Louren{\c c}o, João, and Gon{\c c}alo Cunha. "
Testing patterns for software transactional memory engines."
Proceedings of the 2007 ACM workshop on Parallel and distributed systems: testing and debugging. PADTAD ’07. New York, NY, USA: ACM, 2007. 36-42.
AbstractThe emergence of multi-core processors is promoting the use of concurrency and multithreading. To raise the abstraction level of synchronization constructs is fundamental to ease the development of concurrent software, and Software Transactional Memory (STM) is a good approach towards such goal. However, execution environment issues such as the processor instruction set, caching policy, and memory model, may have strong influence upon the reliability of STM engines. This paper addresses the testing of STM engines aiming at improving their reliability and independence from execution environment. From our experience with porting and extending a specific STM engine, we report on some of the bugs found and synthesize some testing patterns that proved to be useful at testing STM engines.
Fisher, Karl, David J. Lowe, Pedro Tavares, Alice S. Pereira, Boi Hanh Huynh, Dale Edmondson, and William E. Newton. "
{Conformations generated during turnover of the Azotobacter vinelandii nitrogenase MoFe protein and their relationship to physiological function}."
Journal Of Inorganic Biochemistry. 101 (2007): 1649-1656.
AbstractVarious S = 3/2 EPR signals elicited from wild-type and variant Azotobacter vinelandii nitrogenase MoFe proteins appear to reflect different conformations assumed by the FeMo-cofactor with different protonation states. To determine whether these presumed changes in protonation and conformation reflect catalytic capacity, the responses (particularly to changes in electron flux) of the alpha H195Q, alpha H195N, and alpha Q191 K variant MoFe proteins (where His at position 195 in the alpha subunit is replaced by Gln/Asn or Gln at position alpha-191 by Lys), which have strikingly different substrate-reduction properties, were studied by stopped-flow or rapid-freeze techniques. Rapid-freeze EPR at low electron flux (at 3-fold molar excess of wild-type Fe protein) elicited two transient FeMo-cofactor-based EPR signals within 1 s of initiating turnover under N-2 with the alpha H195Q and alpha H195N variants, but not with the alpha Q191K variant. No EPR signals attributable to P cluster oxidation were observed for any of the variants under these conditions. Furthermore, during turnover at low electron flux with the wild-type, alpha H195Q or alpha H195N MoFe protein, the longer-time 430-nm absorbance increase, which likely reflects P cluster oxidation, was also not observed (by stopped-flow spectrophotometry); it did, however, occur for all three MoFe proteins under higher electron flux. No 430-nm absorbance increase occurred with the alpha Q191K variant, not even at higher electron flux. This putative lack of involvement of the P cluster in electron transfer at low electron flux was confirmed by rapid-freeze Fe-57 Mossbauer spectroscopy, which clearly showed FeMo-factor reduction without P cluster oxidation. Because the wild-type, alpha H195Q and alpha H195N MoFe proteins can bind N-2, but alpha Q195K cannot, these results suggest that P cluster oxidation occurs only under high electron flux as required for N-2 reduction. (C) 2007 Elsevier Inc. All rights reserved.