PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
9588903-2	1998	Experimental autoimmune thyroiditis (EAT) with granulomatous histopathological features can be induced by mouse thyroglobulin (MTg)-sensitized spleen cells activated in vitro with MTg and anti-interleukin-2 receptor (anti-IL-2R), anti-IL-2, or anti-interferon-gamma (anti-IFN-gamma) monoclonal antibody (MAb).	(Methylthio)acetic acid	127-130	thyroglobulin	Mus musculus	112-125
7558173-0	1995	Proliferation and autoantibody production by mouse thyroglobulin (MTg)-specific B cells activated in vitro by MTg and MTg-specific T cells.	(Methylthio)acetic acid	66-69	thyroglobulin	Mus musculus	51-64
9344702-1	1997	A few synthetic peptides corresponding to amino acid sequences on human thyroglobulin (Tg) have been reported to induce moderate thyroiditis or activate mouse Tg (MTg)-primed T cells to transfer thyroiditis in mice susceptible to experimental autoimmune thyroiditis.	(Methylthio)acetic acid	163-166	thyroglobulin	Mus musculus	159-161
9184913-1	1997	Experimental autoimmune thyroiditis (EAT) can be induced by transfer of mouse thyroglobulin (MTg) and lipopolysaccharide (LPS)-immunized, MTg-activated spleen cells into syngeneic recipients.	(Methylthio)acetic acid	93-96	thyroglobulin	Mus musculus	78-91
7585972-1	1995	Experimental autoimmune thyroiditis (EAT) induced by the transfer of mouse thyroglobulin (MTg)-immunized spleen cells, activated in vitro with MTg, can be suppressed by oral administration of PTg to donor mice prior to immunization.	(Methylthio)acetic acid	90-93	thyroglobulin	Mus musculus	75-88
7585972-1	1995	Experimental autoimmune thyroiditis (EAT) induced by the transfer of mouse thyroglobulin (MTg)-immunized spleen cells, activated in vitro with MTg, can be suppressed by oral administration of PTg to donor mice prior to immunization.	Teniposide	192-195	thyroglobulin	Mus musculus	75-88
9451592-1	1997	Mouse thyroglobulin (MTg)-sensitized spleen cells activated in vitro with MTg can induce two histologically distinct forms of experimental autoimmune thyroiditis (EAT).	(Methylthio)acetic acid	21-24	thyroglobulin	Mus musculus	6-19
7558173-0	1995	Proliferation and autoantibody production by mouse thyroglobulin (MTg)-specific B cells activated in vitro by MTg and MTg-specific T cells.	(Methylthio)acetic acid	110-113	thyroglobulin	Mus musculus	51-64
7558173-1	1995	Immunization of genetically susceptible strains of mice with mouse thyroglobulin (MTg) and adjuvant results in sensitization of MTg-specific CD4+ T cells that can induce experimental autoimmune thyroiditis (EAT) after in vitro activation with MTg.	(Methylthio)acetic acid	82-85	thyroglobulin	Mus musculus	67-80
7558173-1	1995	Immunization of genetically susceptible strains of mice with mouse thyroglobulin (MTg) and adjuvant results in sensitization of MTg-specific CD4+ T cells that can induce experimental autoimmune thyroiditis (EAT) after in vitro activation with MTg.	(Methylthio)acetic acid	128-131	thyroglobulin	Mus musculus	67-80
7558173-1	1995	Immunization of genetically susceptible strains of mice with mouse thyroglobulin (MTg) and adjuvant results in sensitization of MTg-specific CD4+ T cells that can induce experimental autoimmune thyroiditis (EAT) after in vitro activation with MTg.	(Methylthio)acetic acid	128-131	thyroglobulin	Mus musculus	67-80
34552555-13	2021	Our results strongly suggest that primary cilia harbors LRP2/megalin, and are involved in TSH-mediated endocytosis of Tg in murine thyroid follicles.	Thyrotropin	90-93	thyroglobulin	Mus musculus	118-120
7511888-1	1994	There is evidence from animal models that the iodine content of thyroglobulin (Tg) may influence its antigenicity in thyroid autoimmunity.	Iodine	46-52	thyroglobulin	Mus musculus	64-77
1517579-1	1992	Experimental autoimmune thyroiditis (EAT) can be induced in mice after the transfer of mouse thyroglobulin (MTg)-sensitized donor spleen cells that have been activated in vitro with MTg.	(Methylthio)acetic acid	108-111	thyroglobulin	Mus musculus	93-106
