield NADP(+) using ATP as a phosphoryl donor, and thus, plays a vital role in the cell and represents a potentially powerful antimicrobial drug target.	Adenosine Triphosphate	135-138	NAD kinase	Homo sapiens	0-10
21526340-1	2011	NAD kinase (NADK, EC 2.7.1.23) is the sole NADP(+)-biosynthetic enzyme that catalyzes phosphorylation of NAD(+) to yield NADP(+) using ATP as a phosphoryl donor, and thus, plays a vital role in the cell and represents a potentially powerful antimicrobial drug target.	Adenosine Triphosphate	135-138	NAD kinase	Homo sapiens	12-16
21526340-5	2011	Using the purified human NADK, we revealed a sigmoidal kinetic behavior toward ATP and the inhibitory effects of NADPH and NADH, but not of NADP(+), on the catalytic activity of the enzyme.	Adenosine Triphosphate	79-82	NAD kinase	Homo sapiens	25-29
21526340-5	2011	Using the purified human NADK, we revealed a sigmoidal kinetic behavior toward ATP and the inhibitory effects of NADPH and NADH, but not of NADP(+), on the catalytic activity of the enzyme.	NADP	113-118	NAD kinase	Homo sapiens	25-29
21526340-5	2011	Using the purified human NADK, we revealed a sigmoidal kinetic behavior toward ATP and the inhibitory effects of NADPH and NADH, but not of NADP(+), on the catalytic activity of the enzyme.	NAD	123-127	NAD kinase	Homo sapiens	25-29
21526340-5	2011	Using the purified human NADK, we revealed a sigmoidal kinetic behavior toward ATP and the inhibitory effects of NADPH and NADH, but not of NADP(+), on the catalytic activity of the enzyme.	NADP	113-117	NAD kinase	Homo sapiens	25-29
21526340-7	2011	Furthermore, these attributes may provide a clue to design a novel drug against Mycobacterium tuberculosis in which this bacterial NADK is potently inhibited by NADP(+).	NADP	161-168	NAD kinase	Homo sapiens	131-135
21730068-1	2011	NAD kinase catalyzes the phosphorylation of NAD(+) to synthesize NADP(+), whereas NADH kinase catalyzes conversion of NADH to NADPH.	NAD	44-50	NAD kinase	Homo sapiens	0-10
21730068-1	2011	NAD kinase catalyzes the phosphorylation of NAD(+) to synthesize NADP(+), whereas NADH kinase catalyzes conversion of NADH to NADPH.	NADP	65-72	NAD kinase	Homo sapiens	0-10
21730068-1	2011	NAD kinase catalyzes the phosphorylation of NAD(+) to synthesize NADP(+), whereas NADH kinase catalyzes conversion of NADH to NADPH.	NAD	82-86	NAD kinase	Homo sapiens	0-10
21730068-1	2011	NAD kinase catalyzes the phosphorylation of NAD(+) to synthesize NADP(+), whereas NADH kinase catalyzes conversion of NADH to NADPH.	NADP	126-131	NAD kinase	Homo sapiens	0-10
21730068-4	2011	Detailed analysis, including a comparison of the tertiary structure of Pos5 with the structures of human and bacterial NAD kinases, revealed that Arg-293 of Pos5, corresponding to His-351 of human NAD kinase, confers a positive charge on the surface of NADH-binding site, whereas the corresponding His residue does not.	Arginine	146-149	NAD kinase	Homo sapiens	119-129
21730068-4	2011	Detailed analysis, including a comparison of the tertiary structure of Pos5 with the structures of human and bacterial NAD kinases, revealed that Arg-293 of Pos5, corresponding to His-351 of human NAD kinase, confers a positive charge on the surface of NADH-binding site, whereas the corresponding His residue does not.	Histidine	180-183	NAD kinase	Homo sapiens	119-129
