PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11953438-2	2002	Ligand-binding analyses were conducted to examine effects of residue changes in putative catalytic and regulatory isocitrate-binding sites respectively contained in IDH2 and IDH1 subunits.	isocitric acid	114-124	isocitrate dehydrogenase (NAD(+)) IDH2	Saccharomyces cerevisiae S288C	165-169	
12562755-9	2003	These results are consistent with previous studies demonstrating that the catalytic isocitrate binding sites are comprised of residues primarily contributed by IDH2, whereas sites for regulatory binding of isocitrate are contributed by analogous residues of IDH1.	isocitric acid	84-94	isocitrate dehydrogenase (NAD(+)) IDH2	Saccharomyces cerevisiae S288C	160-164	
12562755-10	2003	In this study, we also demonstrate that a prerequisite for holoenzyme binding of NAD(+) is binding of isocitrate/Mg(2+) at the IDH2 catalytic site.	isocitric acid	102-112	isocitrate dehydrogenase (NAD(+)) IDH2	Saccharomyces cerevisiae S288C	127-131	
11953438-3	2002	Replacement of homologous serine residues in either subunit site, S98A in IDH2 or S92A in IDH1, was found to reduce by half the total number of holoenzyme isocitrate-binding sites, confirming a correlation between detrimental effects on isocitrate binding and respective kinetic defects in catalysis and allosteric activation by AMP.	isocitric acid	155-165	isocitrate dehydrogenase (NAD(+)) IDH2	Saccharomyces cerevisiae S288C	74-78	
11953438-5	2002	The putative isocitrate-binding sites of IDH1 and IDH2 contain five identical and four nonidentical residues.	isocitric acid	13-23	isocitrate dehydrogenase (NAD(+)) IDH2	Saccharomyces cerevisiae S288C	50-54	
9244391-8	1997	Citrate and isocitrate concentrations were also elevated in the idh2 mutants, but probably not to toxic levels.	isocitric acid	12-22	isocitrate dehydrogenase (NAD(+)) IDH2	Saccharomyces cerevisiae S288C	64-68	
11042198-2	2001	IDH2 was previously shown to contain the catalytic site, whereas IDH1 contributes regulatory properties including cooperativity with respect to isocitrate and allosteric activation by AMP.	isocitric acid	144-154	isocitrate dehydrogenase (NAD(+)) IDH2	Saccharomyces cerevisiae S288C	0-4	
11042198-9	2001	A K189A substitution in IDH2 was found to produce a decrease in activation of the enzyme by AMP and a loss of cooperativity with respect to isocitrate.	isocitric acid	140-150	isocitrate dehydrogenase (NAD(+)) IDH2	Saccharomyces cerevisiae S288C	24-28	
11714283-11	2001	Overall, results are consistent with isocitrate binding by IDH2 for catalysis and with isocitrate binding by IDH1 being a prerequisite for allosteric activation by AMP.	isocitric acid	37-47	isocitrate dehydrogenase (NAD(+)) IDH2	Saccharomyces cerevisiae S288C	59-63	
8369302-0	1993	Kinetic analysis of NAD(+)-isocitrate dehydrogenase with altered isocitrate binding sites: contribution of IDH1 and IDH2 subunits to regulation and catalysis.	isocitric acid	27-37	isocitrate dehydrogenase (NAD(+)) IDH2	Saccharomyces cerevisiae S288C	116-120	
8369302-6	1993	The IDH1 mutant enzyme was not activated by AMP, whereas the IDH2 mutant enzyme exhibited an increase in isocitrate affinity in the presence of AMP similar to that observed with the wild-type enzyme.	isocitric acid	105-115	isocitrate dehydrogenase (NAD(+)) IDH2	Saccharomyces cerevisiae S288C	61-65	
8369302-4	1993	The mutant IDH2, in contrast, exhibited a 60-fold decrease in maximal velocity and a 2-fold reduction in S0.5 for isocitrate, but the cooperativity was unaffected.	isocitric acid	114-124	isocitrate dehydrogenase (NAD(+)) IDH2	Saccharomyces cerevisiae S288C	11-15	
21861471-6	2011	A tetrameric form of IDH (an IDH1(G15D)/IDH2 mutant enzyme) demonstrated half-site binding for isocitrate (two sites) in the absence of dithiothreitol and full-site binding (four sites) in the presence of dithiothreitol.	isocitric acid	95-105	isocitrate dehydrogenase (NAD(+)) IDH2	Saccharomyces cerevisiae S288C	40-44	
2198251-8	1990	Mitochondria isolated from the IDH1 and IDH2 mutants exhibited a markedly reduced capacity for utilization of either isocitrate or citrate for respiratory O2 consumption.	isocitric acid	117-127	isocitrate dehydrogenase (NAD(+)) IDH2	Saccharomyces cerevisiae S288C	40-44	
22008468-2	2012	IDH2 contains catalytic isocitrate/Mg2+ and NAD+ binding sites whereas IDH1 contains homologous binding sites, respectively, for cooperative binding of isocitrate and for allosteric binding of AMP.	isocitric acid	24-34	isocitrate dehydrogenase (NAD(+)) IDH2	Saccharomyces cerevisiae S288C	0-4	
22008468-2	2012	IDH2 contains catalytic isocitrate/Mg2+ and NAD+ binding sites whereas IDH1 contains homologous binding sites, respectively, for cooperative binding of isocitrate and for allosteric binding of AMP.	isocitric acid	152-162	isocitrate dehydrogenase (NAD(+)) IDH2	Saccharomyces cerevisiae S288C	0-4