Phosphoregulation of sorting signal–VHS domain interactions by a direct electrostatic mechanism

2002 ◽  
Author(s):  
Yukio Kato ◽  
Saurav Misra ◽  
Rosa Puertollano ◽  
James H. Hurley ◽  
Juan S. Bonifacino
Keyword(s):  
Sorting Signal ◽  
Domain Interactions ◽  
Vhs Domain ◽  
Electrostatic Mechanism

scholarly journals Insights into the Phosphoregulation of β-Secretase Sorting Signal by the VHS Domain of GGA1

Traffic ◽  
2004 ◽  
Vol 5 (6) ◽  
pp. 437-448 ◽  
Author(s):  
Tomoo Shiba ◽  
Satoshi Kametaka ◽  
Masato Kawasaki ◽  
Masahiro Shibata ◽  
Satoshi Waguri ◽  
...  
Keyword(s):  
Sorting Signal ◽  
Vhs Domain

Investigation of ferroelectrics using conventional and in situ electron microscopy

1994 ◽  
Vol 52 ◽  
pp. 586-587
Author(s):  
V. Saikumar ◽  
H. M. Chan ◽  
M. P. Harmer
Keyword(s):  
Nonvolatile Memory ◽  
Ferroelectric Materials ◽  
Gate Insulator ◽  
Sensors And Actuators ◽  
In Situ Electron Microscopy ◽  
Ferroelectric Domains ◽  
Domain Boundaries ◽  
Domain Interactions ◽  
Memory Applications

In recent years, there has been a growing interest in the application of ferroelectric thin films for nonvolatile memory applications and as a gate insulator in DRAM structures. In addition, bulk ferroelectric materials are also widely used as components in electronic circuits and find numerous applications in sensors and actuators. To a large extent, the performance of ferroelectric materials are governed by the ferroelectric domains (with dimensions in the micron to sub-micron range) and the switching of domains in the presence of an applied field. Conventional TEM studies of ferroelectric domains structures, in conjunction with in-situ studies of the domain interactions can aid in explaining the behavior of ferroelectric materials, while providing some answers to the mechanisms and processes that influence the performance of ferroelectric materials. A few examples from bulk and thin film ferroelectric materials studied using the TEM are discussed below.Figure 1 shows micrographs of ferroelectric domains obtained from undoped and Fe-doped BaTiO3 single crystals. The domain boundaries have been identified as 90° domains with the boundaries parallel to <011>.

scholarly journals Viruses go modular

2020 ◽  
Vol 295 (14) ◽  
pp. 4604-4616 ◽  
Author(s):  
Ariel Shepley-McTaggart ◽  
Hao Fan ◽  
Marius Sudol ◽  
Ronald N. Harty
Keyword(s):  
Hippo Pathway ◽  
Host Proteins ◽  
Dna Viruses ◽  
Ww Domain ◽  
Ww Domains ◽  
Host Interactions ◽  
New Class ◽  
Domain Interactions ◽  
Molecular Aspects ◽  
The Hippo Pathway

The WW domain is a modular protein structure that recognizes the proline-rich Pro-Pro-x-Tyr (PPxY) motif contained in specific target proteins. The compact modular nature of the WW domain makes it ideal for mediating interactions between proteins in complex networks and signaling pathways of the cell (e.g. the Hippo pathway). As a result, WW domains play key roles in a plethora of both normal and disease processes. Intriguingly, RNA and DNA viruses have evolved strategies to hijack cellular WW domain–containing proteins and thereby exploit the modular functions of these host proteins for various steps of the virus life cycle, including entry, replication, and egress. In this review, we summarize key findings in this rapidly expanding field, in which new virus-host interactions continue to be identified. Further unraveling of the molecular aspects of these crucial virus-host interactions will continue to enhance our fundamental understanding of the biology and pathogenesis of these viruses. We anticipate that additional insights into these interactions will help support strategies to develop a new class of small-molecule inhibitors of viral PPxY-host WW-domain interactions that could be used as antiviral therapeutics.

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