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G. K. Whitfield

Researcher at University of Arizona

Publications -  21
Citations -  3399

G. K. Whitfield is an academic researcher from University of Arizona. The author has contributed to research in topics: Calcitriol receptor & Retinoid X receptor. The author has an hindex of 16, co-authored 21 publications receiving 3287 citations.

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The nuclear vitamin D receptor: biological and molecular regulatory properties revealed.

TL;DR: The scope of this review will be limited to highlighting the actions of 1,25(OH)2D3 mediated by nuclear VDR and discussing new developments in the structure/function analysis of the receptor, including the phenotype of VDR knockout mice and the biochemical classification of patients with point mutations in the receptor.
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The polymorphic N terminus in human vitamin D receptor isoforms influences transcriptional activity by modulating interaction with transcription factor IIB

TL;DR: It is concluded that the functioning of positively charged Arg-18/Arg-22 as part of an hVDR docking site for TFIIB is influenced by the composition of the adjacent polymorphic N terminus, and increased transactivation by the F/M4 neomorphic HVDR is hypothesized to result from its demonstrated enhanced association withTFIIB.
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The vitamin D hormone and its nuclear receptor: molecular actions and disease states

TL;DR: Vitamin D responsive elements (VDREs) consisting of direct hexanucleotide repeats with a spacer of three nucleotides have been identified in the promoter regions of positively controlled genes expressed in bone, such as osteocalcin, osteopontin, beta 3-integrin and vitamin D 24-OHase.
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Molecular Nature of the Vitamin D Receptor and its Role in Regulation of Gene Expression

TL;DR: The fact that the phenotype of HVDRR patients, excluding alopecia, mimics classic nutritional as well as renal rickets, indicates that 1,25(OH)2D3-liganded VDR not only executes the bone mineral homeostatic actions of vitamin D, but suggests that VDR also participates in the normal hair growth cycle in skin.
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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 partner.

TL;DR: The unique properties of these genetically altered receptors establish a new subclass of natural human VDR mutants that illustrate, in vivo, the importance of both 1,25-(OH)2D3 binding and heterodimerization with RXR in VDR action.