1643752-1	1992	We have used the mouse model of experimental autoimmune thyroiditis (EAT) to examine the hypothesis that the strengthening of self-tolerance to thyroglobulin by exogenous mouse thyroglobulin (MTg) or stimulation of endogenous MTg secretion by thyroid-stimulating hormone (TSH) is correlated with the length of time MTg rises above the normal range.	Thyrotropin	243-270	thyroglobulin	Mus musculus	144-157
1643752-1	1992	We have used the mouse model of experimental autoimmune thyroiditis (EAT) to examine the hypothesis that the strengthening of self-tolerance to thyroglobulin by exogenous mouse thyroglobulin (MTg) or stimulation of endogenous MTg secretion by thyroid-stimulating hormone (TSH) is correlated with the length of time MTg rises above the normal range.	Thyrotropin	272-275	thyroglobulin	Mus musculus	144-157
1672546-1	1991	Spleen cells from CBA/J mice immunized with mouse thyroglobulin (MTg) and the adjuvant lipopolysaccharide induce experimental autoimmune thyroiditis (EAT) after transfer to recipient mice if they are first activated in vitro with MTg.	(Methylthio)acetic acid	65-68	thyroglobulin	Mus musculus	50-63
1672546-1	1991	Spleen cells from CBA/J mice immunized with mouse thyroglobulin (MTg) and the adjuvant lipopolysaccharide induce experimental autoimmune thyroiditis (EAT) after transfer to recipient mice if they are first activated in vitro with MTg.	(Methylthio)acetic acid	230-233	thyroglobulin	Mus musculus	50-63
2564328-1	1989	Mechanisms suppressive to induction of murine experimental autoimmune thyroiditis (EAT) can be activated by pretreatment with tolerogenic doses of mouse thyroglobulin (MTg) or prior TSH infusion to raise circulatory MTg levels.	(Methylthio)acetic acid	168-171	thyroglobulin	Mus musculus	153-166
3488488-4	1986	It appears that only these T lymphoblasts sensitized on thyroid monolayers are specifically labelled by fluorescein-conjugated thyroglobulin.	Fluorescein	104-115	thyroglobulin	Mus musculus	127-140
2924725-6	1989	Sucrose density gradient velocity centrifugation followed by RIA was used to determine the sedimentation properties of cog/cog TG.	Sucrose	0-7	thyroglobulin	Mus musculus	127-129
2924725-13	1989	However, by polyacrylamide gradient gel electrophoresis, distinct 125I-labeled bands comigrating with normal TG were present.	Iodine-125	66-70	thyroglobulin	Mus musculus	109-111
2924725-16	1989	With [35S]methionine labeling, cog/cog and +/cog thyroids formed TG with the same electrophoretic mobilities.	Sulfur-35	6-9	thyroglobulin	Mus musculus	65-67
2924725-16	1989	With [35S]methionine labeling, cog/cog and +/cog thyroids formed TG with the same electrophoretic mobilities.	Methionine	10-20	thyroglobulin	Mus musculus	65-67
3197917-1	1988	Mouse 330 kDa thyroglobulin labeled in vivo was analyzed using a tryptic peptide mapping technique and high performance liquid chromatography (HPLC).	Peptides	73-80	thyroglobulin	Mus musculus	14-27
3197917-5	1988	These data indicate that there is some preferential iodination site(s) within the thyroglobulin molecule and also that their iodoamino acid composition is predetermined.	iodoamino acid	125-139	thyroglobulin	Mus musculus	82-95
3802208-1	1986	Experimental autoimmune thyroiditis (EAT) can be induced in susceptible strains of mice by injection of mouse thyroglobulin (MTg) and adjuvant.	(Methylthio)acetic acid	125-128	thyroglobulin	Mus musculus	110-123
2902931-1	1988	Experimental autoimmune thyroiditis (EAT) can be induced in CBA/J mice following the transfer of spleen cells from mouse thyroglobulin (MTg)-sensitized donors that have been activated in vitro with MTg.	(Methylthio)acetic acid	136-139	thyroglobulin	Mus musculus	121-134
3416995-0	1988	Release of 3,5,3"-triiodothyronine, thyroxine and thyroglobulin from TSH-stimulated mouse thyroids in the perifusion system.	Thyrotropin	69-72	thyroglobulin	Mus musculus	50-63
3873286-1	1985	Spleen cells from CBA/J or SJL mice sensitized with mouse thyroglobulin (MTg) and lipopolysaccharide (LPS) could be activated in vitro with MTg to transfer experimental autoimmune thyroiditis (EAT) to normal syngeneic recipients.	(Methylthio)acetic acid	73-76	thyroglobulin	Mus musculus	58-71
3516644-4	1986	The main factors known to affect diffusion of Tgb in the colloid space are concentration and actual physico-chemical properties of the Tgb molecule itself, the latter parameter depending on several factors such as sugar content, iodination degree, etc.	Sugars	214-219	thyroglobulin	Mus musculus	46-49
