PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
2703276-1	1989	Oncomodulin is a calcium-binding protein, detectable in extra-embryonic human and rat placental cells and in a wide variety of tumors, but not in any normal embryonic or adult rodent or human tissues.	Calcium	17-24	oncomodulin	Homo sapiens	0-11
3571255-2	1987	As deduced from its 1H NMR spectrum, oncomodulin"s solution conformation is very similar to the tertiary structure of other single domain 2-site calcium-binding proteins of the troponin C class.	Hydrogen	20-22	oncomodulin	Homo sapiens	37-48
3179268-0	1988	Disulfide-linked dimer of oncomodulin: comparison to calmodulin.	Disulfides	0-9	oncomodulin	Homo sapiens	26-37
3179268-1	1988	Oncomodulin, an oncofetal Ca2+-binding protein, contains a single Cys residue in position 18 of its primary structure.	Cysteine	66-69	oncomodulin	Homo sapiens	0-11
3179268-4	1988	Evidence presented here shows that oncomodulin can dimerize by intermolecular disulfide formation via the Cys-18 thiol.	Disulfides	78-87	oncomodulin	Homo sapiens	35-46
3179268-4	1988	Evidence presented here shows that oncomodulin can dimerize by intermolecular disulfide formation via the Cys-18 thiol.	Cysteine	106-109	oncomodulin	Homo sapiens	35-46
3179268-4	1988	Evidence presented here shows that oncomodulin can dimerize by intermolecular disulfide formation via the Cys-18 thiol.	Sulfhydryl Compounds	113-118	oncomodulin	Homo sapiens	35-46
3179268-6	1988	The disulfide-linked dimer of oncomodulin appears to be more similar to calmodulin than oncomodulin since the dimer displayed "calmodulin-like" affinity for the amphiphilic peptide melittin.	Disulfides	4-13	oncomodulin	Homo sapiens	30-41
3571255-5	1987	Lineshape analyses of several 1H NMR resonances generated by the Lu(III) titration of Ca2-oncomodulin indicated that Ca(II)----Ln(III) exchange at the CD site was 15-20 s-1, approximately 100 times faster than exchange at the CD site of parvalbumins.	Cadmium	226-228	oncomodulin	Homo sapiens	90-101
3571255-6	1987	Analyses of the distribution of metal-bound oncomodulin species showed that Ca(II)----Lu(III) exchange was cooperative, the coefficient of cooperativity being estimated as 5 +/- 1.	Metals	32-37	oncomodulin	Homo sapiens	44-55
3571255-2	1987	As deduced from its 1H NMR spectrum, oncomodulin"s solution conformation is very similar to the tertiary structure of other single domain 2-site calcium-binding proteins of the troponin C class.	Calcium	145-152	oncomodulin	Homo sapiens	37-48
3571255-7	1987	The kinetics of the release of Yb(III) from oncomodulin as measured by optical stopped-flow techniques corroborated the observed cooperativity in metal binding; the off-rate constant of Yb(III) from the EF site of Yb2-oncomodulin was 0.0036 s-1, approximately 19 times slower than the release of Yb(III) from the EF site of Ca1Yb1-oncomodulin.	Metals	146-151	oncomodulin	Homo sapiens	44-55
3571255-8	1987	We attribute part of the reduced preference of small Ln(III)s for the CD site of oncomodulin to a combination of this site"s inherent incompressibility (Williams, T.C., Corson, D.C. & Sykes, B.D.	Cadmium	70-72	oncomodulin	Homo sapiens	81-92
3571255-5	1987	Lineshape analyses of several 1H NMR resonances generated by the Lu(III) titration of Ca2-oncomodulin indicated that Ca(II)----Ln(III) exchange at the CD site was 15-20 s-1, approximately 100 times faster than exchange at the CD site of parvalbumins.	Hydrogen	30-32	oncomodulin	Homo sapiens	90-101
3571255-8	1987	We attribute part of the reduced preference of small Ln(III)s for the CD site of oncomodulin to a combination of this site"s inherent incompressibility (Williams, T.C., Corson, D.C. & Sykes, B.D.	Adenosine Monophosphate	183-186	oncomodulin	Homo sapiens	81-92