21730068-4	2011	Detailed analysis, including a comparison of the tertiary structure of Pos5 with the structures of human and bacterial NAD kinases, revealed that Arg-293 of Pos5, corresponding to His-351 of human NAD kinase, confers a positive charge on the surface of NADH-binding site, whereas the corresponding His residue does not.	NAD	253-257	NAD kinase	Homo sapiens	119-129
21730068-4	2011	Detailed analysis, including a comparison of the tertiary structure of Pos5 with the structures of human and bacterial NAD kinases, revealed that Arg-293 of Pos5, corresponding to His-351 of human NAD kinase, confers a positive charge on the surface of NADH-binding site, whereas the corresponding His residue does not.	Histidine	298-301	NAD kinase	Homo sapiens	119-129
21730068-6	2011	Conversely, simultaneous changes of Ala-330 and His-351 of human NAD kinase into Ser and Arg residues significantly increased the ratio of NADH kinase activity to NAD kinase activity from 0.043 to 1.39; human Ala-330 corresponds to Pos5 Ser-272, which interacts with the side chain of Arg-293.	Alanine	36-39	NAD kinase	Homo sapiens	65-75
21730068-6	2011	Conversely, simultaneous changes of Ala-330 and His-351 of human NAD kinase into Ser and Arg residues significantly increased the ratio of NADH kinase activity to NAD kinase activity from 0.043 to 1.39; human Ala-330 corresponds to Pos5 Ser-272, which interacts with the side chain of Arg-293.	Alanine	36-39	NAD kinase	Homo sapiens	163-173
21730068-6	2011	Conversely, simultaneous changes of Ala-330 and His-351 of human NAD kinase into Ser and Arg residues significantly increased the ratio of NADH kinase activity to NAD kinase activity from 0.043 to 1.39; human Ala-330 corresponds to Pos5 Ser-272, which interacts with the side chain of Arg-293.	Histidine	48-51	NAD kinase	Homo sapiens	65-75
21730068-6	2011	Conversely, simultaneous changes of Ala-330 and His-351 of human NAD kinase into Ser and Arg residues significantly increased the ratio of NADH kinase activity to NAD kinase activity from 0.043 to 1.39; human Ala-330 corresponds to Pos5 Ser-272, which interacts with the side chain of Arg-293.	Histidine	48-51	NAD kinase	Homo sapiens	163-173
21730068-6	2011	Conversely, simultaneous changes of Ala-330 and His-351 of human NAD kinase into Ser and Arg residues significantly increased the ratio of NADH kinase activity to NAD kinase activity from 0.043 to 1.39; human Ala-330 corresponds to Pos5 Ser-272, which interacts with the side chain of Arg-293.	Serine	81-84	NAD kinase	Homo sapiens	65-75
21730068-6	2011	Conversely, simultaneous changes of Ala-330 and His-351 of human NAD kinase into Ser and Arg residues significantly increased the ratio of NADH kinase activity to NAD kinase activity from 0.043 to 1.39; human Ala-330 corresponds to Pos5 Ser-272, which interacts with the side chain of Arg-293.	Serine	81-84	NAD kinase	Homo sapiens	163-173
21730068-6	2011	Conversely, simultaneous changes of Ala-330 and His-351 of human NAD kinase into Ser and Arg residues significantly increased the ratio of NADH kinase activity to NAD kinase activity from 0.043 to 1.39; human Ala-330 corresponds to Pos5 Ser-272, which interacts with the side chain of Arg-293.	Arginine	89-92	NAD kinase	Homo sapiens	65-75
21730068-6	2011	Conversely, simultaneous changes of Ala-330 and His-351 of human NAD kinase into Ser and Arg residues significantly increased the ratio of NADH kinase activity to NAD kinase activity from 0.043 to 1.39; human Ala-330 corresponds to Pos5 Ser-272, which interacts with the side chain of Arg-293.	Arginine	89-92	NAD kinase	Homo sapiens	163-173
