PubMed:8163464 JSONTXT

{"project":"sentences","denotations":[{"id":"T1","span":{"begin":0,"end":64},"obj":"Sentence"},{"id":"T2","span":{"begin":65,"end":108},"obj":"Sentence"},{"id":"T3","span":{"begin":109,"end":236},"obj":"Sentence"},{"id":"T4","span":{"begin":237,"end":429},"obj":"Sentence"},{"id":"T5","span":{"begin":430,"end":672},"obj":"Sentence"},{"id":"T6","span":{"begin":673,"end":834},"obj":"Sentence"},{"id":"T7","span":{"begin":835,"end":939},"obj":"Sentence"},{"id":"T8","span":{"begin":940,"end":1044},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":64},"obj":"Sentence"},{"id":"T2","span":{"begin":65,"end":108},"obj":"Sentence"},{"id":"T3","span":{"begin":109,"end":236},"obj":"Sentence"},{"id":"T4","span":{"begin":237,"end":429},"obj":"Sentence"},{"id":"T5","span":{"begin":430,"end":672},"obj":"Sentence"},{"id":"T6","span":{"begin":673,"end":834},"obj":"Sentence"},{"id":"T7","span":{"begin":835,"end":939},"obj":"Sentence"},{"id":"T8","span":{"begin":940,"end":1044},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"A novel heterodimerization partner for thyroid hormone receptor. Peroxisome proliferator-activated receptor.\nRetinoid-like receptors play a central role in hormonal responses by forming heterodimers with other nuclear hormone receptors. In this study we have identified the peroxisome proliferator-activated receptor (PPAR) as a new thyroid hormone receptor (THR) auxiliary nuclear protein, heterodimerizing with THR in solution. Although these heterodimers do not recognize a classical thyroid hormone response element (TRE) characterized by direct repeat separated by four nucleotides (DR+4), PPAR behaves as a dominant negative regulator of thyroid hormone (TH) action. However, a TH-dependent positive effect is elicited by selective interaction of the THR beta-PPAR but not the THR alpha-PPAR heterodimer with a novel TRE (DR+2). The critical region of THR beta was mapped to 3 amino acids in the distal box of the DNA binding domain. Hence, PPAR can positively or negatively influence TH action depending on TRE structure and THR isotype."}

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":39,"end":46},"obj":"http://purl.obolibrary.org/obo/MAT_0000081"},{"id":"T2","span":{"begin":333,"end":340},"obj":"http://purl.obolibrary.org/obo/MAT_0000081"},{"id":"T3","span":{"begin":487,"end":494},"obj":"http://purl.obolibrary.org/obo/MAT_0000081"},{"id":"T4","span":{"begin":644,"end":651},"obj":"http://purl.obolibrary.org/obo/MAT_0000081"}],"text":"A novel heterodimerization partner for thyroid hormone receptor. Peroxisome proliferator-activated receptor.\nRetinoid-like receptors play a central role in hormonal responses by forming heterodimers with other nuclear hormone receptors. In this study we have identified the peroxisome proliferator-activated receptor (PPAR) as a new thyroid hormone receptor (THR) auxiliary nuclear protein, heterodimerizing with THR in solution. Although these heterodimers do not recognize a classical thyroid hormone response element (TRE) characterized by direct repeat separated by four nucleotides (DR+4), PPAR behaves as a dominant negative regulator of thyroid hormone (TH) action. However, a TH-dependent positive effect is elicited by selective interaction of the THR beta-PPAR but not the THR alpha-PPAR heterodimer with a novel TRE (DR+2). The critical region of THR beta was mapped to 3 amino acids in the distal box of the DNA binding domain. Hence, PPAR can positively or negatively influence TH action depending on TRE structure and THR isotype."}

