Results 11 to 20 of about 13,548 (269)
A mechanism for intracellular release of Na+ by neurotransmitter/sodium symporters [PDF]
Nature Structural and Molecular Biology, 2014 Neurotransmitter/sodium symporters (NSSs) terminate synaptic signal transmission by Na+-dependent reuptake of released neurotransmitters. Key conformational states have been reported for the bacterial homolog LeuT and an inhibitor-bound Drosophila dopamine transporter. However, a coherent mechanism of Na+-driven transport has not been described.
Joseph A Lyons +2 more
exaly +6 more sources
Mechanism of chloride interaction with neurotransmitter:sodium symporters
Nature, 2007 Neurotransmitter:sodium symporters (NSS) have a critical role in regulating neurotransmission and are targets for psychostimulants, anti-depressants and other drugs. Whereas the non-homologous glutamate transporters mediate chloride conductance, in the eukaryotic NSS chloride is transported together with the neurotransmitter.
Matthias Quick, Jonathan A Javitch
exaly +5 more sources
Effect of Dimerization on the Dynamics of Neurotransmitter:Sodium Symporters
The Journal of Physical Chemistry B, 2017 Dimerization is a common feature among the members of the neurotransmitter:sodium symporter (NSS) family of membrane proteins. Yet, the effect of dimerization on the mechanism of action of NSS members is not fully understood.
Mert Gur +3 more
semanticscholar +5 more sources
Sodium Iodide Symporter (NIS) and Thyroid [PDF]
HORMONES, 2002 idase (TPO) and incorporation into tyrosyl residues along the thyroglobulin (Tg) backbone. The thyroid hormones T3 and T4 are synthesized by coupling of two iodotyrosine residues and stored in the colloid. All of these steps are stimulated by pituitary-derived thyroid stimulating hormone (TSH), which interacts with the TSH receptor at the basolateral ...
Christine Spitzweg, John C. Morris
openalex +3 more sources
Gating Topology of the Proton-Coupled Oligopeptide Symporters [PDF]
Structure, 2015 Proton-coupled oligopeptide transporters belong to the major facilitator superfamily (MFS) of membrane transporters. Recent crystal structures suggest the MFS fold facilitates transport through rearrangement of their two six-helix bundles around a central ligand binding site; how this is achieved, however, is poorly understood.
P. Fowler +10 more
semanticscholar +6 more sources
Prokaryotic Solute/Sodium Symporters: Versatile Functions and Mechanisms of a Transporter Family †
International Journal of Molecular Sciences, 2021 The solute/sodium symporter family (SSS family; TC 2.A.21; SLC5) consists of integral membrane proteins that use an existing sodium gradient to drive the uphill transport of various solutes, such as sugars, amino acids, vitamins, or ions across the ...
T. Henríquez +3 more
semanticscholar +1 more source
Function Trumps Form in Two Sugar Symporters, LacY and vSGLT
International Journal of Molecular Sciences, 2021 Active transport of sugars into bacteria occurs through symporters driven by ion gradients. LacY is the most well-studied proton sugar symporter, whereas vSGLT is the most characterized sodium sugar symporter.
J. Abramson, E. M. Wright
semanticscholar +1 more source
Structure and function of Na+-symporters with inverted repeats
Current Opinion in Structural Biology, 2009 Ernest M Wright
exaly +2 more sources
pH Regulation of Electrogenic Sugar/H+ Symport in MFS Sugar Permeases. [PDF]
PLoS ONE, 2016 Bacterial sugar symporters in the Major Facilitator Superfamily (MFS) use the H+ (and in a few cases Na+) electrochemical gradients to achieve active transport of sugar into the cell.
Andre Bazzone +3 more
doaj +1 more source