3571255-5	1987	Lineshape analyses of several 1H NMR resonances generated by the Lu(III) titration of Ca2-oncomodulin indicated that Ca(II)----Ln(III) exchange at the CD site was 15-20 s-1, approximately 100 times faster than exchange at the CD site of parvalbumins.	Cadmium	151-153	oncomodulin	Homo sapiens	90-101
3571255-14	1987	Like the CD site in oncomodulin, site III in troponin C has not only a lower affinity for calcium relative to the CD site of parvalbumins but also aspartic acid at its -X position; a water molecule bridges the gap between bound metal and the carboxyl group of the relatively short side chain of Asp-114 (Herzberg, O.	Cadmium	9-11	oncomodulin	Homo sapiens	20-31
3571255-14	1987	Like the CD site in oncomodulin, site III in troponin C has not only a lower affinity for calcium relative to the CD site of parvalbumins but also aspartic acid at its -X position; a water molecule bridges the gap between bound metal and the carboxyl group of the relatively short side chain of Asp-114 (Herzberg, O.	Calcium	90-97	oncomodulin	Homo sapiens	20-31
15327280-2	2004	As an example, a calcium binding protein (human oncomodulin), in which one of the calcium ions was selectively substituted with Tb3+, is used.	Calcium	17-24	oncomodulin	Homo sapiens	48-59
3571255-14	1987	Like the CD site in oncomodulin, site III in troponin C has not only a lower affinity for calcium relative to the CD site of parvalbumins but also aspartic acid at its -X position; a water molecule bridges the gap between bound metal and the carboxyl group of the relatively short side chain of Asp-114 (Herzberg, O.	Aspartic Acid	147-160	oncomodulin	Homo sapiens	20-31
3571255-14	1987	Like the CD site in oncomodulin, site III in troponin C has not only a lower affinity for calcium relative to the CD site of parvalbumins but also aspartic acid at its -X position; a water molecule bridges the gap between bound metal and the carboxyl group of the relatively short side chain of Asp-114 (Herzberg, O.	Water	183-188	oncomodulin	Homo sapiens	20-31
3571255-14	1987	Like the CD site in oncomodulin, site III in troponin C has not only a lower affinity for calcium relative to the CD site of parvalbumins but also aspartic acid at its -X position; a water molecule bridges the gap between bound metal and the carboxyl group of the relatively short side chain of Asp-114 (Herzberg, O.	Aspartic Acid	295-298	oncomodulin	Homo sapiens	20-31
3571255-16	1987	Hence, we suggest that Asp-59 in oncomodulin binds metal only indirectly through an intervening water molecule, a proposal which is consistent with the CD site"s reduced affinity for ions the size of Ca(II) or smaller.	Aspartic Acid	23-26	oncomodulin	Homo sapiens	33-44
3571255-16	1987	Hence, we suggest that Asp-59 in oncomodulin binds metal only indirectly through an intervening water molecule, a proposal which is consistent with the CD site"s reduced affinity for ions the size of Ca(II) or smaller.	Metals	51-56	oncomodulin	Homo sapiens	33-44
3571255-16	1987	Hence, we suggest that Asp-59 in oncomodulin binds metal only indirectly through an intervening water molecule, a proposal which is consistent with the CD site"s reduced affinity for ions the size of Ca(II) or smaller.	Water	96-101	oncomodulin	Homo sapiens	33-44
3571255-16	1987	Hence, we suggest that Asp-59 in oncomodulin binds metal only indirectly through an intervening water molecule, a proposal which is consistent with the CD site"s reduced affinity for ions the size of Ca(II) or smaller.	Cadmium	152-154	oncomodulin	Homo sapiens	33-44