3516644-5	1986	Additional factors are thyrotropin which speeds up and drugs such as pentobarbital or verapamil which slow down the velocity of Tgb diffusion.	Pentobarbital	69-82	thyroglobulin	Mus musculus	128-131
3516644-5	1986	Additional factors are thyrotropin which speeds up and drugs such as pentobarbital or verapamil which slow down the velocity of Tgb diffusion.	Verapamil	86-95	thyroglobulin	Mus musculus	128-131
3516644-6	1986	High iodine supply has a retarding effect on Tgb diffusion in the colloid of mice thyroids.	Iodine	5-11	thyroglobulin	Mus musculus	45-48
3873286-1	1985	Spleen cells from CBA/J or SJL mice sensitized with mouse thyroglobulin (MTg) and lipopolysaccharide (LPS) could be activated in vitro with MTg to transfer experimental autoimmune thyroiditis (EAT) to normal syngeneic recipients.	(Methylthio)acetic acid	140-143	thyroglobulin	Mus musculus	58-71
6205252-0	1984	Monoclonal antibodies to hog thyroglobulin recognizing disulfide-dependent conformational structures.	Disulfides	55-64	thyroglobulin	Mus musculus	29-42
6424911-2	1984	These images give new information related to iodine and sulfur load of thyroglobulin and to the intensity of iodine concentration in lysosomes of thyroid cells.	Sulfur	56-62	thyroglobulin	Mus musculus	71-84
7021024-2	1981	Autoantibody to thyroglobulin (Tg) induced by immunization with cross-reactive xenogeneic Tg in Freund"s complete adjuvant and autoerythrocyte antibody induced by the injection of xenogeneic erythrocytes were studied in C57Bl/6 and BALB/c male mice.	freund"s	96-104	thyroglobulin	Mus musculus	16-29
7430900-5	1980	Thyrotrophin (TSH) increased the rate of thyroglobulin hydrolysis and hormone release from both pools by up to four to six times the basal rate, the effect being maximal 2 h after administration of TSH and lasting for 6-8 h. The rate of thyroglobulin hydrolysis after TSH was similar in both pools but the rate of release of labelled iodothyronines was significantly higher from from the old pool.	Thyrotropin	14-17	thyroglobulin	Mus musculus	41-54
7430900-5	1980	Thyrotrophin (TSH) increased the rate of thyroglobulin hydrolysis and hormone release from both pools by up to four to six times the basal rate, the effect being maximal 2 h after administration of TSH and lasting for 6-8 h. The rate of thyroglobulin hydrolysis after TSH was similar in both pools but the rate of release of labelled iodothyronines was significantly higher from from the old pool.	Thyrotropin	14-17	thyroglobulin	Mus musculus	237-250
7430900-5	1980	Thyrotrophin (TSH) increased the rate of thyroglobulin hydrolysis and hormone release from both pools by up to four to six times the basal rate, the effect being maximal 2 h after administration of TSH and lasting for 6-8 h. The rate of thyroglobulin hydrolysis after TSH was similar in both pools but the rate of release of labelled iodothyronines was significantly higher from from the old pool.	iodothyronines	334-348	thyroglobulin	Mus musculus	41-54
26158397-4	2015	Guided by the hypothalamus-pituitary-thyroid axis as a fixed set-point regulator in thyroid hormone metabolism, we used a murine model and compared at key junctures the capacity of circulating thyroglobulin level (raised by thyroid-stimulating hormone or exogenous thyroglobulin administration) to strengthen self-tolerance and resist autoimmune thyroiditis.	Thyrotropin	224-251	thyroglobulin	Mus musculus	193-206
730552-6	1978	This phenomenon indicates that the Golgi apparatus has a functional polarity for the addition of carbohydrates to thyroglobulin and other proteins.	Carbohydrates	97-110	thyroglobulin	Mus musculus	114-127
323406-1	1977	The administration of soluble mouse thyroglobulin (MTg) in conjunction with bacterial lipopolysaccharide (LPS) led to the termination of natural tolerance to MTg in mice.	(Methylthio)acetic acid	51-54	thyroglobulin	Mus musculus	36-49
32961913-1	2020	BACKGROUND: Thyroid follicular cells have physiologically high levels of reactive oxygen species because oxidation of iodide is essential for the iodination of thyroglobulin (Tg) during thyroid hormone synthesis.	Oxygen	82-88	thyroglobulin	Mus musculus	160-173
