MINOTAUR

MINOTAUR

MINing Online Text - A User-friendly Resource

Here you can see the sentences relating to structure that have been excised from the ranked abstracts:

17223342 [abstract score 1]
Investigations in mice lacking the first zinc finger of the VDR have demonstrated that they express a truncated receptor containing an intact ligand binding and AF2 domain .
These mice are a phenocopy of mice lacking the VDR , thus demonstrate the critical requirement of the DNA binding domain for hair follicle homeostasis .
Transgenic mice expressing VDRs with mutations in either the ligand-binding domain or the AF2 domain were generated .
15591533 [abstract score 0.940397350993378]
Keratinocyte-specific expression of a VDR transgene with a mutation in the hormone-binding domain that abolishes ligand binding restores normal hair cycling in VDR null mice , whereas a VDR transgene with a mutation in the activation function 2 domain that impairs nuclear receptor coactivator recruitment results in a partial rescue .
12847098 [abstract score 0.645695364238411]
The Hr contact site in human VDR is localized to the central portion of the ligand binding domain , a known corepressor docking region in other nuclear receptors separate from the activation function-2 domain .
Coimmunoprecipitation and functional studies of Hr deletants reveal that VDR contacts a C-terminal region of Hr that includes motifs required for TR and RORalpha binding .
17657241 [abstract score 0.536423841059603]
Here , we show that this deletion removes the stop codon and creates a new reading frame at the C terminus of the hairless protein , generating a larger mutant protein harboring an additional sequence of 117 amino acids .
18266815 [abstract score 0.480132450331126]
VDR functions as a hormonally activated transcription factor , and a role in transcription has been postulated for Hr due in part to its nuclear localization and homology with the GATA-1 zinc-finger domain .
17078924 [abstract score 0.456953642384106]
The truncated VDR weakly bound [ 3H]-1,25 ( OH ) 2D3 but was able to heterodimerize with RXR , bind to DNA and interact with the corepressor hairless ( HR ) .
17310066 [abstract score 0.440397350993377]
This activity required functional vitamin D-responsive promoter elements as well as an intact VDR DNA binding domain and thus could not be distinguished from 1,25 ( OH ) 2D3-dependent VDR transactivation .
Indeed , this 1,25 ( OH ) 2D3-independent VDR-RXR heterodimerization was sufficient to drive transactivation by VDR ( L233S ) , an inactive ligand binding mutant of VDR that was previously shown to rescue the skin phenotype of VDR null mice .
18290715 [abstract score 0.380794701986755]
Regulation of mouse RANKL by 1,25 ( OH ) ( 2 ) D ( 3 ) supports a cloverleaf model , whereby VDR-RXR heterodimers bound to multiple VDREs are juxtapositioned through chromatin looping to form a supercomplex , potentially allowing simultaneous interactions with multiple co-modulators and chromatin remodeling enzymes .
16946620 [abstract score 0.344370860927152]
The mutated protein is expected to contain no ligand-binding domain .
16455232 [abstract score 0.294701986754967]
This missense mutation occurs in the vicinity of repression domain 3 of the hairless protein ( HR ) .
15246940 [abstract score 0.26158940397351]
The genotypes were classified as FF ( absence of the FokI site ) and ff ( presence of the FokI site ) .
18451650 [abstract score 0.225165562913907]
Two of them were free of osteomalacia-related symptoms .
12223961 [abstract score 0.195364238410596]
These receptors form RAR / RXR heterodimers , which bind to genetic regulatory DNA sequences and activate transcription of RA target genes .
As RXR form heterodimers with a number of other nuclear receptors , such as the vitamin D3 receptor ( VDR ) and are involved in several signaling pathways .
12481554 [abstract score 0.172185430463576]
Vitamin D receptor ( VDR ) and retinoid X receptor ( RXR ) are members of the nuclear receptor superfamily and they bind target DNA sequences as heterodimers to regulate transcription .
Emerging information regarding the regulatory control of dimerization based on biochemical , structural , and genetic studies is then presented .
Finally , the main focus of this article is a new dynamic perspective of dimerization functions , based on recent research with fluorescent protein chimeras in living cells by microscopy .
11034212 [abstract score 0.112582781456954]
It is believed that these receptors form heterodimers with retinoid X receptors ( RXRs ) to act as transcriptional regulators .