Zobrazeno 1 - 10 of 26 pro vyhledávání: '"K R, Yamamoto"'
1
Mutations in the glucocorticoid receptor DNA-binding domain mimic an allosteric effect of DNA
Autor: M A, van Tilborg, J A, Lefstin, M, Kruiskamp, J, Teuben, R, Boelens, K R, Yamamoto, R, Kaptein
Publikováno v: Journal of molecular biology. 301(4)
Two previously isolated mutations in the glucocorticoid receptor DNA-binding domain (DBD), S459A and P493R, have been postulated to mimic DNA-induced conformational changes in the glucocorticoid receptor DBD, thereby constitutively triggering an allo
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6fc95e06684e9251776e78cb9a5348de
https://pubmed.ncbi.nlm.nih.gov/10966797
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2
The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies
Autor: B C, Freeman, S J, Felts, D O, Toft, K R, Yamamoto
Publikováno v: Genesdevelopment. 14(4)
Multiple molecular chaperones, including Hsp90 and p23, interact with members of the intracellular receptor (IR) family. To investigate p23 function, we compared the effects of three p23 proteins on IR activities, yeast p23 (sba1p) and the two human
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d05b818223b1b2c3a4db8e7a0314b0f3
https://pubmed.ncbi.nlm.nih.gov/10691735
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4
Modular structure of glucocorticoid receptor domains is not equivalent to functional independence. Stability and activity of the steroid binding domain are controlled by sequences in separate domains
Autor: M, Xu, P K, Chakraborti, M J, Garabedian, K R, Yamamoto, S S, Simons
Publikováno v: The Journal of biological chemistry. 271(35)
A long-standing conundrum of glucocorticoid receptors has been why the steroid binding domain is active in hybrid proteins but not in isolation. For this reason, the precise boundaries of the steroid binding domain have not been defined. These questi
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::ef92935eface08255de8721654ab2fbf
https://pubmed.ncbi.nlm.nih.gov/8702925
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5
Structure refinement of the glucocorticoid receptor-DNA binding domain from NMR data by relaxation matrix calculations
Autor: M A, van Tilborg, A M, Bonvin, K, Hård, A L, Davis, B, Maler, R, Boelens, K R, Yamamoto, R, Kaptein
Publikováno v: Journal of molecular biology. 247(4)
The solution structure of the glucocorticoid receptor (GR) DNA-binding domain (DBD), consisting of 93 residues, has been refined from two and three-dimensional NMR data using an ensemble iterative relaxation matrix approach followed by direct NOE ref
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::05b19e586486cbb636f6b2f55f848624
https://pubmed.ncbi.nlm.nih.gov/7723024
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7
Glucocorticoid receptor-cAMP response element-binding protein interaction and the response of the phosphoenolpyruvate carboxykinase gene to glucocorticoids
Autor: E, Imai, J N, Miner, J A, Mitchell, K R, Yamamoto, D K, Granner
Publikováno v: The Journal of biological chemistry. 268(8)
The phosphoenolpyruvate carboxykinase (PEPCK) gene encodes the rate-limiting enzyme in gluconeogenesis. Glucocorticoids enhance PEPCK gene expression through a multicomponent regulatory complex. We show that a full response to glucocorticoids require
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5177870e4989cffee41d385467452c6d
https://pubmed.ncbi.nlm.nih.gov/8449898
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8
Role of cysteines 640, 656, and 661 in steroid binding to rat glucocorticoid receptors
Autor: P K, Chakraborti, M J, Garabedian, K R, Yamamoto, S S, Simons
Publikováno v: The Journal of biological chemistry. 267(16)
The involvement of a vicinally spaced dithiol group in steroid binding to the glucocorticoid receptor has been deduced from experiments with the thiol-specific reagent methyl methanethiolsulfonate and the vicinal dithiol-specific reagent sodium arsen
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d773fb9a6275d2e715d6ed8f481da74c
https://pubmed.ncbi.nlm.nih.gov/1597467
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9
1H NMR studies of DNA recognition by the glucocorticoid receptor: complex of the DNA binding domain with a half-site response element
Autor: M L, Remerowski, E, Kellenbach, R, Boelens, G A, van der Marel, J H, van Boom, B A, Maler, K R, Yamamoto, R, Kaptein
Publikováno v: Biochemistry. 30(50)
The complex of the rat glucocorticoid receptor (GR) DNA binding domain (DBD) and half-site sequence of the consensus glucocorticoid response element (GRE) has been studied by two-dimensional 1H NMR spectroscopy. The DNA fragment is a 10 base-pair oli
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c5e39013acd7cef5fb6a17396fa9e21d
https://pubmed.ncbi.nlm.nih.gov/1751485
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10
Creation of 'super' glucocorticoid receptors by point mutations in the steroid binding domain
Autor: P K, Chakraborti, M J, Garabedian, K R, Yamamoto, S S, Simons
Publikováno v: The Journal of biological chemistry. 266(33)
Almost all modifications of the steroid binding domain of glucocorticoid receptors are known to cause a reduction or loss of steroid binding activity. Nonetheless, we now report that mutations of cysteine 656 of the rat receptor, which was previously
Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::190e8a9c14c9c3e10ce2ba14664534ed
https://pubmed.ncbi.nlm.nih.gov/1939229
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