32961913-1	2020	BACKGROUND: Thyroid follicular cells have physiologically high levels of reactive oxygen species because oxidation of iodide is essential for the iodination of thyroglobulin (Tg) during thyroid hormone synthesis.	Iodides	118-124	thyroglobulin	Mus musculus	160-173
20687399-0	2010	Iodine content of thyroglobulin in Nod.H2h4 mice developing iodine-accelerated autoimmune thyroiditis.	Iodine	0-6	thyroglobulin	Mus musculus	18-31
24879795-0	2014	The thyroxine-containing thyroglobulin peptide (aa 2549-2560) is a target epitope in iodide-accelerated spontaneous autoimmune thyroiditis.	Iodides	85-91	thyroglobulin	Mus musculus	25-38
24879795-3	2014	In this study, we show that the previously identified thyroglobulin (Tg) T cell epitope p2549-2560 containing thyroxine at position 2553 (T4p2553) induces thyroiditis as well as strong specific T and B cell responses in NOD.H2(h4) mice.	Thyroxine	110-119	thyroglobulin	Mus musculus	54-67
20943721-7	2011	Furthermore, the extent and duration of radioiodine accumulation stimulated by bTSH was less in the thyroids of the thyroid-targeted RET/PTC1 (thyroglobulin (Tg)-PTC1) mice bearing thyroid tumors compared with the thyroids in wild-type (WT) mice.	Iodine-131	40-51	thyroglobulin	Mus musculus	143-156
25101840-7	2014	Low-dose treatment of TBTCl exposure markedly decreased the serum thyroid hormone levels via the down-regulation of the thyroid peroxidase (TPO) and thyroglobulin (Tg) genes by 40% and 25%, respectively, while augmenting the thyroid stimulating hormone (TSH) levels.	tributyltin	22-27	thyroglobulin	Mus musculus	149-162
24395757-1	2014	We have created a mouse model expressing tamoxifen-inducible Cre recombinase (CreER(T2) ) under the control of the thyroglobulin (Tg) gene promoter to be able to study the role of defined genetic modifications in the regulation of thyroid function.	Tamoxifen	41-50	thyroglobulin	Mus musculus	115-128
24098053-1	2013	NOD.H-2h4 mice given NaI in their drinking water develop iodine-accelerated spontaneous autoimmune thyroiditis (ISAT) with chronic inflammation of the thyroid by T and B cells and production of anti-mouse thyroglobulin (MTg) autoantibody.	Sodium Iodide	21-24	thyroglobulin	Mus musculus	205-218
23360087-2	2013	The thyroid transcription factors-NKx2 homeobox 1 (NKx2-1, formerly called TTF-1) and Paired box gene 8 (Pax8)-are known to associate biochemically and synergistically in the activation of thyroid functional genes including the sodium/iodide symporter (NIS), thyrotropin (TSH) receptor (TSHR), thyroglobulin (Tg), and thyroid peroxidase (TPO) genes.	Sodium	228-234	thyroglobulin	Mus musculus	294-307
23360087-2	2013	The thyroid transcription factors-NKx2 homeobox 1 (NKx2-1, formerly called TTF-1) and Paired box gene 8 (Pax8)-are known to associate biochemically and synergistically in the activation of thyroid functional genes including the sodium/iodide symporter (NIS), thyrotropin (TSH) receptor (TSHR), thyroglobulin (Tg), and thyroid peroxidase (TPO) genes.	Sodium	228-234	thyroglobulin	Mus musculus	309-311
23360087-2	2013	The thyroid transcription factors-NKx2 homeobox 1 (NKx2-1, formerly called TTF-1) and Paired box gene 8 (Pax8)-are known to associate biochemically and synergistically in the activation of thyroid functional genes including the sodium/iodide symporter (NIS), thyrotropin (TSH) receptor (TSHR), thyroglobulin (Tg), and thyroid peroxidase (TPO) genes.	Iodides	235-241	thyroglobulin	Mus musculus	294-307
23360087-2	2013	The thyroid transcription factors-NKx2 homeobox 1 (NKx2-1, formerly called TTF-1) and Paired box gene 8 (Pax8)-are known to associate biochemically and synergistically in the activation of thyroid functional genes including the sodium/iodide symporter (NIS), thyrotropin (TSH) receptor (TSHR), thyroglobulin (Tg), and thyroid peroxidase (TPO) genes.	Iodides	235-241	thyroglobulin	Mus musculus	309-311
23360087-2	2013	The thyroid transcription factors-NKx2 homeobox 1 (NKx2-1, formerly called TTF-1) and Paired box gene 8 (Pax8)-are known to associate biochemically and synergistically in the activation of thyroid functional genes including the sodium/iodide symporter (NIS), thyrotropin (TSH) receptor (TSHR), thyroglobulin (Tg), and thyroid peroxidase (TPO) genes.	Nickel	253-256	thyroglobulin	Mus musculus	294-307
