Structural basis of species-selective antagonist binding to the succinate receptor

Nature ◽  
2019 ◽  
Vol 574 (7779) ◽  
pp. 581-585 ◽  
Author(s):  
Matthias Haffke ◽  
Dominique Fehlmann ◽  
Gabriele Rummel ◽  
Jacques Boivineau ◽  
Myriam Duckely ◽  
...  
Keyword(s):  
Structural Basis ◽  
Selective Antagonist ◽  
Antagonist Binding

scholarly journals Structural insights into the subtype-selective antagonist binding to the M2 muscarinic receptor

2018 ◽  
Vol 14 (12) ◽  
pp. 1150-1158 ◽  
Author(s):  
Ryoji Suno ◽  
Sangbae Lee ◽  
Shoji Maeda ◽  
Satoshi Yasuda ◽  
Keitaro Yamashita ◽  
...  
Keyword(s):  
Muscarinic Receptor ◽  
Selective Antagonist ◽  
M2 Muscarinic Receptor ◽  
Antagonist Binding ◽  
Subtype Selective ◽  
Structural Insights

Structural Basis of NR2B-Selective Antagonist Recognition by N-Methyl-d-aspartate Receptors

2008 ◽  
Vol 75 (1) ◽  
pp. 60-74 ◽  
Author(s):  
Laetitia Mony ◽  
Lucie Krzaczkowski ◽  
Manuel Leonetti ◽  
Anne Le Goff ◽  
Karine Alarcon ◽  
...  
Keyword(s):  
Structural Basis ◽  
Selective Antagonist

scholarly journals Structural Insights into the Subtype-Selective Antagonist Binding to the M2 Muscarinic Receptor

2019 ◽  
Vol 116 (3) ◽  
pp. 206a
Author(s):  
Sangbae Lee ◽  
Suno Ryoji ◽  
Maeda Shoji ◽  
Takuya Kobayashi ◽  
Brian K. Kobilka ◽  
...  
Keyword(s):  
Muscarinic Receptor ◽  
Selective Antagonist ◽  
M2 Muscarinic Receptor ◽  
Antagonist Binding ◽  
Subtype Selective ◽  
Structural Insights

Organization of tight junctions in the choroid plexus epithelium

1978 ◽  
Vol 36 (2) ◽  
pp. 336-337
Author(s):  
B. Van Deurs ◽  
J. K. Koehler
Keyword(s):  
Choroid Plexus ◽  
Present Report ◽  
Freeze Fracture ◽  
Barrier Properties ◽  
Cell Junctions ◽  
Structural Basis ◽  
Apical Surface ◽  
Choroid Plexus Epithelium ◽  
Solid Nitrogen ◽  
Special Composition

The choroid plexus epithelium constitutes a blood-cerebrospinal fluid (CSF) barrier, and is involved in regulation of the special composition of the CSF. The epithelium is provided with an ouabain-sensitive Na/K-pump located at the apical surface, actively pumping ions into the CSF. The choroid plexus epithelium has been described as “leaky” with a low transepithelial resistance, and a passive transepithelial flux following a paracellular route (intercellular spaces and cell junctions) also takes place. The present report describes the structural basis for these “barrier” properties of the choroid plexus epithelium as revealed by freeze fracture.Choroid plexus from the lateral, third and fourth ventricles of rats were used. The tissue was fixed in glutaraldehyde and stored in 30% glycerol. Freezing was performed either in liquid nitrogen-cooled Freon 22, or directly in a mixture of liquid and solid nitrogen prepared in a special vacuum chamber. The latter method was always used, and considered necessary, when preparations of complementary (double) replicas were made.

High resolution spot scan imaging of frozen, hydrated actin bundles with 400kV electrons

1992 ◽  
Vol 50 (1) ◽  
pp. 512-513
Author(s):  
J. Jakana ◽  
M.F. Schmid ◽  
P. Matsudaira ◽  
W. Chiu
Keyword(s):  
High Resolution ◽  
Binding Proteins ◽  
Actin Binding ◽  
Eukaryotic Cells ◽  
Dimensional Structure ◽  
Structural Basis ◽  
Actin Bundle ◽  
Actin Bundles ◽  
3 Dimensional ◽  
Macromolecular Assembly

Actin is a protein found in all eukaryotic cells. In its polymerized form, the cells use it for motility, cytokinesis and for cytoskeletal support. An example of this latter class is the actin bundle in the acrosomal process from the Limulus sperm. The different functions actin performs seem to arise from its interaction with the actin binding proteins. A 3-dimensional structure of this macromolecular assembly is essential to provide a structural basis for understanding this interaction in relationship to its development and functions.

Electron Microscopy and image reconstruction reveal the structural basis for spectrin's elastic properties

1992 ◽  
Vol 50 (1) ◽  
pp. 510-511
Author(s):  
Amy M. McGough ◽  
Robert Josephs
Keyword(s):  
Electron Microscopy ◽  
Elastic Properties ◽  
Conformational Changes ◽  
Quaternary Structure ◽  
Three Dimensional ◽  
Membrane Skeleton ◽  
Projection Algorithm ◽  
Structural Basis ◽  
Iterative Approximation ◽  
Membrane Skeletons

The remarkable deformability of the erythrocyte derives in large part from the elastic properties of spectrin, the major component of the membrane skeleton. It is generally accepted that spectrin's elasticity arises from marked conformational changes which include variations in its overall length (1). In this work the structure of spectrin in partially expanded membrane skeletons was studied by electron microscopy to determine the molecular basis for spectrin's elastic properties. Spectrin molecules were analysed with respect to three features: length, conformation, and quaternary structure. The results of these studies lead to a model of how spectrin mediates the elastic deformation of the erythrocyte.Membrane skeletons were isolated from erythrocyte membrane ghosts, negatively stained, and examined by transmission electron microscopy (2). Particle lengths and end-to-end distances were measured from enlarged prints using the computer program MACMEASURE. Spectrin conformation (straightness) was assessed by calculating the particles’ correlation length by iterative approximation (3). Digitised spectrin images were correlation averaged or Fourier filtered to improve their signal-to-noise ratios. Three-dimensional reconstructions were performed using a suite of programs which were based on the filtered back-projection algorithm and executed on a cluster of Microvax 3200 workstations (4).

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