21730068-6	2011	Conversely, simultaneous changes of Ala-330 and His-351 of human NAD kinase into Ser and Arg residues significantly increased the ratio of NADH kinase activity to NAD kinase activity from 0.043 to 1.39; human Ala-330 corresponds to Pos5 Ser-272, which interacts with the side chain of Arg-293.	Alanine	209-212	NAD kinase	Homo sapiens	65-75
21730068-6	2011	Conversely, simultaneous changes of Ala-330 and His-351 of human NAD kinase into Ser and Arg residues significantly increased the ratio of NADH kinase activity to NAD kinase activity from 0.043 to 1.39; human Ala-330 corresponds to Pos5 Ser-272, which interacts with the side chain of Arg-293.	Alanine	209-212	NAD kinase	Homo sapiens	163-173
21730068-6	2011	Conversely, simultaneous changes of Ala-330 and His-351 of human NAD kinase into Ser and Arg residues significantly increased the ratio of NADH kinase activity to NAD kinase activity from 0.043 to 1.39; human Ala-330 corresponds to Pos5 Ser-272, which interacts with the side chain of Arg-293.	Serine	237-240	NAD kinase	Homo sapiens	65-75
21730068-6	2011	Conversely, simultaneous changes of Ala-330 and His-351 of human NAD kinase into Ser and Arg residues significantly increased the ratio of NADH kinase activity to NAD kinase activity from 0.043 to 1.39; human Ala-330 corresponds to Pos5 Ser-272, which interacts with the side chain of Arg-293.	Arginine	285-288	NAD kinase	Homo sapiens	65-75
18391451-0	2008	Structure and function of NAD kinase and NADP phosphatase: key enzymes that regulate the intracellular balance of NAD(H) and NADP(H).	NAD	114-120	NAD kinase	Homo sapiens	26-36
19355893-2	2009	Key reactions for NAD(P) biosynthesis in all organisms, common to both de novo and salvage routes, are catalyzed by NMN/NaMN adenylyltransferase (NMNAT), NAD synthetase (NADS), and NAD kinase (NADK).	NADP	18-24	NAD kinase	Homo sapiens	181-191
19355893-2	2009	Key reactions for NAD(P) biosynthesis in all organisms, common to both de novo and salvage routes, are catalyzed by NMN/NaMN adenylyltransferase (NMNAT), NAD synthetase (NADS), and NAD kinase (NADK).	NADP	18-24	NAD kinase	Homo sapiens	193-197
19430699-1	2009	NAD kinase catalyzes the phosphorylation of NAD(H) to form NADP(H), using ATP as phosphoryl donor.	NAD	44-50	NAD kinase	Homo sapiens	0-10
19430699-1	2009	NAD kinase catalyzes the phosphorylation of NAD(H) to form NADP(H), using ATP as phosphoryl donor.	NADP	59-66	NAD kinase	Homo sapiens	0-10
19430699-1	2009	NAD kinase catalyzes the phosphorylation of NAD(H) to form NADP(H), using ATP as phosphoryl donor.	Adenosine Triphosphate	74-77	NAD kinase	Homo sapiens	0-10
19430699-4	2009	Recent studies have partially demonstrated that NAD kinase plays a crucial role in the regulation of NAD(H)/NADP(H) conversion.	NAD	101-107	NAD kinase	Homo sapiens	48-58
19430699-4	2009	Recent studies have partially demonstrated that NAD kinase plays a crucial role in the regulation of NAD(H)/NADP(H) conversion.	NADP	108-115	NAD kinase	Homo sapiens	48-58
17855339-5	2007	Overexpression of NADK resulted in a 4-5-fold increase in the NADPH, but not NADP(+), concentration, although the recombinant enzyme phosphorylated preferentially NAD(+).	NADP	77-84	NAD kinase	Homo sapiens	18-22
17855339-5	2007	Overexpression of NADK resulted in a 4-5-fold increase in the NADPH, but not NADP(+), concentration, although the recombinant enzyme phosphorylated preferentially NAD(+).	NAD	163-169	NAD kinase	Homo sapiens	18-22
16242716-0	2005	Crystal structures of an NAD kinase from Archaeoglobus fulgidus in complex with ATP, NAD, or NADP.	Adenosine Triphosphate	80-83	NAD kinase	Homo sapiens	25-35
