Conformational rearrangements to the intracellular open states of the LeuT and ApcT transporters are modulated by common mechanisms
about
Visualizing functional motions of membrane transporters with molecular dynamics simulationsX-ray structures of LeuT in substrate-free outward-open and apo inward-open statesAlternating-access mechanism in conformationally asymmetric trimers of the betaine transporter BetPInsights from molecular dynamics: the binding site of cocaine in the dopamine transporter and permeation pathways of substrates in the leucine and dopamine transporters.Conformational dynamics of ligand-dependent alternating access in LeuT.Not just an oil slick: how the energetics of protein-membrane interactions impacts the function and organization of transmembrane proteins.The substrate-driven transition to an inward-facing conformation in the functional mechanism of the dopamine transporter.Conserved tyrosine in the first transmembrane segment of solute:sodium symporters is involved in Na+-coupled substrate co-transport.Conformational cycle and ion-coupling mechanism of the Na+/hydantoin transporter Mhp1.The molecular mechanism of ion-dependent gating in secondary transporters.Substrate-modulated gating dynamics in a Na+-coupled neurotransmitter transporter homologue.Experimental conditions can obscure the second high-affinity site in LeuT.The Environment Shapes the Inner Vestibule of LeuT.Ion-controlled conformational dynamics in the outward-open transition from an occluded state of LeuT.Substrate-induced unlocking of the inner gate determines the catalytic efficiency of a neurotransmitter:sodium symporter.Investigation of the sodium-binding sites in the sodium-coupled betaine transporter BetP.Steric hindrance mutagenesis in the conserved extracellular vestibule impedes allosteric binding of antidepressants to the serotonin transporterStructure-based ligand discovery for the Large-neutral Amino Acid Transporter 1, LAT-1The cost of living in the membrane: a case study of hydrophobic mismatch for the multi-segment protein LeuT.Chloride binding site of neurotransmitter sodium symporters.The two Na+ sites in the human serotonin transporter play distinct roles in the ion coupling and electrogenicity of transportA comparative study of structures and structural transitions of secondary transporters with the LeuT fold.Physiological sodium concentrations enhance the iodide affinity of the Na+/I- symporter.A novel proton transfer mechanism in the SLC11 family of divalent metal ion transporters.Insights on Na(+) binding and conformational dynamics in multidrug and toxic compound extrusion transporter NorM.The role of transmembrane segment 5 (TM5) in Na2 release and the conformational transition of neurotransmitter:sodium symporters toward the inward-open state.Insights into the Structure, Function, and Ligand Discovery of the Large Neutral Amino Acid Transporter 1, LAT1.
P2860
Q26826746-21B2CD13-551E-428A-9345-B6B5A2ECFFD0Q27676655-A8A74835-E6C2-42C6-ACD0-7D1B6FFBE171Q27682108-C9E61447-63EA-47F5-9140-49F578D46891Q30532521-9D671633-BE2F-438C-9943-2ED0C6D5B73FQ33729757-51BECDF2-093D-41FD-B96F-EBE7CB114DEEQ33736493-85E4C084-52E7-4FD1-9846-7ECBEE009877Q33813126-49BD5A5A-FA03-4E84-8A85-26166C21043EQ34195404-C3143E72-5BB7-46C2-917C-91F295367A3AQ34384175-809F273B-0B20-4544-8E27-EB04DEA2DAA4Q35034126-FFB61693-D3FE-469D-95E7-8C217684E965Q35227331-BF3BD9EC-657B-465A-99BC-AD675690F8B6Q35737247-A9AE5291-812B-4BA2-90C3-8AA54E84EDBDQ36189760-772C344F-245F-491E-820A-024892E7909BQ36208010-888DBCCF-8C1F-41EE-999E-45319A37E5F1Q36283737-861F4BCA-D3DC-4CE1-B5AC-AD52E42F369BQ36398069-89A798C0-6512-410F-A58F-DB074524593FQ36407799-9BA2A584-069F-457E-A9CD-E831ABBA0943Q36747640-B106F5D4-A654-4755-9723-E19808EC647FQ36781347-1304E76A-04BA-493C-BAC1-0E9D934E39BEQ36884270-F1AC463F-6B6C-45AB-8E65-AF9A59DB8A97Q37488576-07ECE5DA-4EE6-47A6-B3FE-FEA4B8AE9A59Q38424508-CFE9EF1D-65BF-46B7-91B1-9532CB5400EFQ38989161-7DB5E7D6-DB5A-4858-98EF-35EBBDED4AC1Q42150684-88ECF406-2F5A-4F5A-BE7B-428CBBDFC1EDQ45342240-B1E86DF2-2F5B-4FCE-BAE7-E8CCF87E5512Q47923139-DF795C2A-BDD5-44BE-8939-32865C00C0EFQ52563214-1E576013-4D36-4807-B15C-3919B0A35AEC
P2860
Conformational rearrangements to the intracellular open states of the LeuT and ApcT transporters are modulated by common mechanisms
description
2010 nî lūn-bûn
@nan
2010 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի դեկտեմբերին 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
Conformational rearrangements ...... modulated by common mechanisms
@ast
Conformational rearrangements ...... modulated by common mechanisms
@en
Conformational rearrangements ...... modulated by common mechanisms
@nl
type
label
Conformational rearrangements ...... modulated by common mechanisms
@ast
Conformational rearrangements ...... modulated by common mechanisms
@en
Conformational rearrangements ...... modulated by common mechanisms
@nl
prefLabel
Conformational rearrangements ...... modulated by common mechanisms
@ast
Conformational rearrangements ...... modulated by common mechanisms
@en
Conformational rearrangements ...... modulated by common mechanisms
@nl
P2860
P1433
P1476
Conformational rearrangements ...... modulated by common mechanisms
@en
P2093
Harel Weinstein
P2860
P304
P356
10.1016/J.BPJ.2010.10.003
P407
P50
P577
2010-12-01T00:00:00Z