Dynamic elements at both cytoplasmically and extracellularly facing sides of the UapA transporter selectively control the accessibility of substrates to their translocation pathway.
about
Transporter oligomerization: form and functionCysteine-scanning analysis of helices TM8, TM9a, and TM9b and intervening loops in the YgfO xanthine permease: a carboxyl group is essential at ASP-276.Insights to the evolution of Nucleobase-Ascorbate Transporters (NAT/NCS2 family) from the Cys-scanning analysis of xanthine permease XanQIdentification of the substrate recognition and transport pathway in a eukaryotic member of the nucleobase-ascorbate transporter (NAT) familyOrigin, diversification and substrate specificity in the family of NCS1/FUR transporters.Structure-function relationship of a plant NCS1 member--homology modeling and mutagenesis identified residues critical for substrate specificity of PLUTO, a nucleobase transporter from Arabidopsis.The role of transmembrane segment TM3 in the xanthine permease XanQ of Escherichia coli.Substrate selectivity of YgfU, a uric acid transporter from Escherichia coli.Understanding transporter specificity and the discrete appearance of channel-like gating domains in transporters.Structure of eukaryotic purine/H(+) symporter UapA suggests a role for homodimerization in transport activity.Analysis of conserved NCS2 motifs in the Escherichia coli xanthine permease XanQ.Modeling, substrate docking, and mutational analysis identify residues essential for the function and specificity of a eukaryotic purine-cytosine NCS1 transporter.A substrate translocation trajectory in a cytoplasm-facing topological model of the monocarboxylate/H⁺ symporter Jen1p.The arrestin-like protein ArtA is essential for ubiquitination and endocytosis of the UapA transporter in response to both broad-range and specific signals.Substrate Specificity of the FurE Transporter Is Determined by Cytoplasmic Terminal Domain Interactions.Evolution of substrate specificity in the Nucleobase-Ascorbate Transporter (NAT) protein family.
P2860
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P2860
Dynamic elements at both cytoplasmically and extracellularly facing sides of the UapA transporter selectively control the accessibility of substrates to their translocation pathway.
description
2010 nî lūn-bûn
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2010年の論文
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年学术文章
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2010年学术文章
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name
Dynamic elements at both cytop ...... o their translocation pathway.
@en
Dynamic elements at both cytop ...... o their translocation pathway.
@nl
type
label
Dynamic elements at both cytop ...... o their translocation pathway.
@en
Dynamic elements at both cytop ...... o their translocation pathway.
@nl
prefLabel
Dynamic elements at both cytop ...... o their translocation pathway.
@en
Dynamic elements at both cytop ...... o their translocation pathway.
@nl
P2093
P1476
Dynamic elements at both cytop ...... o their translocation pathway.
@en
P2093
George Diallinas
Ioannis Papageorgiou
Vasiliki Kosti
P304
P356
10.1016/J.JMB.2010.02.037
P407
P577
2010-02-25T00:00:00Z