16242716-0	2005	Crystal structures of an NAD kinase from Archaeoglobus fulgidus in complex with ATP, NAD, or NADP.	NADP	93-97	NAD kinase	Homo sapiens	25-35
16242716-1	2005	NAD kinase is a ubiquitous enzyme that catalyzes the phosphorylation of NAD to NADP using ATP or inorganic polyphosphate (poly(P)) as phosphate donor, and is regarded as the only enzyme responsible for the synthesis of NADP.	NADP	79-83	NAD kinase	Homo sapiens	0-10
16242716-1	2005	NAD kinase is a ubiquitous enzyme that catalyzes the phosphorylation of NAD to NADP using ATP or inorganic polyphosphate (poly(P)) as phosphate donor, and is regarded as the only enzyme responsible for the synthesis of NADP.	Adenosine Triphosphate	90-93	NAD kinase	Homo sapiens	0-10
16242716-1	2005	NAD kinase is a ubiquitous enzyme that catalyzes the phosphorylation of NAD to NADP using ATP or inorganic polyphosphate (poly(P)) as phosphate donor, and is regarded as the only enzyme responsible for the synthesis of NADP.	inorganic polyphosphate	97-120	NAD kinase	Homo sapiens	0-10
15855156-1	2005	NAD kinase phosphorylates NAD+ to form NADP+ and is strictly specific to NAD+, whereas NADH kinase phosphorylates both NAD+ and NADH, thereby showing relaxed substrate specificity.	NAD	26-30	NAD kinase	Homo sapiens	0-10
15855156-1	2005	NAD kinase phosphorylates NAD+ to form NADP+ and is strictly specific to NAD+, whereas NADH kinase phosphorylates both NAD+ and NADH, thereby showing relaxed substrate specificity.	NADP	39-44	NAD kinase	Homo sapiens	0-10
15855156-1	2005	NAD kinase phosphorylates NAD+ to form NADP+ and is strictly specific to NAD+, whereas NADH kinase phosphorylates both NAD+ and NADH, thereby showing relaxed substrate specificity.	NAD	73-77	NAD kinase	Homo sapiens	0-10
15855156-1	2005	NAD kinase phosphorylates NAD+ to form NADP+ and is strictly specific to NAD+, whereas NADH kinase phosphorylates both NAD+ and NADH, thereby showing relaxed substrate specificity.	NAD	73-77	NAD kinase	Homo sapiens	0-10
15855156-4	2005	The substitution of Arg in one NAD kinase with polar amino acids also relaxed the substrate specificity, whereas substitution with charged and hydrophobic amino acids did not show a similar result.	Arginine	20-23	NAD kinase	Homo sapiens	31-41
17083911-4	2006	The product, oxidized nicotinamide adenine dinucleotide phosphate (NADP(+)), formed following the reaction of NADK with NAD(+) and adenosine 5"-triphosphate was detected with the aid of glucose-6-phosphate dehydrogenase or NADP(+)-isocitrate dehydrogenase, iodonitrotetrazolium chloride, and phenazine methosulfate.	NADP	22-65	NAD kinase	Homo sapiens	110-114
17083911-4	2006	The product, oxidized nicotinamide adenine dinucleotide phosphate (NADP(+)), formed following the reaction of NADK with NAD(+) and adenosine 5"-triphosphate was detected with the aid of glucose-6-phosphate dehydrogenase or NADP(+)-isocitrate dehydrogenase, iodonitrotetrazolium chloride, and phenazine methosulfate.	NADP	67-74	NAD kinase	Homo sapiens	110-114
17083911-4	2006	The product, oxidized nicotinamide adenine dinucleotide phosphate (NADP(+)), formed following the reaction of NADK with NAD(+) and adenosine 5"-triphosphate was detected with the aid of glucose-6-phosphate dehydrogenase or NADP(+)-isocitrate dehydrogenase, iodonitrotetrazolium chloride, and phenazine methosulfate.	NAD	120-126	NAD kinase	Homo sapiens	110-114
