scholarly journals On the IID Capacity-Achieving Input for Binding Channels With Multiple Ligand Receptors

IEEE Access ◽  
2019 ◽  
Vol 7 ◽  
pp. 104380-104393
Author(s):  
Jianfeng Sun ◽  
Hui Li
Keyword(s):  
Ligand Receptors ◽  
Multiple Ligand

scholarly journals On the importance of composite protein multiple ligand interactions in protein pockets

2016 ◽  
Vol 38 (15) ◽  
pp. 1252-1259 ◽  
Author(s):  
Sam Tonddast-Navaei ◽  
Bharath Srinivasan ◽  
Jeffrey Skolnick
Keyword(s):  
Ligand Interactions ◽  
Protein Pockets ◽  
Multiple Ligand

Polymers with Multiple Ligand Sites for Metal Extractions in Dense-Phase Carbon Dioxide†

2001 ◽  
Vol 40 (5) ◽  
pp. 1301-1305 ◽  
Author(s):  
Kimberly R. Powell ◽  
T. Mark McCleskey ◽  
William Tumas ◽  
Joseph M. DeSimone
Keyword(s):  
Carbon Dioxide ◽  
Dense Phase ◽  
Multiple Ligand

Maximum Common Binding Modes (MCBM):  Consensus Docking Scoring Using Multiple Ligand Information and Interaction Fingerprints

2008 ◽  
Vol 48 (2) ◽  
pp. 319-332 ◽  
Author(s):  
Steffen Renner ◽  
Swetlana Derksen ◽  
Sebastian Radestock ◽  
Fabian Mörchen
Keyword(s):  
Binding Modes ◽  
Multiple Ligand ◽  
Interaction Fingerprints

scholarly journals G protein-coupled receptors--recent advances.

2012 ◽  
Vol 59 (4) ◽  
Author(s):  
Dorota Latek ◽  
Anna Modzelewska ◽  
Bartosz Trzaskowski ◽  
Krzysztof Palczewski ◽  
Sławomir Filipek
Keyword(s):  
G Protein ◽  
Biochemical Characterization ◽  
Membrane Receptors ◽  
Signaling Cascades ◽  
Protein Signaling ◽  
Partial Activation ◽  
Bovine Rhodopsin ◽  
G Protein Coupled ◽  
Multiple Ligand

The years 2000 and 2007 witnessed milestones in current understanding of G protein-coupled receptor (GPCR) structural biology. In 2000 the first GPCR, bovine rhodopsin, was crystallized and the structure was solved, while in 2007 the structure of β(2)-adrenergic receptor, the first GPCR with diffusible ligands, was determined owing to advances in microcrystallization and an insertion of the fast-folding lysozyme into the receptor. In parallel with those crystallographic studies, the biological and biochemical characterization of GPCRs has advanced considerably because those receptors are molecular targets for many of currently used drugs. Therefore, the mechanisms of activation and signal transduction to the cell interior deduced from known GPCRs structures are of the highest importance for drug discovery. These proteins are the most diversified membrane receptors encoded by hundreds of genes in our genome. They participate in processes responsible for vision, smell, taste and neuronal transmission in response to photons or binding of ions, hormones, peptides, chemokines and other factors. Although the GPCRs share a common seven-transmembrane α-helical bundle structure their binding sites can accommodate thousands of different ligands. The ligands, including agonists, antagonists or inverse agonists change the structure of the receptor. With bound agonists they can form a complex with a suitable G protein, be phosphorylated by kinases or bind arrestin. The discovered signaling cascades invoked by arrestin independently of G proteins makes the GPCR activating scheme more complex such that a ligand acting as an antagonist for G protein signaling can also act as an agonist in arrestin-dependent signaling. Additionally, the existence of multiple ligand-dependent partial activation states as well as dimerization of GPCRs result in a 'microprocessor-like' action of these receptors rather than an 'on-off' switch as was commonly believed only a decade ago.

scholarly journals Synapse type-specific proteomic dissection identifies IgSF8 as a hippocampal CA3 microcircuit organizer

2019 ◽  
Author(s):  
Nuno Apóstolo ◽  
Samuel N. Smukowski ◽  
Jeroen Vanderlinden ◽  
Giuseppe Condomitti ◽  
Vasily Rybakin ◽  
...  
Keyword(s):  
Cell Surface ◽  
Pyramidal Neurons ◽  
Mossy Fiber ◽  
Surface Protein ◽  
Guidance Cue ◽  
Hippocampal Ca3 ◽  
Cell Surface Interactions ◽  
Ca3 Pyramidal Neurons ◽  
Ca3 Neurons ◽  
Multiple Ligand

SummarySynaptic diversity is a key feature of neural circuits. The structural and functional diversity of closely spaced inputs converging on the same neuron suggests that cell-surface interactions are essential in organizing input properties. Here, we analyzed the cell-surface protein (CSP) composition of hippocampal mossy fiber (MF) inputs on CA3 pyramidal neurons to identify regulators of MF-CA3 synapse properties. We uncover a rich cell-surface repertoire that includes adhesion proteins, guidance cue receptors, extracellular matrix (ECM) proteins, and uncharacterized CSPs. Interactome screening reveals multiple ligand-receptor modules and identifies ECM protein Tenascin-R (TenR) as a ligand of the uncharacterized neuronal receptor IgSF8. Presynaptic Igsf8 deletion impairs MF-CA3 synaptic architecture and robustly decreases the density of bouton filopodia that provide feedforward inhibition of CA3 neurons. Consequently, loss of IgSF8 increases CA3 neuron excitability. Our findings identify IgSF8 as a regulator of CA3 microcircuit development and suggest that combinations of CSP modules define input identity.

scholarly journals A new opioid designed multiple ligand derived from the μ opioid agonist endomorphin-2 and the δ opioid antagonist pharmacophore Dmt-Tic

2007 ◽  
Vol 15 (22) ◽  
pp. 6876-6881 ◽  
Author(s):  
Severo Salvadori ◽  
Claudio Trapella ◽  
Stella Fiorini ◽  
Lucia Negri ◽  
Roberta Lattanzi ◽  
...  
Keyword(s):  
Opioid Antagonist ◽  
Opioid Agonist ◽  
Multiple Ligand

scholarly journals Zn-Templated synthesis of substituted (2,6-diimine)pyridine proligands and evaluation of their iron complexes as anolytes for flow battery applications

2020 ◽  
Vol 49 (45) ◽  
pp. 16175-16183 ◽  
Author(s):  
Jason D. Braun ◽  
Paul A. Gray ◽  
Baldeep K. Sidhu ◽  
Dion B. Nemez ◽  
David E. Herbert
Keyword(s):  
Iron Complexes ◽  
Flow Battery ◽  
Strong Electron ◽  
Templated Synthesis ◽  
Redox Flow Batteries ◽  
Pyridine Ligands ◽  
Flow Batteries ◽  
Multiple Ligand

Zn2+ templating enables synthesis of redox ‘non-innocent’ diimine pyridine ligands with strong electron-withdrawing groups, allowing construction of iron complexes with multiple ligand-based reductions for application in redox flow batteries.

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