scholarly journals Phase Mask-Based Multimodal Superresolution Microscopy

Photonics ◽  
2017 ◽  
Vol 4 (4) ◽  
pp. 39 ◽  
Author(s):  
Ryan Beams ◽  
Jeremiah Woodcock ◽  
Jeffrey Gilman ◽  
Stephan Stranick
2008 ◽  
Author(s):  
Yuankun Lin ◽  
Ahmad Harb ◽  
Daniel Rodriguez ◽  
Karen Lozano ◽  
Di Xu ◽  
...  

2020 ◽  
Vol 118 (3) ◽  
pp. 149a
Author(s):  
Craig Leighton ◽  
Mathew Horrocks ◽  
Tilo Kunath

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Angika Bulbul ◽  
Joseph Rosen

AbstractPartial aperture imaging system (PAIS) is a recently developed concept in which the traditional disc-shaped aperture is replaced by an aperture with a much smaller area and yet its imaging capabilities are comparable to the full aperture systems. Recently PAIS was demonstrated as an indirect incoherent digital three-dimensional imaging technique. Later it was successfully implemented in the study of the synthetic marginal aperture with revolving telescopes (SMART) to provide superresolution with subaperture area that was less than one percent of the area of the full synthetic disc-shaped aperture. In the study of SMART, the concept of PAIS was tested by placing eight coded phase reflectors along the boundary of the full synthetic aperture. In the current study, various improvements of PAIS are tested and its performance is compared with the other equivalent systems. Among the structural changes, we test ring-shaped eight coded phase subapertures with the same area as of the previous circular subapertures, distributed along the boundary of the full disc-shaped aperture. Another change in the current system is the use of coded phase mask with a point response of a sparse dot pattern. The third change is in the reconstruction process in which a nonlinear correlation with optimal parameters is implemented. With the improved image quality, the modified-PAIS can save weight and cost of imaging devices in general and of space telescopes in particular. Experimental results with reflective objects show that the concept of coded aperture extends the limits of classical imaging.


2021 ◽  
Author(s):  
Jun He ◽  
Baijie Xu ◽  
Xizhen Xu ◽  
Changrui Liao ◽  
Yiping Wang

AbstractFiber Bragg grating (FBG) is the most widely used optical fiber sensor due to its compact size, high sensitivity, and easiness for multiplexing. Conventional FBGs fabricated by using an ultraviolet (UV) laser phase-mask method require the sensitization of the optical fiber and could not be used at high temperatures. Recently, the fabrication of FBGs by using a femtosecond laser has attracted extensive interests due to its excellent flexibility in creating FBGs array or special FBGs with complex spectra. The femtosecond laser could also be used for inscribing various FBGs on almost all fiber types, even fibers without any photosensitivity. Such femtosecond-laser-induced FBGs exhibit excellent thermal stability, which is suitable for sensing in harsh environment. In this review, we present the historical developments and recent advances in the fabrication technologies and sensing applications of femtosecond-laser-inscribed FBGs. Firstly, the mechanism of femtosecond-laser-induced material modification is introduced. And then, three different fabrication technologies, i.e., femtosecond laser phase mask technology, femtosecond laser holographic interferometry, and femtosecond laser direct writing technology, are discussed. Finally, the advances in high-temperature sensing applications and vector bending sensing applications of various femtosecond-laser-inscribed FBGs are summarized. Such femtosecond-laser-inscribed FBGs are promising in many industrial areas, such as aerospace vehicles, nuclear plants, oil and gas explorations, and advanced robotics in harsh environments.


mBio ◽  
2015 ◽  
Vol 6 (6) ◽  
Author(s):  
Maude F. Lévêque ◽  
Laurence Berry ◽  
Michael J. Cipriano ◽  
Hoa-Mai Nguyen ◽  
Boris Striepen ◽  
...  

ABSTRACT Autophagy is a catabolic process widely conserved among eukaryotes that permits the rapid degradation of unwanted proteins and organelles through the lysosomal pathway. This mechanism involves the formation of a double-membrane structure called the autophagosome that sequesters cellular components to be degraded. To orchestrate this process, yeasts and animals rely on a conserved set of autophagy-related proteins (ATGs). Key among these factors is ATG8, a cytoplasmic protein that is recruited to nascent autophagosomal membranes upon the induction of autophagy. Toxoplasma gondii is a potentially harmful human pathogen in which only a subset of ATGs appears to be present. Although this eukaryotic parasite seems able to generate autophagosomes upon stresses such as nutrient starvation, the full functionality and biological relevance of a canonical autophagy pathway are as yet unclear. Intriguingly, in T. gondii, ATG8 localizes to the apicoplast under normal intracellular growth conditions. The apicoplast is a nonphotosynthetic plastid enclosed by four membranes resulting from a secondary endosymbiosis. Using superresolution microscopy and biochemical techniques, we show that TgATG8 localizes to the outermost membrane of this organelle. We investigated the unusual function of TgATG8 at the apicoplast by generating a conditional knockdown mutant. Depletion of TgATG8 led to rapid loss of the organelle and subsequent intracellular replication defects, indicating that the protein is essential for maintaining apicoplast homeostasis and thus for survival of the tachyzoite stage. More precisely, loss of TgATG8 led to abnormal segregation of the apicoplast into the progeny because of a loss of physical interactions of the organelle with the centrosomes. IMPORTANCE By definition, autophagy is a catabolic process that leads to the digestion and recycling of eukaryotic cellular components. The molecular machinery of autophagy was identified mainly in model organisms such as yeasts but remains poorly characterized in phylogenetically distant apicomplexan parasites. We have uncovered an unusual function for autophagy-related protein ATG8 in Toxoplasma gondii: TgATG8 is crucial for normal replication of the parasite inside its host cell. Seemingly unrelated to the catabolic autophagy process, TgATG8 associates with the outer membrane of the nonphotosynthetic plastid harbored by the parasite called the apicoplast, and there it plays an important role in the centrosome-driven inheritance of the organelle during cell division. This not only reveals an unexpected function for an autophagy-related protein but also sheds new light on the division process of an organelle that is vital to a group of important human and animal pathogens.


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