23360087-2	2013	The thyroid transcription factors-NKx2 homeobox 1 (NKx2-1, formerly called TTF-1) and Paired box gene 8 (Pax8)-are known to associate biochemically and synergistically in the activation of thyroid functional genes including the sodium/iodide symporter (NIS), thyrotropin (TSH) receptor (TSHR), thyroglobulin (Tg), and thyroid peroxidase (TPO) genes.	Nickel	253-256	thyroglobulin	Mus musculus	309-311
20687399-0	2010	Iodine content of thyroglobulin in Nod.H2h4 mice developing iodine-accelerated autoimmune thyroiditis.	h2h4	39-43	thyroglobulin	Mus musculus	18-31
20687399-0	2010	Iodine content of thyroglobulin in Nod.H2h4 mice developing iodine-accelerated autoimmune thyroiditis.	Iodine	60-66	thyroglobulin	Mus musculus	18-31
20687399-2	2010	The aim of the study was to examine whether the NOD.H2h4 genetic background predisposes to enhanced iodine organification in thyroglobulin (Tg), a target autoantigen in ISAT.	h2h4	52-56	thyroglobulin	Mus musculus	125-138
20687399-2	2010	The aim of the study was to examine whether the NOD.H2h4 genetic background predisposes to enhanced iodine organification in thyroglobulin (Tg), a target autoantigen in ISAT.	h2h4	52-56	thyroglobulin	Mus musculus	140-142
20687399-2	2010	The aim of the study was to examine whether the NOD.H2h4 genetic background predisposes to enhanced iodine organification in thyroglobulin (Tg), a target autoantigen in ISAT.	Iodine	100-106	thyroglobulin	Mus musculus	125-138
20687399-2	2010	The aim of the study was to examine whether the NOD.H2h4 genetic background predisposes to enhanced iodine organification in thyroglobulin (Tg), a target autoantigen in ISAT.	Iodine	100-106	thyroglobulin	Mus musculus	140-142
20687399-4	2010	Additionally, we tested whether humoral or cellular immune responses of iodine-fed NOD.H2h4 mice are preferentially directed to Tg with increased iodine content (I-Tg) or known pathogenic Tg peptides that contained iodine.	Iodine	72-78	thyroglobulin	Mus musculus	128-130
20687399-4	2010	Additionally, we tested whether humoral or cellular immune responses of iodine-fed NOD.H2h4 mice are preferentially directed to Tg with increased iodine content (I-Tg) or known pathogenic Tg peptides that contained iodine.	Iodine	72-78	thyroglobulin	Mus musculus	164-166
20687399-4	2010	Additionally, we tested whether humoral or cellular immune responses of iodine-fed NOD.H2h4 mice are preferentially directed to Tg with increased iodine content (I-Tg) or known pathogenic Tg peptides that contained iodine.	Iodine	72-78	thyroglobulin	Mus musculus	164-166
20687399-4	2010	Additionally, we tested whether humoral or cellular immune responses of iodine-fed NOD.H2h4 mice are preferentially directed to Tg with increased iodine content (I-Tg) or known pathogenic Tg peptides that contained iodine.	h2h4	87-91	thyroglobulin	Mus musculus	128-130
20687399-4	2010	Additionally, we tested whether humoral or cellular immune responses of iodine-fed NOD.H2h4 mice are preferentially directed to Tg with increased iodine content (I-Tg) or known pathogenic Tg peptides that contained iodine.	h2h4	87-91	thyroglobulin	Mus musculus	164-166
20687399-4	2010	Additionally, we tested whether humoral or cellular immune responses of iodine-fed NOD.H2h4 mice are preferentially directed to Tg with increased iodine content (I-Tg) or known pathogenic Tg peptides that contained iodine.	h2h4	87-91	thyroglobulin	Mus musculus	164-166
20687399-5	2010	RESULTS: The iodine content of Tg was not significantly different between control (9.0 +/- 2.7 I atoms per monomer) and iodine-fed mice (10.9 +/- 0.3 I atoms per monomer).	Iodine	13-19	thyroglobulin	Mus musculus	31-33
20687399-6	2010	Furthermore, in iodine-fed NOD.H2h4 mice developing ISAT, strong but equivalent serum IgG responses were detected to both Tg or I-Tg, whereas their lymphoid cells were stimulated weakly but equally well by Tg or I-Tg in vitro and did not show reactivity against a panel of five pathogenic Tg peptides that contained iodine.	Iodine	16-22	thyroglobulin	Mus musculus	122-124
