On the Fuzzy Spatio-temporal Specification of Multimedia Synchronisation Scenarios

2004 ◽  
pp. 53-60
Author(s):  
André L. V. Coelho ◽  
Ivan L. M. Ricarte
Keyword(s):  
Spatio Temporal ◽  
Temporal Specification

scholarly journals A spatio-temporal specification language and its completeness & decidability

2020 ◽  
Vol 9 (1) ◽  
Author(s):  
Tengfei Li ◽  
Jing Liu ◽  
Haiying Sun ◽  
Xiang Chen ◽  
Lipeng Zhang ◽  
...  
Keyword(s):  
Intelligent Transportation System ◽  
Cyber Physical Systems ◽  
Specification Language ◽  
Finite Model ◽  
Critical Systems ◽  
Physical Systems ◽  
Spatial Objects ◽  
Temporal Properties ◽  
Spatio Temporal ◽  
Temporal Specification

AbstractIn the past few years, significant progress has been made on spatio-temporal cyber-physical systems in achieving spatio-temporal properties on several long-standing tasks. With the broader specification of spatio-temporal properties on various applications, the concerns over their spatio-temporal logics have been raised in public, especially after the widely reported safety-critical systems involving self-driving cars, intelligent transportation system, image processing. In this paper, we present a spatio-temporal specification language, STSL PC, by combining Signal Temporal Logic (STL) with a spatial logic S4 u, to characterize spatio-temporal dynamic behaviors of cyber-physical systems. This language is highly expressive: it allows the description of quantitative signals, by expressing spatio-temporal traces over real valued signals in dense time, and Boolean signals, by constraining values of spatial objects across threshold predicates. STSL PC combines the power of temporal modalities and spatial operators, and enjoys important properties such as finite model property. We provide a Hilbert-style axiomatization for the proposed STSL PC and prove the soundness and completeness by the spatio-temporal extension of maximal consistent set and canonical model. Further, we demonstrate the decidability of STSL PC and analyze the complexity of STSL PC. Besides, we generalize STSL to the evolution of spatial objects over time, called STSL OC, and provide the proof of its axiomatization system and decidability.

scholarly journals Spatio-temporal specification of olfactory bulb interneurons

2007 ◽  
Vol 38 (6) ◽  
pp. 563-569 ◽  
Author(s):  
Serena Bovetti ◽  
Paolo Peretto ◽  
Aldo Fasolo ◽  
Silvia De Marchis
Keyword(s):  
Olfactory Bulb ◽  
Spatio Temporal ◽  
Temporal Specification

Runtime Verification of Spatio-Temporal Specification Language

2021 ◽  
Author(s):  
Tengfei Li ◽  
Jing Liu ◽  
Haiying Sun ◽  
Xiaohong Chen ◽  
Ling Yin ◽  
...  
Keyword(s):  
Runtime Verification ◽  
Specification Language ◽  
Spatio Temporal ◽  
Temporal Specification

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.

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