3,904 research outputs found
Model-checking Quantitative Alternating-time Temporal Logic on One-counter Game Models
We consider quantitative extensions of the alternating-time temporal logics
ATL/ATLs called quantitative alternating-time temporal logics (QATL/QATLs) in
which the value of a counter can be compared to constants using equality,
inequality and modulo constraints. We interpret these logics in one-counter
game models which are infinite duration games played on finite control graphs
where each transition can increase or decrease the value of an unbounded
counter. That is, the state-space of these games are, generally, infinite. We
consider the model-checking problem of the logics QATL and QATLs on one-counter
game models with VASS semantics for which we develop algorithms and provide
matching lower bounds. Our algorithms are based on reductions of the
model-checking problems to model-checking games. This approach makes it quite
simple for us to deal with extensions of the logical languages as well as the
infinite state spaces. The framework generalizes on one hand qualitative
problems such as ATL/ATLs model-checking of finite-state systems,
model-checking of the branching-time temporal logics CTL and CTLs on
one-counter processes and the realizability problem of LTL specifications. On
the other hand the model-checking problem for QATL/QATLs generalizes
quantitative problems such as the fixed-initial credit problem for energy games
(in the case of QATL) and energy parity games (in the case of QATLs). Our
results are positive as we show that the generalizations are not too costly
with respect to complexity. As a byproduct we obtain new results on the
complexity of model-checking CTLs in one-counter processes and show that
deciding the winner in one-counter games with LTL objectives is
2ExpSpace-complete.Comment: 22 pages, 12 figure
Multi-Agent Programming Contest 2011 - The Python-DTU Team
We provide a brief description of the Python-DTU system, including the
overall design, the tools and the algorithms that we plan to use in the agent
contest.Comment: 4 page
Multi-Agent Programming Contest 2010 - The Jason-DTU Team
We provide a brief description of the Jason-DTU system, including the
methodology, the tools and the team strategy that we plan to use in the agent
contest.Comment: 4 page
Production, purification and structural characterisation of recombinant barley limit dextrinase and characterisation of its interaction with the endogenous limit dextrinase inhibitor
Viewpoints and changing practices of Arkansas rice farmers
To grow crops and to feed this country, water is essential. Farmers used to having abundant water must begin to use water-saving devices: just because you have abundant water doesn’t mean you are entitled to use it wastefully. Our challenge as agricultural leaders is to bring this knowledge to the farming community
Resistance to Linezolid Caused by Modifications at Its Binding Site on the Ribosome
Linezolid is an oxazolidinone antibiotic in clinical use for the treatment of serious infections of resistant Gram-positive bacteria. It inhibits protein synthesis by binding to the peptidyl transferase center on the ribosome. Almost all known resistance mechanisms involve small alterations to the linezolid binding site, so this review will therefore focus on the various changes that can adversely affect drug binding and confer resistance. High-resolution structures of linezolid bound to the 50S ribosomal subunit show that it binds in a deep cleft that is surrounded by 23S rRNA nucleotides. Mutation of 23S rRNA has for some time been established as a linezolid resistance mechanism. Although ribosomal proteins L3 and L4 are located further away from the bound drug, mutations in specific regions of these proteins are increasingly being associated with linezolid resistance. However, very little evidence has been presented to confirm this. Furthermore, recent findings on the Cfr methyltransferase underscore the modification of 23S rRNA as a highly effective and transferable form of linezolid resistance. On a positive note, detailed knowledge of the linezolid binding site has facilitated the design of a new generation of oxazolidinones that show improved properties against the known resistance mechanisms
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