33093204-0	2020	Amyloid formation of fish beta-parvalbumin involves primary nucleation triggered by disulfide-bridged protein dimers.	Disulfides	84-93	oncomodulin	Homo sapiens	26-42
33093204-4	2020	We performed biophysical experiments in combination with mathematical modeling of aggregation kinetics and discovered that the aggregation of beta-parvalbumin is initiated by the formation of dimers stabilized by disulfide bonds and then proceeds via primary nucleation and fibril elongation processes.	Disulfides	213-222	oncomodulin	Homo sapiens	142-158
32350587-3	2020	However, recent analyses revealed that subtle differences in the topographic expression of oncomodulin, another calcium-binding protein, reflects heterogeneous factors driving the subtle variations in expression.	Calcium	112-119	oncomodulin	Homo sapiens	91-102
16609936-8	2006	We extended an earlier study in which we identified a novel calcium-binding protein by IEF, oncomodulin, localized in the outer hair cells and show here the applicability of prefractionation for the screening of calcium-binding proteins of organ of Corti.	Calcium	60-67	oncomodulin	Homo sapiens	92-103
16609936-8	2006	We extended an earlier study in which we identified a novel calcium-binding protein by IEF, oncomodulin, localized in the outer hair cells and show here the applicability of prefractionation for the screening of calcium-binding proteins of organ of Corti.	Calcium	212-219	oncomodulin	Homo sapiens	92-103
29318409-1	2018	Oncomodulin (OCM, aka beta-parvalbumin) is an EF-hand calcium binding protein that is expressed in a restricted set of hair cells in the peristriolar region of the mammalian utricle.	Calcium	54-61	oncomodulin	Homo sapiens	0-11
15327280-2	2004	As an example, a calcium binding protein (human oncomodulin), in which one of the calcium ions was selectively substituted with Tb3+, is used.	tb3+	128-132	oncomodulin	Homo sapiens	48-59
9636056-0	1998	Interconversion of the ligand arrays in the CD and EF sites of oncomodulin.	Cadmium	44-46	oncomodulin	Homo sapiens	63-74
9636056-10	1998	Whereas the oncomodulin EF site exhibits the expected Ca2+/Mg2+ signature, the Ca2+ affinity of the CD site is severely attenuated.	magnesium ion	59-63	oncomodulin	Homo sapiens	12-23
9636056-19	1998	Significantly, the Ca2+ affinity of the oncomodulin CD site is increased by mutations that weaken binding at the EF site, indicating a negatively cooperative interaction between the two sites.	Cadmium	52-54	oncomodulin	Homo sapiens	40-51
7628071-1	1995	OBJECTIVES: The objective of this work was to demonstrate the utility of luminescence from lanthanides bound to a mutant of the Ca2+ binding protein, oncomodulin, to monitor protease activity.	Lanthanoid Series Elements	91-102	oncomodulin	Homo sapiens	150-161
8639547-0	1996	Introduction of a fifth carboxylate ligand heightens the affinity of the oncomodulin CD and EF sites for Ca2+.	carboxylate	24-35	oncomodulin	Homo sapiens	73-84
8639547-5	1996	Interestingly, for oncomodulin, we observe that introduction of a fifth carboxylate residue at the +z position in the CD coordination sphere or at the -x position in the EF coordination sphere significantly increases the affinity of those sites for Ca2+.	carboxylate	72-83	oncomodulin	Homo sapiens	19-30
8639547-5	1996	Interestingly, for oncomodulin, we observe that introduction of a fifth carboxylate residue at the +z position in the CD coordination sphere or at the -x position in the EF coordination sphere significantly increases the affinity of those sites for Ca2+.	Cadmium	118-120	oncomodulin	Homo sapiens	19-30