17083911-4	2006	The product, oxidized nicotinamide adenine dinucleotide phosphate (NADP(+)), formed following the reaction of NADK with NAD(+) and adenosine 5"-triphosphate was detected with the aid of glucose-6-phosphate dehydrogenase or NADP(+)-isocitrate dehydrogenase, iodonitrotetrazolium chloride, and phenazine methosulfate.	5"-triphosphate	141-156	NAD kinase	Homo sapiens	110-114
17083911-4	2006	The product, oxidized nicotinamide adenine dinucleotide phosphate (NADP(+)), formed following the reaction of NADK with NAD(+) and adenosine 5"-triphosphate was detected with the aid of glucose-6-phosphate dehydrogenase or NADP(+)-isocitrate dehydrogenase, iodonitrotetrazolium chloride, and phenazine methosulfate.	NADP	67-71	NAD kinase	Homo sapiens	110-114
17083911-4	2006	The product, oxidized nicotinamide adenine dinucleotide phosphate (NADP(+)), formed following the reaction of NADK with NAD(+) and adenosine 5"-triphosphate was detected with the aid of glucose-6-phosphate dehydrogenase or NADP(+)-isocitrate dehydrogenase, iodonitrotetrazolium chloride, and phenazine methosulfate.	iodonitrotetrazolium	257-286	NAD kinase	Homo sapiens	110-114
17083911-4	2006	The product, oxidized nicotinamide adenine dinucleotide phosphate (NADP(+)), formed following the reaction of NADK with NAD(+) and adenosine 5"-triphosphate was detected with the aid of glucose-6-phosphate dehydrogenase or NADP(+)-isocitrate dehydrogenase, iodonitrotetrazolium chloride, and phenazine methosulfate.	Methylphenazonium Methosulfate	292-314	NAD kinase	Homo sapiens	110-114
17083911-6	2006	Hence this novel electrophoretic method allows the easy detection of NADK, a critical enzyme involved in pyridine homeostasis.	pyridine	105-113	NAD kinase	Homo sapiens	69-73
16842123-0	2006	Structural and functional properties of NAD kinase, a key enzyme in NADP biosynthesis.	NADP	68-72	NAD kinase	Homo sapiens	40-50
16242716-1	2005	NAD kinase is a ubiquitous enzyme that catalyzes the phosphorylation of NAD to NADP using ATP or inorganic polyphosphate (poly(P)) as phosphate donor, and is regarded as the only enzyme responsible for the synthesis of NADP.	Phosphates	111-120	NAD kinase	Homo sapiens	0-10
16242716-1	2005	NAD kinase is a ubiquitous enzyme that catalyzes the phosphorylation of NAD to NADP using ATP or inorganic polyphosphate (poly(P)) as phosphate donor, and is regarded as the only enzyme responsible for the synthesis of NADP.	NADP	219-223	NAD kinase	Homo sapiens	0-10
16242716-2	2005	We present here the crystal structures of an NAD kinase from the archaeal organism Archaeoglobus fulgidus in complex with its phosphate donor ATP at 1.7 A resolution, with its substrate NAD at 3.05 A resolution, and with the product NADP in two different crystal forms at 2.45 A and 2.0 A resolution, respectively.	Phosphates	126-135	NAD kinase	Homo sapiens	45-55
16242716-2	2005	We present here the crystal structures of an NAD kinase from the archaeal organism Archaeoglobus fulgidus in complex with its phosphate donor ATP at 1.7 A resolution, with its substrate NAD at 3.05 A resolution, and with the product NADP in two different crystal forms at 2.45 A and 2.0 A resolution, respectively.	Adenosine Triphosphate	142-145	NAD kinase	Homo sapiens	45-55
16242716-2	2005	We present here the crystal structures of an NAD kinase from the archaeal organism Archaeoglobus fulgidus in complex with its phosphate donor ATP at 1.7 A resolution, with its substrate NAD at 3.05 A resolution, and with the product NADP in two different crystal forms at 2.45 A and 2.0 A resolution, respectively.	NADP	233-237	NAD kinase	Homo sapiens	45-55