three-dimensional structures of both the wild-type and mutant pigt (Accelrys)
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Accelrys
three-dimensional structures of both the wild-type and mutant pigt
Three Dimensional Structures Of Both The Wild Type And Mutant Pigt, supplied by Accelrys, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/three-dimensional+structures/three+dimensional+structures+of+both+the+wild+type+and+mutant+pigt/pmc11943126-186-8-15
Average 90 stars, based on 1 article reviews
Three Dimensional Structures Of Both The Wild Type And Mutant Pigt, supplied by Accelrys, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/three-dimensional+structures/three+dimensional+structures+of+both+the+wild+type+and+mutant+pigt/pmc11943126-186-8-15
Average 90 stars, based on 1 article reviews
three-dimensional structures of both the wild-type and mutant pigt - by Bioz Stars,
2026-10
90/100 stars
Images
1) Product Images from "A Novel Homozygous Missense Variant of PIGT Related to Multiple Congenital Anomalies-Hypotonia Seizures Syndrome 3 with Elevated of Serum ALP Level in a Thai Newborn Patient"
Article Title: A Novel Homozygous Missense Variant of PIGT Related to Multiple Congenital Anomalies-Hypotonia Seizures Syndrome 3 with Elevated of Serum ALP Level in a Thai Newborn Patient
Journal: International Journal of Molecular Sciences
doi: 10.3390/ijms26062790
Figure Legend Snippet: Prediction of protein stability at the alteration site through interaction formation. ( a ) Visualization performed using BIOVIA Discovery Studio Visualizer (Version 21.1.0.20298). ( b ) Conservation of amino acids around position 86 in PIGT across different species. An asterisk ( * ) indicates p.86 of the PIGT protein in each species. ( c , d ) Comparison of intramolecular bonds at the alteration site in wild-type (wt) and mutant (mt) proteins, computed and visualized via DDMut.
Techniques Used: Comparison, Mutagenesis
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![Coumarin <t>derivatives</t> can selectively bind to RNA G 1 × 0 bulges: ( A ) RNA structures of the 1 × 0 RNA bulges used for in vitro binding profiling using the FP assay. N = G , A , U , or C (RNA1-4). ( B ) Heatmap profile of the ΔmP = (FP RNA-ligand – FP ligand ) × 1000 for RNA binders in the presence of [RNA] = 5 or 1 μM (red = high polarization, blue = low polarization). ( C ) ΔmP of RNA-ligand complex for RNA ligands at 5 μM. Each data point represents a measurement of a ligand in the 69-compound collection. **** indicates P < .0001. ( D ) Dose-response curves for compounds (SMSM6, <t>C30)</t> selectively binding to the bulged G RNA (RNA1) compared to an 11-nucleotide GA-rich sequence that would form a double loop-like RNA structure measured by the FP assay.](https://pub-med-central-images-cdn.bioz.com/pub_med_central_ids_ending_with_8297/pmc12188297/pmc12188297__gkaf559fig2.jpg)
