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Additional Domain (additional + domain)

Distribution by Scientific Domains

Medical Sciences	50%

Selected Abstracts

A comparison of changes in dental students' and medical students' approaches to learning during professional training

EUROPEAN JOURNAL OF DENTAL EDUCATION, Issue 4 2001
Robert Lindemann
The purposes of this study were 1) to compare the learning approaches of dental students (DS) and medical students (MS) for the Class of 1998 at a single institution at admission and graduation and 2) to determine if their learning approaches changed over the course of their studies. An Approaches to Studying Inventory (ASI) was administered to DS and MS at two times: their first month in school and their last month in school. Means and standard deviations were calculated for three ASI orientations to studying: ,Meaning', ,Reproducing', and ,Achieving'. An additional domain referred to as ,Styles and Pathologies' identified learning problems. In comparison, DS and MS demonstrated a different pattern of learning approaches at matriculation; however, at graduation these differences were less apparent. Over time, DS reported a decreased use, and MS reported an increased use of the Reproducing orientation bringing them closer together. MS also demonstrated an increased use of the Achieving orientation. The Meaning orientation, which indicates a deep approach to learning, was equivalently used by both groups at entry and remained unaltered. [source]

Integron-encoded IntI integrases preferentially recognize the adjacent cognate attI site in recombination with a 59-be site

MOLECULAR MICROBIOLOGY, Issue 5 2002
Christina M. Collis
Summary Integrons have the capacity to capture small mobile elements known as gene cassettes, and this reaction is catalysed by integron-encoded IntI integrases. IntI integrases form a distinct family within the tyrosine recombinase superfamily and include a characteristic additional domain that is well conserved. Two different IntI enzymes were used to examine their ability to recognize heterologous attI sites in both integration and excision assays. IntI1 and IntI3 are 59% identical and catalyse both integrative and excisive recombination between a cassette-associated 59-be site and the cognate attI1 or attI3 site. Integrative recombination events involving a 59-be and a non-cognate attI site, attI2 and attI3 for IntI1 or attI1 and attI2 for IntI3, were detected extremely rarely. In cassette excision assays, the non-cognate attI3 site was recognized by IntI1, but attI1 was not well recognized by IntI3. The purified IntI1 and IntI3 proteins bound strongly only to their cognate attI site. [source]

A new, broad-spectrum azole antifungal: posaconazole , mechanisms of action and resistance, spectrum of activity

MYCOSES, Issue 2006
H. Hof
Summary Posaconazole, a new triazole antifungal, exerts principally the same mechanism of action as the other azole derivatives, i.e. it inhibits the ergosterol production by binding and inhibiting the lanosterol-14,-demethylase which is present in almost all fungi except Pneumocystis and Pythium. Posaconazole has an exquisitely high affinity to this target. Since posaconazole has a chemical structure different from fluconazole and voriconazole, it can interact with an additional domain of the target so that it may inhibit even mutated strains resistant to fluconazole and voriconazole. In addition posaconazole is a bad substrate for efflux pumps in fungi, so it can stay active when other azoles are already inactive. Furthermore, the spectrum of posaconazole is rather large including also some zygomycetes resistant to other azoles. In conclusion, posaconazole is actually the most potent azole derivative used in medicine. A combination of posaconazole with other groups of antifungals may have a favourable effect. There are several methods to test the in vitro activities of posaconazole including the E-test, though interpretive breakpoints are still lacking. [source]

Vibrio cholerae cytolysin is composed of an ,-hemolysin-like core

PROTEIN SCIENCE, Issue 2 2003
Rich Olson
VCC, Vibrio cholerae cytolysin; ,HL, ,-hemolysin; LukF, leukocidin F component Abstract The enteric pathogen Vibrio cholerae secretes a water-soluble 80-kD cytolysin, Vibrio cholerae cytolysin (VCC) that assembles into pentameric channels following proteolytic activation by exogenous proteases. Until now, VCC has been placed in a unique class of pore-forming toxins, distinct from paradigms such as Staphyloccal ,-hemolysin. However, as reported here, amino acid sequence analysis and three-dimensional structure modeling indicate that the core component of the VCC toxin is related in sequence and structure to a family of hemolysins from Staphylococcus aureus that include leukocidin F and ,-hemolysin. Furthermore, our analysis has identified the channel-forming region of VCC and a potential lipid head-group binding site, and suggests a conserved mechanism of assembly and lysis. An additional domain in the VCC toxin is related to plant lectins, conferring additional target cell specificity to the toxin. [source]