scholarly journals Ten-year survival of pressed, acid-etched e.max lithium disilicate monolithic and bilayered complete-coverage restorations: Performance and outcomes as a function of tooth position and age

2019 ◽  
Vol 121 (5) ◽  
pp. 782-790 ◽  
Author(s):  
Kenneth A. Malament ◽  
Zuhair S. Natto ◽  
Van Thompson ◽  
Dianne Rekow ◽  
Steven Eckert ◽  
...  
2018 ◽  
Vol 28 (2) ◽  
pp. 163-170 ◽  
Author(s):  
Petrina Gerogianni ◽  
Wen Lien ◽  
Despoina Bompolaki ◽  
Ronald Verrett ◽  
Stephan Haney ◽  
...  

Author(s):  
Walter C. McCrone

An excellent chapter on this subject by V.D. Fréchette appeared in a book edited by L.L. Hench and R.W. Gould in 1971 (1). That chapter with the references cited there provides a very complete coverage of the subject. I will add a more complete coverage of an important polarized light microscope (PLM) technique developed more recently (2). Dispersion staining is based on refractive index and its variation with wavelength (dispersion of index). A particle of, say almandite, a garnet, has refractive indices of nF = 1.789 nm, nD = 1.780 nm and nC = 1.775 nm. A Cargille refractive index liquid having nD = 1.780 nm will have nF = 1.810 and nC = 1.768 nm. Almandite grains will disappear in that liquid when observed with a beam of 589 nm light (D-line), but it will have a lower refractive index than that liquid with 486 nm light (F-line), and a higher index than that liquid with 656 nm light (C-line).


2020 ◽  
Vol 69 (3) ◽  
Author(s):  
Felipe Sczepanski ◽  
Cláudia R. Brunnquell ◽  
Sandrine B. Berger ◽  
Eloisa A. Paloco ◽  
Murilo B. Lopes ◽  
...  

Author(s):  
Rocco J. Rotello ◽  
Timothy D. Veenstra

: In the current omics-age of research, major developments have been made in technologies that attempt to survey the entire repertoire of genes, transcripts, proteins, and metabolites present within a cell. While genomics has led to a dramatic increase in our understanding of such things as disease morphology and how organisms respond to medications, it is critical to obtain information at the proteome level since proteins carry out most of the functions within the cell. The primary tool for obtaining proteome-wide information on proteins within the cell is mass spectrometry (MS). While it has historically been associated with the protein identification, developments over the past couple of decades have made MS a robust technology for protein quantitation as well. Identifying quantitative changes in proteomes is complicated by its dynamic nature and the inability of any technique to guarantee complete coverage of every protein within a proteome sample. Fortunately, the combined development of sample preparation and MS methods have made it capable to quantitatively compare many thousands of proteins obtained from cells and organisms.


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