Simultaneous detection of 3D orientation and 3D spatial localization of single emitters for nanoscale structural imaging (Conference Presentation)

2019 ◽  
Author(s):  
Sophie Brasselet ◽  
Valentina Curcio ◽  
Thomas Brown ◽  
Miguel Alonso
Keyword(s):  
Simultaneous Detection ◽  
Spatial Localization ◽  
Structural Imaging

The Nature of Oxide Surfaces: Topographic and Electronic Structure

1993 ◽  
Vol 51 ◽  
pp. 966-967
Author(s):  
Dawn A. Bonnell ◽  
Yong Liang
Keyword(s):  
Transition Metal Oxides ◽  
Electronic Structures ◽  
Recent Progress ◽  
Spatial Localization ◽  
Level Of Detail ◽  
Scanning Tunneling ◽  
Oxide Surfaces ◽  
Tunneling Microscopy ◽  
Considerable Effort ◽  
Complete Understanding

Recent progress in the application of scanning tunneling microscopy (STM) and tunneling spectroscopy (STS) to oxide surfaces has allowed issues of image formation mechanism and spatial resolution limitations to be addressed. As the STM analyses of oxide surfaces continues, it is becoming clear that the geometric and electronic structures of these surfaces are intrinsically complex. Since STM requires conductivity, the oxides in question are transition metal oxides that accommodate aliovalent dopants or nonstoichiometry to produce mobile carriers. To date, considerable effort has been directed toward probing the structures and reactivities of ZnO polar and nonpolar surfaces, TiO2 (110) and (001) surfaces and the SrTiO3 (001) surface, with a view towards integrating these results with the vast amount of previous surface analysis (LEED and photoemission) to build a more complete understanding of these surfaces. However, the spatial localization of the STM/STS provides a level of detail that leads to conclusions somewhat different from those made earlier.

Species Specific Immunoassays to Measure Blood Platelet and Coagulation Activation in the Rat

1996 ◽  
Vol 76 (06) ◽  
pp. 1090-1095 ◽  
Author(s):  
C Ravanat ◽  
M Freund ◽  
S Schuhler ◽  
P Grunert ◽  
L Meyer ◽  
...  
Keyword(s):  
Antithrombin Iii ◽  
Plasma Concentrations ◽  
Simultaneous Detection ◽  
Blood Platelet ◽  
Coagulation Activation ◽  
Platelet Factor ◽  
Prethrombotic State ◽  
Low Levels ◽  
Species Specific ◽  
Higher Sensitivity

SummaryThe purpose of this study was to develop specific and sensitive immunoassays to detect early indices of hypercoagulability in the rat. Rat platelet factor 4 (rPF4) and rat fibrinopeptide A (rFPA) assays, tools for the detection of activation of platelets and coagulation respectively, were designed using antibodies raised against purified rPF4 and against synthetic rFPA. The relevance of these new assays and of the commercially available ELISA kit for thrombin-antithrombin III (TAT) complexes was demonstrated in a rat model of a prethrombotic state induced by intravenous infusion of varying doses of thromboplastin (90 to 2400 μl/kg/h). In this model, the immunoassays allowed simultaneous detection of low levels of rFPA and rPF4 which were correlated with fibrinogen and platelet consumption and TAT generation and further proved to be of higher sensitivity than the classical methods of platelet count or measurement of fibrinogen levels. Plasma concentrations of rFPA, rPF4 and TAT were dependent on infusion time and thromboplastin dose, while hirudin (1 mg/kg) prevented their appearance. Thus the new specific immunoassays for rPF4 and rFPA and the commercial human TAT assay represent useful tools for pathophysiological studies or the screening of antithrombotic drugs in rats.

Spatial localization of unknown proteins in the endoplasmic reticulum predicts functions

2007 ◽  
Vol 30 (4) ◽  
pp. 84
Author(s):  
Michael D. Jain ◽  
Hisao Nagaya ◽  
Annalyn Gilchrist ◽  
Miroslaw Cygler ◽  
John J.M. Bergeron
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Folding ◽  
Protein Synthesis ◽  
Protein Function ◽  
Protein Translocation ◽  
Spatial Localization ◽  
Predict Protein Function ◽  
Insight Into ◽  
Soluble Fractions ◽  
Er Membrane

Protein synthesis, folding and degradation functions are spatially segregated in the endoplasmic reticulum (ER) with respect to the membrane and the ribosome (rough and smooth ER). Interrogation of a proteomics resource characterizing rough and smooth ER membranes subfractionated into cytosolic, membrane, and soluble fractions gives a spatial map of known proteins involved in ER function. The spatial localization of 224 identified unknown proteins in the ER is predicted to give insight into their function. Here we provide evidence that the proteomics resource accurately predicts the function of new proteins involved in protein synthesis (nudilin), protein translocation across the ER membrane (nicalin), co-translational protein folding (stexin), and distal protein folding in the lumen of the ER (erlin-1, TMX2). Proteomics provides the spatial localization of proteins and can be used to accurately predict protein function.

Sign in / Sign up

Export Citation Format

Share Document