20687399-6	2010	Furthermore, in iodine-fed NOD.H2h4 mice developing ISAT, strong but equivalent serum IgG responses were detected to both Tg or I-Tg, whereas their lymphoid cells were stimulated weakly but equally well by Tg or I-Tg in vitro and did not show reactivity against a panel of five pathogenic Tg peptides that contained iodine.	Iodine	16-22	thyroglobulin	Mus musculus	130-132
20687399-6	2010	Furthermore, in iodine-fed NOD.H2h4 mice developing ISAT, strong but equivalent serum IgG responses were detected to both Tg or I-Tg, whereas their lymphoid cells were stimulated weakly but equally well by Tg or I-Tg in vitro and did not show reactivity against a panel of five pathogenic Tg peptides that contained iodine.	Iodine	16-22	thyroglobulin	Mus musculus	130-132
20687399-6	2010	Furthermore, in iodine-fed NOD.H2h4 mice developing ISAT, strong but equivalent serum IgG responses were detected to both Tg or I-Tg, whereas their lymphoid cells were stimulated weakly but equally well by Tg or I-Tg in vitro and did not show reactivity against a panel of five pathogenic Tg peptides that contained iodine.	Iodine	16-22	thyroglobulin	Mus musculus	130-132
20687399-6	2010	Furthermore, in iodine-fed NOD.H2h4 mice developing ISAT, strong but equivalent serum IgG responses were detected to both Tg or I-Tg, whereas their lymphoid cells were stimulated weakly but equally well by Tg or I-Tg in vitro and did not show reactivity against a panel of five pathogenic Tg peptides that contained iodine.	Iodine	16-22	thyroglobulin	Mus musculus	130-132
20687399-6	2010	Furthermore, in iodine-fed NOD.H2h4 mice developing ISAT, strong but equivalent serum IgG responses were detected to both Tg or I-Tg, whereas their lymphoid cells were stimulated weakly but equally well by Tg or I-Tg in vitro and did not show reactivity against a panel of five pathogenic Tg peptides that contained iodine.	Iodine	52-53	thyroglobulin	Mus musculus	122-124
16547286-0	2006	Iodination of tyrosyls in thyroglobulin generates neoantigenic determinants that cause thyroiditis.	tyrosyls	14-22	thyroglobulin	Mus musculus	26-39
19845793-1	2010	Granulomatous experimental autoimmune thyroiditis (G-EAT) is induced by mouse thyroglobulin (MTg)-sensitized splenocytes activated with MTg and interleukin (IL)-12.	(Methylthio)acetic acid	93-96	thyroglobulin	Mus musculus	78-91
18810759-1	2008	Granulomatous experimental autoimmune thyroiditis (G-EAT) is induced by mouse thyroglobulin (MTG)-sensitized splenocytes activated in vitro with MTG and IL-12.	(Methylthio)acetic acid	93-96	thyroglobulin	Mus musculus	78-91
16547286-5	2006	These results demonstrate that iodotyrosyl formation in normal Tg confers pathogenic potential to certain peptides that may otherwise remain innocuous and undetectable by conventional mapping methods.	iodotyrosyl	31-42	thyroglobulin	Mus musculus	63-65
16547286-1	2006	Thyroglobulin (Tg) is unique in its ability to incorporate and store available iodine in the form of iodotyrosyl residues.	Iodine	79-85	thyroglobulin	Mus musculus	0-13
16547286-1	2006	Thyroglobulin (Tg) is unique in its ability to incorporate and store available iodine in the form of iodotyrosyl residues.	Iodine	79-85	thyroglobulin	Mus musculus	15-17
16547286-1	2006	Thyroglobulin (Tg) is unique in its ability to incorporate and store available iodine in the form of iodotyrosyl residues.	iodotyrosyl	101-112	thyroglobulin	Mus musculus	0-13
16547286-1	2006	Thyroglobulin (Tg) is unique in its ability to incorporate and store available iodine in the form of iodotyrosyl residues.	iodotyrosyl	101-112	thyroglobulin	Mus musculus	15-17
16547286-2	2006	Iodination of Tg has been known to increase its immunopathogenicity in experimental animals, presumably through the formation of iodine-containing neoantigenic determinants that can elicit an autoimmune response, but defined pathogenic Tg peptides carrying iodotyrosyls have not yet been identified.	Iodine	129-135	thyroglobulin	Mus musculus	14-16
16547286-2	2006	Iodination of Tg has been known to increase its immunopathogenicity in experimental animals, presumably through the formation of iodine-containing neoantigenic determinants that can elicit an autoimmune response, but defined pathogenic Tg peptides carrying iodotyrosyls have not yet been identified.	iodotyrosyls	257-269	thyroglobulin	Mus musculus	14-16
