34‐5: Adaptive Refresh Rate and Resolution: Exploiting the Limitations of Spatio‐Temporal Vision

2021 ◽  
Vol 52 (1) ◽  
pp. 465-468
Author(s):  
Rafał K. Mantiuk ◽  
Gyorgy Denes
Keyword(s):  
Refresh Rate ◽  
Temporal Vision ◽  
Spatio Temporal

The Design Of Systems That Display Moving Images Based On Spatio-Temporal Vision Data

1988 ◽  
Author(s):  
William E. Glenn ◽  
Karen G. Glenn
Keyword(s):  
Moving Images ◽  
Temporal Vision ◽  
Spatio Temporal

scholarly journals Temporal Resolution Multiplexing: Exploiting the limitations of spatio-temporal vision for more efficient VR rendering

2019 ◽  
Vol 25 (5) ◽  
pp. 2072-2082 ◽  
Author(s):  
Gyorgy Denes ◽  
Kuba Maruszczyk ◽  
George Ash ◽  
Rafal K. Mantiuk
Keyword(s):  
Temporal Resolution ◽  
Temporal Vision ◽  
Spatio Temporal

Spatio-temporal vision of macaques with severe loss of Pβ retinal ganglion cells

1986 ◽  
Vol 26 (11) ◽  
pp. 1751-1761 ◽  
Author(s):  
William H. Merigan ◽  
Thomas A. Eskin
Keyword(s):  
Retinal Ganglion Cells ◽  
Ganglion Cells ◽  
Retinal Ganglion ◽  
Severe Loss ◽  
Temporal Vision ◽  
Spatio Temporal

scholarly journals Exploiting the limitations of spatio-temporal vision for more efficient VR rendering

2018 ◽  
Author(s):  
Gyorgy Denes ◽  
Kuba Maruszczyk ◽  
Rafał K. Mantiuk
Keyword(s):  
Temporal Vision ◽  
Spatio Temporal

scholarly journals A cortical locus for post adaptation facilitation in spatio-temporal vision

2010 ◽  
Vol 7 (9) ◽  
pp. 386-386 ◽  
Author(s):  
P. Bex ◽  
K. Langley ◽  
J. Cass
Keyword(s):  
Temporal Vision ◽  
Spatio Temporal

E3 ubiquitin ligases

2005 ◽  
Vol 41 ◽  
pp. 15-30 ◽  
Author(s):  
Helen C. Ardley ◽  
Philip A. Robinson
Keyword(s):  
Protein Complexes ◽  
Loss Of Function ◽  
Direct Role ◽  
Cellular Processes ◽  
Substrate Protein ◽  
Protein Ubiquitination ◽  
C Terminus ◽  
Full Complement ◽  
Spatio Temporal ◽  
Eukaryotic Organisms

The selectivity of the ubiquitin–26 S proteasome system (UPS) for a particular substrate protein relies on the interaction between a ubiquitin-conjugating enzyme (E2, of which a cell contains relatively few) and a ubiquitin–protein ligase (E3, of which there are possibly hundreds). Post-translational modifications of the protein substrate, such as phosphorylation or hydroxylation, are often required prior to its selection. In this way, the precise spatio-temporal targeting and degradation of a given substrate can be achieved. The E3s are a large, diverse group of proteins, characterized by one of several defining motifs. These include a HECT (homologous to E6-associated protein C-terminus), RING (really interesting new gene) or U-box (a modified RING motif without the full complement of Zn2+-binding ligands) domain. Whereas HECT E3s have a direct role in catalysis during ubiquitination, RING and U-box E3s facilitate protein ubiquitination. These latter two E3 types act as adaptor-like molecules. They bring an E2 and a substrate into sufficiently close proximity to promote the substrate's ubiquitination. Although many RING-type E3s, such as MDM2 (murine double minute clone 2 oncoprotein) and c-Cbl, can apparently act alone, others are found as components of much larger multi-protein complexes, such as the anaphase-promoting complex. Taken together, these multifaceted properties and interactions enable E3s to provide a powerful, and specific, mechanism for protein clearance within all cells of eukaryotic organisms. The importance of E3s is highlighted by the number of normal cellular processes they regulate, and the number of diseases associated with their loss of function or inappropriate targeting.

Elucidating cyclic AMP signaling in subcellular domains with optogenetic tools and fluorescent biosensors

2019 ◽  
Vol 47 (6) ◽  
pp. 1733-1747 ◽  
Author(s):  
Christina Klausen ◽  
Fabian Kaiser ◽  
Birthe Stüven ◽  
Jan N. Hansen ◽  
Dagmar Wachten
Keyword(s):  
Cyclic Amp ◽  
Adenosine Monophosphate ◽  
Adenylyl Cyclases ◽  
Temporal Precision ◽  
Fluorescent Biosensors ◽  
Subcellular Domains ◽  
Spatio Temporal ◽  
Hydrolysis Of ◽  
Shed Light ◽  
Cyclic Amp Signaling

The second messenger 3′,5′-cyclic nucleoside adenosine monophosphate (cAMP) plays a key role in signal transduction across prokaryotes and eukaryotes. Cyclic AMP signaling is compartmentalized into microdomains to fulfil specific functions. To define the function of cAMP within these microdomains, signaling needs to be analyzed with spatio-temporal precision. To this end, optogenetic approaches and genetically encoded fluorescent biosensors are particularly well suited. Synthesis and hydrolysis of cAMP can be directly manipulated by photoactivated adenylyl cyclases (PACs) and light-regulated phosphodiesterases (PDEs), respectively. In addition, many biosensors have been designed to spatially and temporarily resolve cAMP dynamics in the cell. This review provides an overview about optogenetic tools and biosensors to shed light on the subcellular organization of cAMP signaling.

Spatio-temporal source analysis

1997 ◽  
Vol 103 (1) ◽  
pp. 47
Author(s):  
M Scherq
Keyword(s):  
Source Analysis ◽  
Spatio Temporal
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