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G K Whitfield

Showing results (21-30 of 32) with videos related to

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Molecular Endocrinology (Baltimore, Md.)|September 1, 1995
A highly conserved region in the hormone-binding domain of the human vitamin D receptor contains residues vital for heterodimerization with retinoid X receptor and for transcriptional activationG K Whitfield, J C Hsieh, S Nakajima, et al.
Genomics|August 1, 1988
Two thyroid hormone regulated genes, the beta-subunits of nerve growth factor (NGFB) and thyroid stimulating hormone (TSHB), are located less than 310 kb apart in both human and mouse genomesN C Dracopoli, E Rose, G K Whitfield, et al.
The Journal of Biological Chemistry|July 15, 1993
Phosphorylation of the human vitamin D receptor by protein kinase C. Biochemical and functional evaluation of the serine 51 recognition siteJ C Hsieh, P W Jurutka, S Nakajima, et al.
Proceedings of the National Academy of Sciences of the United States of America|March 1, 1986
Assignment of the gene for the beta subunit of thyroid-stimulating hormone to the short arm of human chromosome 1N C Dracopoli, W J Rettig, G K Whitfield, et al.
The Journal of Endocrinology|October 24, 1997
The vitamin D hormone and its nuclear receptor: molecular actions and disease statesM R Haussler, C A Haussler, P W Jurutka, et al.
The Journal of Biological Chemistry|June 6, 1997
Mutations in the 1,25-dihydroxyvitamin D3 receptor identifying C-terminal amino acids required for transcriptional activation that are functionally dissociated from hormone binding, heterodimeric DNA binding, and interaction with basal transcription factor IIB, in vitroP W Jurutka, J C Hsieh, L S Remus, et al.
Journal of Cellular Biochemistry|October 28, 1999
Vitamin D receptor displays DNA binding and transactivation as a heterodimer with the retinoid X receptor, but not with the thyroid hormone receptorP D Thompson, J C Hsieh, G K Whitfield, et al.
Journal of Molecular Endocrinology|September 21, 2001
Distinct retinoid X receptor activation function-2 residues mediate transactivation in homodimeric and vitamin D receptor heterodimeric contextsP D Thompson, L S Remus, J C Hsieh, et al.
Biochemistry|December 10, 1999
Characterization of unique DNA-binding and transcriptional-activation functions in the carboxyl-terminal extension of the zinc finger region in the human vitamin D receptorJ C Hsieh, G K Whitfield, A K Oza, et al.
Molecular Endocrinology (Baltimore, Md.)|December 1, 1996
Vitamin D receptors from patients with resistance to 1,25-dihydroxyvitamin D3: point mutations confer reduced transactivation in response to ligand and impaired interaction with the retinoid X receptor heterodimeric partnerG K Whitfield, S H Selznick, C A Haussler, et al.
Pageof 4

Showing results (21-30 of 32) with videos related to

Sort By:
Pageof 4
Molecular Endocrinology (Baltimore, Md.)|September 1, 1995
A highly conserved region in the hormone-binding domain of the human vitamin D receptor contains residues vital for heterodimerization with retinoid X receptor and for transcriptional activationG K Whitfield, J C Hsieh, S Nakajima, et al.
Genomics|August 1, 1988
Two thyroid hormone regulated genes, the beta-subunits of nerve growth factor (NGFB) and thyroid stimulating hormone (TSHB), are located less than 310 kb apart in both human and mouse genomesN C Dracopoli, E Rose, G K Whitfield, et al.
The Journal of Biological Chemistry|July 15, 1993
Phosphorylation of the human vitamin D receptor by protein kinase C. Biochemical and functional evaluation of the serine 51 recognition siteJ C Hsieh, P W Jurutka, S Nakajima, et al.
Proceedings of the National Academy of Sciences of the United States of America|March 1, 1986
Assignment of the gene for the beta subunit of thyroid-stimulating hormone to the short arm of human chromosome 1N C Dracopoli, W J Rettig, G K Whitfield, et al.
The Journal of Endocrinology|October 24, 1997
The vitamin D hormone and its nuclear receptor: molecular actions and disease statesM R Haussler, C A Haussler, P W Jurutka, et al.
The Journal of Biological Chemistry|June 6, 1997
Mutations in the 1,25-dihydroxyvitamin D3 receptor identifying C-terminal amino acids required for transcriptional activation that are functionally dissociated from hormone binding, heterodimeric DNA binding, and interaction with basal transcription factor IIB, in vitroP W Jurutka, J C Hsieh, L S Remus, et al.
Journal of Cellular Biochemistry|October 28, 1999
Vitamin D receptor displays DNA binding and transactivation as a heterodimer with the retinoid X receptor, but not with the thyroid hormone receptorP D Thompson, J C Hsieh, G K Whitfield, et al.
Journal of Molecular Endocrinology|September 21, 2001
Distinct retinoid X receptor activation function-2 residues mediate transactivation in homodimeric and vitamin D receptor heterodimeric contextsP D Thompson, L S Remus, J C Hsieh, et al.
Biochemistry|December 10, 1999
Characterization of unique DNA-binding and transcriptional-activation functions in the carboxyl-terminal extension of the zinc finger region in the human vitamin D receptorJ C Hsieh, G K Whitfield, A K Oza, et al.
Molecular Endocrinology (Baltimore, Md.)|December 1, 1996
Vitamin D receptors from patients with resistance to 1,25-dihydroxyvitamin D3: point mutations confer reduced transactivation in response to ligand and impaired interaction with the retinoid X receptor heterodimeric partnerG K Whitfield, S H Selznick, C A Haussler, et al.
Pageof 4