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Staphylococcus aureus has several extracellular proteases with proposed roles in virulence. SspA (serine protease), SspB (cysteine protease) and Aur (metalloprotease) have been characterized previously and SspA and SspB were found to be cotranscribed. The coding region for the cysteine protease ScpA has been identified and characterized. It is in a probable(More)
S. aureus is a highly successful pathogen that is speculated to be the most common cause of human disease. The progression of disease in S. aureus is subject to multi-factorial regulation, in response to the environments encountered during growth. This adaptive nature is thought to be central to pathogenesis, and is the result of multiple regulatory(More)
Staphylococcus epidermidis, a Gram-positive, coagulase-negative bacterium is a predominant inhabitant of human skin and mucous membranes. Recently, however, it has become one of the most important agents of hospital-acquired bacteriemia, as it has been found to be responsible for surgical wound infections developed in individuals with indwelling catheters(More)
In previous studies of homework in core academic subjects, positive student attitudes toward homework were linked to higher achievement, whereas time spent on homework showed an inconsistent relationship with achievement. This study examined the generalizability of these findings to foreign language learning by analyzing 2,342 adult students’ attitudes(More)
Staphylococcus aureus , a leading cause of bacterial infections in humans, is endowed with a wealth of virulence factors that contribute to the disease process. Several extracellular proteolytic enzymes, including cysteine proteinases referred to as the staphopains (staphopain A, encoded by the scpA gene, and staphopain B, encoded by sspB ), have proposed(More)
The genes encoding secreted, broad-spectrum activity cysteine proteases of Staphylococcus spp. (staphopains) and Streptococcus pyogenes (streptopain, SpeB) are genetically linked to genes encoding cytoplasmic inhibitors. While staphopain inhibitors have lipocalin-like folds, streptopain is inhibited by a protein bearing the scaffold of the enzyme(More)
The cytoplasmic protein SspC of Staphylococcus aureus, referred to as staphostatin B, is a very specific, tightly binding inhibitor of the secreted protease staphopain B (SspB). SspC is hypothesized to protect intracellular proteins against proteolytic damage by prematurely folded and activated staphopain B (M. Rzychon, A. Sabat, K. Kosowska, J. Potempa,(More)
Bacterial pathogens secrete a multitude of factors, many of which exhibit enzymatic activity that is directed against host-specific targets or are activated by host-specific functions. To counter these toxic molecules, producing organisms have developed several mechanisms in order to protect themselves against enzymes that have the ability to adversely(More)
rom diplomatic negotiation to translation of foreign communications to interpreting in conflict zones, language skills are vital to national security. Because it is sometimes difficult to predict which languages will be of strategic importance in the future, U.S. Government agencies need to select and train personnel in new languages as quickly as possible.(More)
he LanguageNation platform aims to make online language learning more effective and efficient by leveraging the resources of Human Language Technology and Second Language Acquisition research. Part of this goal involves tailoring training to learner profiles at the individual level, which may be accomplished more easily in an online environment than in(More)