scholarly journals Determination of Specific Electrocatalytic Sites in the Oxidation of Small Molecules on Crystalline Metal Surfaces

2019 ◽  
Vol 377 (1) ◽  
Author(s):  
Manuel J. S. Farias ◽  
Juan M. Feliu
Keyword(s):  
Small Molecules ◽  
Metal Surfaces ◽  
Crystalline Metal

scholarly journals Hot electron-induced reduction of small molecules on photorecycling metal surfaces

2015 ◽  
Vol 6 (1) ◽  
Author(s):  
Wei Xie ◽  
Sebastian Schlücker
Keyword(s):  
Small Molecules ◽  
Metal Surfaces ◽  
Hot Electron

Working with Small Molecules: Preparing and Storing Stock Solutions and Determination of Kinetic Solubility

2011 ◽  
pp. 265-271 ◽  
Author(s):  
Andrea Wolf ◽  
Satoko Shimamura ◽  
Friedrich B. M. Reinhard
Keyword(s):  
Small Molecules ◽  
Stock Solutions ◽  
Kinetic Solubility

scholarly journals Cryo-EM structure of the NLRP3 decamer bound to the cytokine release inhibitory drug CRID3

2021 ◽  
Author(s):  
Inga V. Hochheiser ◽  
Michael Pilsl ◽  
Gregor Hagelueken ◽  
Jonas Moecking ◽  
Michael Marleaux ◽  
...  
Keyword(s):  
Small Molecules ◽  
Nucleotide Binding Domain ◽  
Native Form ◽  
Spherical Structure ◽  
Cryo Electron Microscopy ◽  
Rational Drug ◽  
Inhibitory Drug ◽  
Drug Optimization ◽  
Apical Axis

NLRP3 is an intracellular sensor protein whose activation by a broad spectrum of exogenous and endogenous stimuli leads to inflammasome formation and pyroptosis. The mechanisms leading to NLRP3 activation and the way how antagonistic small molecules function remain poorly understood. Here we report the cryo-electron microscopy structures of full-length NLRP3 in its native form and complexed with the inhibitor CRID3 (also named MCC950). Inactive, ADP-bound NLRP3 is a decamer composed of homodimers of intertwined LRR domains that assemble back-to-back as pentamers with the NACHT domain located at the apical axis of this spherical structure. Molecular contacts between the concave sites of two opposing LRRs are mediated by an acidic loop extending from an LRR transition segment. Binding of CRID3 significantly stabilizes the NACHT and LRR domains relative to each other, allowing structural resolution of 3.9-4.2 Ang. CRID3 binds into a cleft, connecting four subdomains of the NACHT with the transition LRR. Its central sulfonylurea group interacts with the Walker A motif of the NLRP3 nucleotide-binding domain and is sandwiched between two arginines from opposing sites, explaining the specificity of NLRP3 for this chemical entity. With the determination of the binding site of this lead therapeutic, specific targeting of NLRP3 for the treatment of autoinflammatory and autoimmune diseases and rational drug optimization are within reach.

scholarly journals THE DETERMINATION OF TRACE RESIDUES ON METAL SURFACES

1964 ◽  
Author(s):  
J.L. Holst ◽  
D.K. Strangfeld
Keyword(s):  
Metal Surfaces

Theoretical determination of the lithium affinity of several small molecules

1994 ◽  
Vol 74 (4) ◽  
Author(s):  
I. Tamássy-Lentei ◽  
J. Szaniszló
Keyword(s):  
Small Molecules ◽  
Theoretical Determination

Rapid lateral flow assays based on the quantification of magnetic nanoparticle labels for multiplexed immunodetection of small molecules: application to the determination of drugs of abuse

2019 ◽  
Vol 186 (9) ◽  
Author(s):  
Natalia V. Guteneva ◽  
Sergey L. Znoyko ◽  
Alexey V. Orlov ◽  
Maxim P. Nikitin ◽  
Petr I. Nikitin
Keyword(s):  
Small Molecules ◽  
Magnetic Nanoparticle ◽  
Drugs Of Abuse ◽  
Lateral Flow ◽  
Lateral Flow Assays

Determination of the basic parameters characterizing the roughness of metal surfaces by laser light scattering

1999 ◽  
Vol 46 (2) ◽  
pp. 279-293 ◽  
Author(s):  
Miloslav Ohlídal ◽  
Marek Uncˇovsky´ ◽  
Ivan Ohlídal ◽  
Daniel Franta
Keyword(s):  
Light Scattering ◽  
Metal Surfaces ◽  
Laser Light ◽  
Laser Light Scattering ◽  
Basic Parameters
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