8639547-9	1996	Interestingly, the S55D mutation also increases the affinity of the oncomodulin CD site for Mg2+, decreasing the dissociation constant from > 1 mM to approximately 30 microM.	magnesium ion	92-96	oncomodulin	Homo sapiens	68-79
7628071-2	1995	DESIGN AND METHODS: A mutant of oncomodulin with a cysteine residue at position 57 located in the CD binding loop was conjugated to a salicylic acid group.	Cysteine	51-59	oncomodulin	Homo sapiens	32-43
7628071-2	1995	DESIGN AND METHODS: A mutant of oncomodulin with a cysteine residue at position 57 located in the CD binding loop was conjugated to a salicylic acid group.	Cadmium	98-100	oncomodulin	Homo sapiens	32-43
7628071-2	1995	DESIGN AND METHODS: A mutant of oncomodulin with a cysteine residue at position 57 located in the CD binding loop was conjugated to a salicylic acid group.	Salicylic Acid	134-148	oncomodulin	Homo sapiens	32-43
7827057-0	1995	Interconversion of the CD and EF sites in oncomodulin.	Cadmium	23-25	oncomodulin	Homo sapiens	42-53
7827057-7	1995	As in other parvalbumins, the liganding residues in the CD and EF sites of oncomodulin differ at the +z and -x coordination positions: serine and aspartate, respectively, in the CD site; aspartate and glycine in the EF site.	Cadmium	56-58	oncomodulin	Homo sapiens	75-86
7827057-7	1995	As in other parvalbumins, the liganding residues in the CD and EF sites of oncomodulin differ at the +z and -x coordination positions: serine and aspartate, respectively, in the CD site; aspartate and glycine in the EF site.	Serine	135-141	oncomodulin	Homo sapiens	75-86
7827057-7	1995	As in other parvalbumins, the liganding residues in the CD and EF sites of oncomodulin differ at the +z and -x coordination positions: serine and aspartate, respectively, in the CD site; aspartate and glycine in the EF site.	Aspartic Acid	146-155	oncomodulin	Homo sapiens	75-86
7827057-7	1995	As in other parvalbumins, the liganding residues in the CD and EF sites of oncomodulin differ at the +z and -x coordination positions: serine and aspartate, respectively, in the CD site; aspartate and glycine in the EF site.	Cadmium	178-180	oncomodulin	Homo sapiens	75-86
7827057-7	1995	As in other parvalbumins, the liganding residues in the CD and EF sites of oncomodulin differ at the +z and -x coordination positions: serine and aspartate, respectively, in the CD site; aspartate and glycine in the EF site.	Aspartic Acid	187-196	oncomodulin	Homo sapiens	75-86
7827057-7	1995	As in other parvalbumins, the liganding residues in the CD and EF sites of oncomodulin differ at the +z and -x coordination positions: serine and aspartate, respectively, in the CD site; aspartate and glycine in the EF site.	Glycine	201-208	oncomodulin	Homo sapiens	75-86
7827057-20	1995	In wild-type oncomodulin, the CD site signal dominates the low-pH spectrum.	Cadmium	30-32	oncomodulin	Homo sapiens	13-24
24233453-0	1994	Effects of metal ion binding on an oncomodulin mutant containing a novel calcium-binding loop.	Metals	11-16	oncomodulin	Homo sapiens	35-46
24233453-0	1994	Effects of metal ion binding on an oncomodulin mutant containing a novel calcium-binding loop.	Calcium	73-80	oncomodulin	Homo sapiens	35-46
24233453-1	1994	The Ca(2+)-binding protein oncomodulin was altered by cassette mutagenesis of the CD site (CDOM33) with a sequence that was derived by a consensus method using over 250 known Ca(2+)-binding loop sequences.	Cadmium	82-84	oncomodulin	Homo sapiens	27-38
24233453-6	1994	The Trp analogue, 5-hydroxytryptophan (5HW), was incorporated into both oncomodulin mutants to produce Y75(5HW) and 5HW-CDOM33.	Tryptophan	4-7	oncomodulin	Homo sapiens	72-83