16306076-8	2006	Enhanced 125I- efflux upon perchlorate and presence of 125I-Tg as autoradiographic rings at follicle periphery demonstrated delayed iodide organification.	Iodides	132-138	thyroglobulin	Mus musculus	60-62
10502541-12	1999	The disease, moreover, can be transferred adoptively, using spleen cells from iodine-fed donors treated in vitro with iodinated thyroglobulin.	Iodine	78-84	thyroglobulin	Mus musculus	128-141
11099302-1	2000	Experimental autoimmune thyroiditis (EAT) with granulomatous histopathology (G-EAT) can be induced by cells from mouse thyroglobulin (MTg)-immunized donors activated in vitro with MTg and IL-12.	(Methylthio)acetic acid	134-137	thyroglobulin	Mus musculus	119-132
11099302-1	2000	Experimental autoimmune thyroiditis (EAT) with granulomatous histopathology (G-EAT) can be induced by cells from mouse thyroglobulin (MTg)-immunized donors activated in vitro with MTg and IL-12.	(Methylthio)acetic acid	180-183	thyroglobulin	Mus musculus	119-132
16084270-4	2005	A mild form of EAT was induced by subcutaneous injection of mouse thyroglobulin (MTg) with either Freund"s adjuvant (complete and incomplete, CFA and IFA) or lipopolysaccharide (LPS).	(Methylthio)acetic acid	81-84	thyroglobulin	Mus musculus	66-79
15878230-4	2005	As expected from the knowledge that megalin mediates Tg transcytosis, serum Tg levels were significantly reduced in homozygous (megalin-/-) mice, which, more importantly, were found to be hypothyroid, as demonstrated by significantly reduced serum free thyroxine and significantly increased serum thyroid stimulating hormone (TSH) levels.	Thyroxine	253-262	thyroglobulin	Mus musculus	76-78
15878230-4	2005	As expected from the knowledge that megalin mediates Tg transcytosis, serum Tg levels were significantly reduced in homozygous (megalin-/-) mice, which, more importantly, were found to be hypothyroid, as demonstrated by significantly reduced serum free thyroxine and significantly increased serum thyroid stimulating hormone (TSH) levels.	Thyrotropin	326-329	thyroglobulin	Mus musculus	76-78
15728526-2	2005	We report that a THB mAb recognizing the 5" iodine atom of the outer phenolic ring of thyroxine (T4) can block T cell recognition of the pathogenic thyroglobulin (Tg) peptide (2549-2560) that contains T4 at aa position 2553 (T4(2553)).	Sapropterin	17-20	thyroglobulin	Mus musculus	148-161
15728526-2	2005	We report that a THB mAb recognizing the 5" iodine atom of the outer phenolic ring of thyroxine (T4) can block T cell recognition of the pathogenic thyroglobulin (Tg) peptide (2549-2560) that contains T4 at aa position 2553 (T4(2553)).	Iodine	44-50	thyroglobulin	Mus musculus	148-161
15728526-2	2005	We report that a THB mAb recognizing the 5" iodine atom of the outer phenolic ring of thyroxine (T4) can block T cell recognition of the pathogenic thyroglobulin (Tg) peptide (2549-2560) that contains T4 at aa position 2553 (T4(2553)).	Thyroxine	86-95	thyroglobulin	Mus musculus	148-161
14764582-1	2004	Secretion of thyroglobulin (Tg, a large homodimeric glycoprotein) is essential to deliver Tg to its site of iodination for thyroxine biosynthesis.	Thyroxine	123-132	thyroglobulin	Mus musculus	13-26
14764582-1	2004	Secretion of thyroglobulin (Tg, a large homodimeric glycoprotein) is essential to deliver Tg to its site of iodination for thyroxine biosynthesis.	Thyroxine	123-132	thyroglobulin	Mus musculus	28-30
14764582-1	2004	Secretion of thyroglobulin (Tg, a large homodimeric glycoprotein) is essential to deliver Tg to its site of iodination for thyroxine biosynthesis.	Thyroxine	123-132	thyroglobulin	Mus musculus	90-92
12023396-2	2002	One hypothesis has been that enhanced incorporation of iodine in thyroglobulin (Tg) promotes the generation of pathogenic T cell determinants.	Iodine	55-61	thyroglobulin	Mus musculus	65-78
11466396-1	2001	Granulomatous experimental autoimmune thyroiditis (G-EAT) is induced by transfer of mouse thyroglobulin (MTg)-sensitized spleen cells activated in vitro with MTg and anti-IL-2R or MTg and IL-12.	(Methylthio)acetic acid	105-108	thyroglobulin	Mus musculus	90-103
11466396-1	2001	Granulomatous experimental autoimmune thyroiditis (G-EAT) is induced by transfer of mouse thyroglobulin (MTg)-sensitized spleen cells activated in vitro with MTg and anti-IL-2R or MTg and IL-12.	(Methylthio)acetic acid	158-161	thyroglobulin	Mus musculus	90-103
