Guaranteed Loop Bound Identification from Program Traces for WCET

2009 ◽  
Author(s):  
Mark Bartlett ◽  
Iain Bate ◽  
Dimitar Kazakov
Keyword(s):  
Program Traces ◽  
Loop Bound

Software Co-Verification Based on Program Traces from Different Processors

2015 ◽  
Author(s):  
Rodolfo Jardim De Azevedo ◽  
LuÍs Fernando Antonioli
Keyword(s):  
Program Traces

scholarly journals Reducing WCET Overestimations by Correcting Errors in Loop Bound Constraints

Energies ◽  
2017 ◽  
Vol 10 (12) ◽  
pp. 2113 ◽  
Author(s):  
Fanqi Meng ◽  
Xiaohong Su
Keyword(s):  
Bound Constraints ◽  
Loop Bound

scholarly journals Model Checking Merged Program Traces

2009 ◽  
Vol 240 ◽  
pp. 97-112 ◽  
Author(s):  
Paulo Salem da Silva ◽  
Ana C.V. de Melo
Keyword(s):  
Model Checking ◽  
Program Traces

Light-Weight Instrumentation From Relational Queries Over Program Traces

2004 ◽  
Author(s):  
Simon Goldsmith ◽  
Robert O'Callahan ◽  
Alex Aiken
Keyword(s):  
Light Weight ◽  
Program Traces

scholarly journals Analysis of the interaction between RGD-expressing adenovirus type 5 fiber knob domains and αvβ3 integrin reveals distinct binding profiles and intracellular trafficking

2006 ◽  
Vol 87 (9) ◽  
pp. 2497-2505 ◽  
Author(s):  
Rosie Lord ◽  
Maddy Parsons ◽  
Ian Kirby ◽  
Andrew Beavil ◽  
James Hunt ◽  
...  
Keyword(s):  
Intracellular Trafficking ◽  
Adenovirus Type ◽  
Rgd Peptide ◽  
Αvβ3 Integrin ◽  
Therapeutic Gene ◽  
Rgd Sequence ◽  
Cell Adsorption ◽  
Endosomal Transport ◽  
Loop Bound ◽  
Adenovirus Type 5

Adenovirus (Ad) vectors are used widely for experimental and therapeutic gene transfer. Ad-mediated gene delivery is often inefficient and, thus, there is considerable interest in developing Ad vectors that overcome biological barriers to efficient virus uptake. For this strategy to succeed, it is imperative that the interaction between such Ad vectors and their novel receptors is well understood. In this study, three surface-exposed loops (HI, CD and IJ loops) on the Ad5 fiber knob domain were selected as sites for insertion of an αvβ3 integrin-binding RGD sequence. Three RGD-containing Ad5 fiber knob-domain mutants were produced as recombinant proteins and all were shown to interact with soluble αvβ3 integrin by using biomolecular cell-free assays. Cell adsorption and subsequent internalization and intracellular trafficking of each of these proteins were assessed by confocal microscopy. Whilst the Ad5 fiber knob domain expressing the RGD sequence in the HI and CD loops bound with similar association and dissociation profiles, the fiber knob domain expressing the RGD sequence in the IJ loop bound with slower association and faster dissociation rates. By using molecular modelling, it was shown that the Ad5 fiber knob domain in which the RGD peptide was expressed in the IJ loop was only capable of binding to one αvβ3 integrin molecule per trimer. In contrast, fiber knob domains in which the RGD peptide was expressed in the HI and CD loops were capable of binding to one integrin molecule per monomer. These differences in the interactions between each mutant and αvβ3 may explain our observation that the three RGD-bearing Ad5 fiber knob domains demonstrated similar internalization rates, but distinct patterns of endosomal transport and escape.

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