Structural basis of Na(+)-independent and cooperative substrate/product antiport in CaiT
about
Crystal structure of a SLC11 (NRAMP) transporter reveals the basis for transition-metal ion transportInsights to ligand binding to the monoamine transporters-from homology modeling to LeuBAT and dDATUnveiling the Mechanism of Arginine Transport through AdiC with Molecular Dynamics Simulations: The Guiding Role of Aromatic ResiduesSubstrate specificity and ion coupling in the Na+/betaine symporter BetPMolecular basis of substrate-induced permeation by an amino acid antiporterStructures of a Na+-coupled, substrate-bound MATE multidrug transporterArginine oscillation explains Na+ independence in the substrate/product antiporter CaiTMolecular mechanism of ligand recognition by membrane transport protein, Mhp1A gate-free pathway for substrate release from the inward-facing state of the Na⁺-galactose transporterRetrieving backbone string neighbors provides insights into structural modeling of membrane proteins.Simulated annealing reveals the kinetic activity of SGLT1, a member of the LeuT structural family.Structural and mechanistic basis of proton-coupled metal ion transport in the SLC11/NRAMP family.Variation of the detergent-binding capacity and phospholipid content of membrane proteins when purified in different detergents.Molecular modeling and ligand docking for solute carrier (SLC) transportersUnbiased simulations reveal the inward-facing conformation of the human serotonin transporter and Na(+) ion release.Cytoplasmic permeation pathway of neurotransmitter transporters.Identification of the substrate recognition and transport pathway in a eukaryotic member of the nucleobase-ascorbate transporter (NAT) familyEvolutionary relationship between 5+5 and 7+7 inverted repeat folds within the amino acid-polyamine-organocation superfamily.Identification of a second substrate-binding site in solute-sodium symporters.Protonation of glutamate 208 induces the release of agmatine in an outward-facing conformation of an arginine/agmatine antiporterAn unusual transmembrane helix in the endoplasmic reticulum ubiquitin ligase Doa10 modulates degradation of its cognate E2 enzyme.The Aspergillus nidulans proline permease as a model for understanding the factors determining substrate binding and specificity of fungal amino acid transporters.Ectoine and hydroxyectoine as protectants against osmotic and cold stress: uptake through the SigB-controlled betaine-choline- carnitine transporter-type carrier EctT from Virgibacillus pantothenticus.Importance of host cell arginine uptake in Francisella phagosomal escape and ribosomal protein amounts.Locating an extracellular K+-dependent interaction site that modulates betaine-binding of the Na+-coupled betaine symporter BetP.dissectHMMER: a HMMER-based score dissection framework that statistically evaluates fold-critical sequence segments for domain fold similarity.Bridging the gap between structure and kinetics of human SGLT1.A conformational switch in a partially unwound helix selectively determines the pathway for substrate release from the carnitine/γ-butyrobetaine antiporter CaiTCarnitine in bacterial physiology and metabolism.Investigation of the sodium-binding sites in the sodium-coupled betaine transporter BetP.Cotranslational folding of membrane proteins probed by arrest-peptide-mediated force measurements.The two Na+ sites in the human serotonin transporter play distinct roles in the ion coupling and electrogenicity of transportThe Na+/I- symporter (NIS): mechanism and medical impact.The BCCT family of carriers: from physiology to crystal structure.OCTN cation transporters in health and disease: role as drug targets and assay development.The sodium/multivitamin transporter: a multipotent system with therapeutic implications.A comparative study of structures and structural transitions of secondary transporters with the LeuT fold.GRIFFIN: A versatile methodology for optimization of protein-lipid interfaces for membrane protein simulations.The SUD1 gene encodes a putative E3 ubiquitin ligase and is a positive regulator of 3-hydroxy-3-methylglutaryl coenzyme a reductase activity in Arabidopsis.Alternating access mechanisms of LeuT-fold transporters: trailblazing towards the promised energy landscapes.
P2860
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P2860
Structural basis of Na(+)-independent and cooperative substrate/product antiport in CaiT
description
2010 nî lūn-bûn
@nan
2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Structural basis of Na(+)-independent and cooperative substrate/product antiport in CaiT
@ast
Structural basis of Na(+)-independent and cooperative substrate/product antiport in CaiT
@en
Structural basis of Na(+)-independent and cooperative substrate/product antiport in CaiT
@nl
type
label
Structural basis of Na(+)-independent and cooperative substrate/product antiport in CaiT
@ast
Structural basis of Na(+)-independent and cooperative substrate/product antiport in CaiT
@en
Structural basis of Na(+)-independent and cooperative substrate/product antiport in CaiT
@nl
prefLabel
Structural basis of Na(+)-independent and cooperative substrate/product antiport in CaiT
@ast
Structural basis of Na(+)-independent and cooperative substrate/product antiport in CaiT
@en
Structural basis of Na(+)-independent and cooperative substrate/product antiport in CaiT
@nl
P2093
P921
P3181
P356
P1433
P1476
Structural basis of Na(+)-independent and cooperative substrate/product antiport in CaiT
@en
P2093
Anke C Terwisscha van Scheltinga
Sabrina Schulze
Ulrike Geldmacher
P2888
P3181
P356
10.1038/NATURE09310
P407
P577
2010-09-09T00:00:00Z
P6179
1014416368