11453662-6	2001	Tg, but not triiodothyronine (T(3)) significantly increased MC proliferation above control as determined by DNA content of MC cultures.	Methylcholanthrene	60-62	thyroglobulin	Mus musculus	0-2
11453662-6	2001	Tg, but not triiodothyronine (T(3)) significantly increased MC proliferation above control as determined by DNA content of MC cultures.	Methylcholanthrene	123-125	thyroglobulin	Mus musculus	0-2
11129114-1	2000	Experimental autoimmune thyroiditis (EAT) is a chronic inflammatory autoimmune disease that can be induced in genetically susceptible animals by immunization with mouse thyroglobulin (MTg) in an appropriate adjuvant or by the adoptive transfer of MTg-sensitized donor spleen cells, activated in vitro with MTg, into naive recipients.	(Methylthio)acetic acid	184-187	thyroglobulin	Mus musculus	169-182
10502541-14	1999	Based on T-cell proliferation, it appears that the NOD-H2(h4) strain of mice has innately a greater response to murine thyroglobulin than do other mouse strains and that the proliferation is increased even more by feeding iodine.	Iodine	222-228	thyroglobulin	Mus musculus	119-132
10502541-15	1999	We suggest, therefore, that the presence of iodine increases the autoantigenic potency of thyroglobulin, a major pathogenic antigen in the induction of autoimmune thyroiditis.	Iodine	44-50	thyroglobulin	Mus musculus	90-103
10358139-2	1999	Here we show that generation of the nondominant pathogenic Tg epitope (2549-2560), containing thyroxine (T4) at position 2553 (T4(2553)), is augmented by Tg-specific IgG mAbs that facilitate FcR-mediated internalization of Tg.	Thyroxine	94-103	thyroglobulin	Mus musculus	154-156
10447778-5	1999	We report that, in contrast to the previous findings, this antibody had an exacerbating effect on thyroiditis induced by immunization of mice with mouse thyroglobulin (MTg) and complete Freund"s adjuvant (CFA).	(Methylthio)acetic acid	168-171	thyroglobulin	Mus musculus	153-166
10450830-0	1999	Hexamethylene bisacetamide (HMBA) increases thyroglobulin levels in porcine thyroid cells without increasing cyclic-AMP.	hexamethylene bisacetamide	0-26	thyroglobulin	Mus musculus	44-57
10450830-0	1999	Hexamethylene bisacetamide (HMBA) increases thyroglobulin levels in porcine thyroid cells without increasing cyclic-AMP.	hexamethylene bisacetamide	28-32	thyroglobulin	Mus musculus	44-57
10358139-2	1999	Here we show that generation of the nondominant pathogenic Tg epitope (2549-2560), containing thyroxine (T4) at position 2553 (T4(2553)), is augmented by Tg-specific IgG mAbs that facilitate FcR-mediated internalization of Tg.	Thyroxine	94-103	thyroglobulin	Mus musculus	59-61
10358139-2	1999	Here we show that generation of the nondominant pathogenic Tg epitope (2549-2560), containing thyroxine (T4) at position 2553 (T4(2553)), is augmented by Tg-specific IgG mAbs that facilitate FcR-mediated internalization of Tg.	Thyroxine	94-103	thyroglobulin	Mus musculus	154-156
10028017-1	1999	The interaction of CD40 on antigen presenting cells (APC) with CD40L on mouse thyroglobulin (MTg)-specific T cells may deliver an essential signal for the development of CD4(+) experimental autoimmune thyroiditis (EAT) effector cells and anti-MTg producing B cells.	(Methylthio)acetic acid	93-96	thyroglobulin	Mus musculus	78-91
10650339-0	1999	Hexamethylenebisacetamide modulation of thyroglobulin and protein levels in thyroid cells is not mediated by phosphatidylinositol-3-kinase: a study with wortmannin.	hexamethylene bisacetamide	0-25	thyroglobulin	Mus musculus	40-53
9707574-6	1998	Comparison of the complete sequences reveals that cog/cog mice express a Leu-2263 --> Pro missense mutation in the acetylcholinesterase-homology domain of Tg.	Leucine	73-76	thyroglobulin	Mus musculus	158-160
9707574-8	1998	Site-directed mutagenesis of cog Tg to convert the single amino acid back to Leu-2263 restores normal Tg secretion.	Leucine	77-80	thyroglobulin	Mus musculus	33-35
9707574-8	1998	Site-directed mutagenesis of cog Tg to convert the single amino acid back to Leu-2263 restores normal Tg secretion.	Leucine	77-80	thyroglobulin	Mus musculus	102-104