24233453-6	1994	The Trp analogue, 5-hydroxytryptophan (5HW), was incorporated into both oncomodulin mutants to produce Y75(5HW) and 5HW-CDOM33.	5-Hydroxytryptophan	18-37	oncomodulin	Homo sapiens	72-83
24233453-6	1994	The Trp analogue, 5-hydroxytryptophan (5HW), was incorporated into both oncomodulin mutants to produce Y75(5HW) and 5HW-CDOM33.	5HW	39-42	oncomodulin	Homo sapiens	72-83
8489002-1	1993	In this study, the CD loop of the Ca(2+)-binding protein oncomodulin was replaced by a high-affinity, metal-binding sequence that was found to reverse the order of fill of the two sites in the protein.	Cadmium	19-21	oncomodulin	Homo sapiens	57-68
8054481-6	1994	We found that recombinant 6xHis-OncM remains fully active in a growth inhibition assay.	6xhis	26-31	oncomodulin	Homo sapiens	32-36
8489002-1	1993	In this study, the CD loop of the Ca(2+)-binding protein oncomodulin was replaced by a high-affinity, metal-binding sequence that was found to reverse the order of fill of the two sites in the protein.	Metals	102-107	oncomodulin	Homo sapiens	57-68
1333989-5	1992	Site-specific mutagenesis studies on the parvalbumin-like protein known as oncomodulin now suggest that the species in question is a liganding serine hydroxyl group.	serine hydroxyl	143-158	oncomodulin	Homo sapiens	75-86
2365679-0	1990	Comparison of metal ion-induced conformational changes in parvalbumin and oncomodulin as probed by the intrinsic fluorescence of tryptophan 102.	Metals	14-19	oncomodulin	Homo sapiens	74-85
1383030-1	1992	Biosynthetic incorporation of 5-hydroxytryptophan into oncomodulin.	5-Hydroxytryptophan	30-49	oncomodulin	Homo sapiens	55-66
1383030-3	1992	Here for the first time a method is reported for the biosynthetic incorporation of 5HW into an expressed protein, the Y57W mutant of the Ca2+ binding protein, oncomodulin.	5HW	83-86	oncomodulin	Homo sapiens	159-170
1618836-3	1992	The effect of changing the molecular environment around Tb3+ on its luminescence was studied using native Cod III parvalbumin and site-directed mutants of both oncomodulin and calmodulin.	tb3+	56-60	oncomodulin	Homo sapiens	160-171
1618836-5	1992	Tryptophan in binding loop position 7 best enhanced Tb3+ luminescence in the oncomodulin mutant Y57W, as well as VU-9 (F99W) and VU-32 (T26W) calmodulin.	Tryptophan	0-10	oncomodulin	Homo sapiens	77-88
1618836-6	1992	Excitation spectra of Y57F, F102W, Y65W oncomodulin, and Cod III parvalbumin revealed that the principal Tb3+ luminescence donor residues were phenylalanine or tyrosine located in position 7 of a loop, despite the presence of other nearby donors, including tryptophan.	tb3	105-108	oncomodulin	Homo sapiens	40-51
1618836-8	1992	An alternate binding loop, based on Tb3+ binding to model peptides, was inserted into the CD loop of oncomodulin by cassette mutagenesis.	tb3+	36-40	oncomodulin	Homo sapiens	101-112
1618836-11	1992	The mutant loop inserted into oncomodulin had 32 times more Tb3+ luminescence than the identical synthetic peptide, despite having the same donor tryptophan and metal binding ligands.	Peptides	107-114	oncomodulin	Homo sapiens	30-41
1618836-11	1992	The mutant loop inserted into oncomodulin had 32 times more Tb3+ luminescence than the identical synthetic peptide, despite having the same donor tryptophan and metal binding ligands.	Tryptophan	146-156	oncomodulin	Homo sapiens	30-41
1618836-11	1992	The mutant loop inserted into oncomodulin had 32 times more Tb3+ luminescence than the identical synthetic peptide, despite having the same donor tryptophan and metal binding ligands.	Metals	161-166	oncomodulin	Homo sapiens	30-41