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{"project":"pubmed-sentences-benchmark","denotations":[{"id":"S1","span":{"begin":0,"end":64},"obj":"Sentence"},{"id":"S2","span":{"begin":65,"end":108},"obj":"Sentence"},{"id":"S3","span":{"begin":109,"end":236},"obj":"Sentence"},{"id":"S4","span":{"begin":237,"end":429},"obj":"Sentence"},{"id":"S5","span":{"begin":430,"end":672},"obj":"Sentence"},{"id":"S6","span":{"begin":673,"end":834},"obj":"Sentence"},{"id":"S7","span":{"begin":835,"end":939},"obj":"Sentence"},{"id":"S8","span":{"begin":940,"end":1044},"obj":"Sentence"}],"text":"A novel heterodimerization partner for thyroid hormone receptor. Peroxisome proliferator-activated receptor.\nRetinoid-like receptors play a central role in hormonal responses by forming heterodimers with other nuclear hormone receptors. In this study we have identified the peroxisome proliferator-activated receptor (PPAR) as a new thyroid hormone receptor (THR) auxiliary nuclear protein, heterodimerizing with THR in solution. Although these heterodimers do not recognize a classical thyroid hormone response element (TRE) characterized by direct repeat separated by four nucleotides (DR+4), PPAR behaves as a dominant negative regulator of thyroid hormone (TH) action. However, a TH-dependent positive effect is elicited by selective interaction of the THR beta-PPAR but not the THR alpha-PPAR heterodimer with a novel TRE (DR+2). The critical region of THR beta was mapped to 3 amino acids in the distal box of the DNA binding domain. Hence, PPAR can positively or negatively influence TH action depending on TRE structure and THR isotype."}

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{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":39,"end":46},"obj":"Body_part"},{"id":"T2","span":{"begin":333,"end":340},"obj":"Body_part"},{"id":"T3","span":{"begin":487,"end":494},"obj":"Body_part"},{"id":"T4","span":{"begin":644,"end":651},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000081"},{"id":"A2","pred":"mat_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/MAT_0000081"},{"id":"A3","pred":"mat_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/MAT_0000081"},{"id":"A4","pred":"mat_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/MAT_0000081"}],"text":"A novel heterodimerization partner for thyroid hormone receptor. Peroxisome proliferator-activated receptor.\nRetinoid-like receptors play a central role in hormonal responses by forming heterodimers with other nuclear hormone receptors. In this study we have identified the peroxisome proliferator-activated receptor (PPAR) as a new thyroid hormone receptor (THR) auxiliary nuclear protein, heterodimerizing with THR in solution. Although these heterodimers do not recognize a classical thyroid hormone response element (TRE) characterized by direct repeat separated by four nucleotides (DR+4), PPAR behaves as a dominant negative regulator of thyroid hormone (TH) action. However, a TH-dependent positive effect is elicited by selective interaction of the THR beta-PPAR but not the THR alpha-PPAR heterodimer with a novel TRE (DR+2). The critical region of THR beta was mapped to 3 amino acids in the distal box of the DNA binding domain. Hence, PPAR can positively or negatively influence TH action depending on TRE structure and THR isotype."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":39,"end":46},"obj":"Body_part"},{"id":"T2","span":{"begin":333,"end":340},"obj":"Body_part"},{"id":"T3","span":{"begin":487,"end":494},"obj":"Body_part"},{"id":"T4","span":{"begin":644,"end":651},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0002046"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0002046"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0002046"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0002046"}],"text":"A novel heterodimerization partner for thyroid hormone receptor. Peroxisome proliferator-activated receptor.\nRetinoid-like receptors play a central role in hormonal responses by forming heterodimers with other nuclear hormone receptors. In this study we have identified the peroxisome proliferator-activated receptor (PPAR) as a new thyroid hormone receptor (THR) auxiliary nuclear protein, heterodimerizing with THR in solution. Although these heterodimers do not recognize a classical thyroid hormone response element (TRE) characterized by direct repeat separated by four nucleotides (DR+4), PPAR behaves as a dominant negative regulator of thyroid hormone (TH) action. However, a TH-dependent positive effect is elicited by selective interaction of the THR beta-PPAR but not the THR alpha-PPAR heterodimer with a novel TRE (DR+2). The critical region of THR beta was mapped to 3 amino acids in the distal box of the DNA binding domain. Hence, PPAR can positively or negatively influence TH action depending on TRE structure and THR isotype."}