Results 11 to 20 of about 201,093 (287)
Muscarinic receptor oligomerization [PDF]
Neuropharmacology, 2018 G protein-coupled receptors (GPCRs) have been classically described as monomeric entities that function by binding in a 1:1 stoichiometric ratio to both ligand and downstream signalling proteins.
Alvarez-Curto, Elisa +3 more
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International Journal of Molecular Sciences, 2023 Protein self-association is a biologically remarkable event that involves and affects the structural and functional properties of proteins [...]
Gotte, Giovanni, Menegazzi, Marta
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SLC6 transporter oligomerization [PDF]
Journal of Neurochemistry, 2020 AbstractTransporters of the solute carrier 6 (SLC6) family mediate the reuptake of neurotransmitters such as dopamine, norepinephrine, serotonin, GABA, and glycine. SLC6 family members are 12 transmembrane helix‐spanning proteins that operate using the transmembrane sodium gradient for transport.
Kumaresan Jayaraman +7 more
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GPCR homo-oligomerization [PDF]
Current Opinion in Cell Biology, 2019 G protein-coupled receptors (GPCRs) are an extensive class of trans-plasma membrane proteins that function to regulate a wide range of physiological functions. Despite a general perception that GPCRs exist as monomers an extensive literature has examined whether GPCRs can also form dimers and even higher-order oligomers, and if such organization ...
Milligan, Graeme +2 more
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Identification of Two Novel Peptides That Inhibit α-Synuclein Toxicity and Aggregation
Frontiers in Molecular Neuroscience, 2021 Aggregation of α-synuclein (αSyn) into proteinaceous deposits is a pathological hallmark of a range of neurodegenerative diseases including Parkinson’s disease (PD).
Blagovesta Popova +12 more
doaj +1 more source
An unfolded protein-induced conformational switch activates mammalian IRE1. [PDF]
, 2017 The unfolded protein response (UPR) adjusts the cell's protein folding capacity in the endoplasmic reticulum (ER) according to need. IRE1 is the most conserved UPR sensor in eukaryotic cells.
Acosta-Alvear, Diego +5 more
core +3 more sources
Can Short Peptides Be Inhibitors of Serum Amyloid a Protein Aggregation?
Proceedings, 2019 One of the approaches in the design of anti-amyloid drugs is to find compounds that are able to hamper self-association of amyloidogenic protein molecules. [...]
Sandra Skibiszewska, Elzbieta Jankowska
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Overview of the structure and function of the dopamine transporter and its protein interactions
Frontiers in Physiology, 2023 The dopamine transporter (DAT) plays an integral role in dopamine neurotransmission through the clearance of dopamine from the extracellular space. Dysregulation of DAT is central to the pathophysiology of numerous neuropsychiatric disorders and as such ...
Binod Nepal +3 more
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Concentration‐dependent oligomerization and oligomeric arrangement of LptA [PDF]
Protein Science, 2011 AbstractGram‐negative bacteria such as Escherichia coli have an inner membrane and an asymmetric outer membrane (OM) that together protect the cytoplasm and act as a highly selective permeability barrier. Lipopolysaccharide (LPS) is the major component of the outer leaflet of the OM and is essential for the survival of nearly all Gram‐negative bacteria.
Jacqueline A, Merten +2 more
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Multiscale modeling of interaction of alane clusters on Al(111) surfaces: A reactive force field and infrared absorption spectroscopy approach [PDF]
, 2010 We have used reactive force field (ReaxFF) to investigate the mechanism of interaction of alanes on Al(111) surface. Our simulations show that, on the Al(111) surface, alanes oligomerize into larger alanes.
Chabal, Yves J. +7 more
core +1 more source