1854760-0	1991	Metal-induced changes in the fluorescence properties of tyrosine and tryptophan site-specific mutants of oncomodulin.	Metals	0-5	oncomodulin	Homo sapiens	105-116
1854760-0	1991	Metal-induced changes in the fluorescence properties of tyrosine and tryptophan site-specific mutants of oncomodulin.	Tyrosine	56-64	oncomodulin	Homo sapiens	105-116
1854760-0	1991	Metal-induced changes in the fluorescence properties of tyrosine and tryptophan site-specific mutants of oncomodulin.	Tryptophan	69-79	oncomodulin	Homo sapiens	105-116
1854760-1	1991	Oncomodulin is a 108-residue, oncodevelopmental protein containing two calcium-binding sites identified as the CD- and EF-loops.	Calcium	71-78	oncomodulin	Homo sapiens	0-11
1854760-5	1991	Although both tyrosine residues responded to decalcification, the fluorescence intensity changes were in opposite directions, with the more dominant Tyr-57 accounting for the majority of the intrinsic fluorescence observed in native oncomodulin.	Tyrosine	149-152	oncomodulin	Homo sapiens	233-244
2365679-0	1990	Comparison of metal ion-induced conformational changes in parvalbumin and oncomodulin as probed by the intrinsic fluorescence of tryptophan 102.	Tryptophan	129-139	oncomodulin	Homo sapiens	74-85
2365679-1	1990	The calcium-induced conformational changes of the 108-amino acid residue proteins, cod III parvalbumin and oncomodulin, were compared using tryptophan as a sensitive spectroscopic probe.	Calcium	4-11	oncomodulin	Homo sapiens	107-118
2365679-2	1990	As native oncomodulin is devoid of tryptophan, site-specific mutagenesis was performed to create a mutant protein in which tryptophan was placed in the identical position (residue 102) as the single tryptophan residue in cod III parvalbumin.	Tryptophan	123-133	oncomodulin	Homo sapiens	10-21
2365679-2	1990	As native oncomodulin is devoid of tryptophan, site-specific mutagenesis was performed to create a mutant protein in which tryptophan was placed in the identical position (residue 102) as the single tryptophan residue in cod III parvalbumin.	Tryptophan	123-133	oncomodulin	Homo sapiens	10-21
2365679-10	1990	However, oncomodulin is distinct from cod III parvalbumin in terms of the electronic environment of the hydrophobic core, the magnitude of the Ca2(+)-induced conformational changes, and the number of calcium ions required to modulate the major conformational changes.	Calcium	200-207	oncomodulin	Homo sapiens	9-20
2351666-4	1990	Results obtained with the site-specific variant of oncomodulin known as D59E, in which glutamate replaces the aspartate naturally present at position 59, have necessitated substantial revision of these ideas.	Glutamic Acid	87-96	oncomodulin	Homo sapiens	51-62
2351666-4	1990	Results obtained with the site-specific variant of oncomodulin known as D59E, in which glutamate replaces the aspartate naturally present at position 59, have necessitated substantial revision of these ideas.	Aspartic Acid	110-119	oncomodulin	Homo sapiens	51-62
2108959-0	1990	Calcium- and magnesium-binding properties of oncomodulin.	Calcium	0-7	oncomodulin	Homo sapiens	45-56
2108959-0	1990	Calcium- and magnesium-binding properties of oncomodulin.	Magnesium	13-22	oncomodulin	Homo sapiens	45-56
2108959-11	1990	The characteristics of Ca2+ binding to the specific site (likely the CD domain) are different from those of the Ca2+ specific sites in troponin C and in calmodulin and suggest that in oncomodulin hydrophobic forces do not play a predominant role in the binding process at the specific site.	Cadmium	69-71	oncomodulin	Homo sapiens	184-195