scholarly journals Ultrafast Polymerization Inhibition by Stimulated Emission Depletion for Three-dimensional Nanolithography

2012 ◽  
Vol 24 (10) ◽  
pp. OP65-OP69 ◽  
Author(s):  
Joachim Fischer ◽  
Martin Wegener
Keyword(s):  
Three Dimensional ◽  
Stimulated Emission ◽  
Stimulated Emission Depletion

scholarly journals Three-Dimensional Stimulated Emission Depletion Microscopy of Nitrogen-Vacancy Centers in Diamond Using Continuous-Wave Light

Nano Letters ◽  
2009 ◽  
Vol 9 (9) ◽  
pp. 3323-3329 ◽  
Author(s):  
Kyu Young Han ◽  
Katrin I. Willig ◽  
Eva Rittweger ◽  
Fedor Jelezko ◽  
Christian Eggeling ◽  
...  
Keyword(s):  
Continuous Wave ◽  
Three Dimensional ◽  
Stimulated Emission ◽  
Nitrogen Vacancy ◽  
Nitrogen Vacancy Centers ◽  
Stimulated Emission Depletion ◽  
Continuous Wave Light

scholarly journals Stimulated Emission Depletion Microscopy with Color Centers in Hexagonal Boron Nitride

ACS Photonics ◽  
2021 ◽  
Author(s):  
Prince Khatri ◽  
Ralph Nicholas Edward Malein ◽  
Andrew J. Ramsay ◽  
Isaac J. Luxmoore
Keyword(s):  
Boron Nitride ◽  
Hexagonal Boron Nitride ◽  
Stimulated Emission ◽  
Color Centers ◽  
Stimulated Emission Depletion

scholarly journals A Super-Resolved View of the Alzheimer’s Disease-Related Amyloidogenic Pathway in Hippocampal Neurons

2021 ◽  
pp. 1-20
Author(s):  
Yang Yu ◽  
Yang Gao ◽  
Bengt Winblad ◽  
Lars Tjernberg ◽  
Sophia Schedin Weiss
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Hippocampal Neurons ◽  
Three Dimensional ◽  
Amyloid Β ◽  
Stimulated Emission ◽  
Amyloid Β Peptide ◽  
Primary Neurons ◽  
Amyloid Β Protein ◽  
Early Endosomes

Background: Processing of the amyloid-β protein precursor (AβPP) is neurophysiologically important due to the resulting fragments that regulate synapse biology, as well as potentially harmful due to generation of the 42 amino acid long amyloid β-peptide (Aβ 42), which is a key player in Alzheimer’s disease. Objective: Our aim was to clarify the subcellular locations of the amyloidogenic AβPP processing in primary neurons, including the intracellular pools of the immediate substrate, AβPP C-terminal fragment (APP-CTF) and the product (Aβ 42). To overcome the difficulties of resolving these compartments due to their small size, we used super-resolution microscopy. Methods: Mouse primary hippocampal neurons were immunolabelled and imaged by stimulated emission depletion (STED) microscopy, including three-dimensional, three-channel imaging and image analyses. Results: The first (β-secretase) and second (γ-secretase) cleavages of AβPP were localized to functionally and distally distinct compartments. The β-secretase cleavage was observed in early endosomes, where we were able to show that the liberated N- and C-terminal fragments were sorted into distinct vesicles budding from the early endosomes in soma. Lack of colocalization of Aβ 42 and APP-CTF in soma suggested that γ-secretase cleavage occurs in neurites. Indeed, APP-CTF was, in line with Aβ 42 in our previous study, enriched in the presynapse but absent from the postsynapse. In contrast, full-length AβPP was not detected in either the pre- or the postsynaptic side of the synapse. Furthermore, we observed that endogenously produced and endocytosed Aβ 42 were localized in different compartments. Conclusion: These findings provide critical super-resolved insight into amyloidogenic AβPP processing in primary neurons.

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