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P.V.R. Kumarasiri,S.N. Arseculeratne,P.D. Premasiri,B. Simpson EWHA INSTITUTE FOR BIOMEDICAL LAW & ETHICS 2008 BIOMEDICAL LAW & ETHICS Vol.2 No.2
The achievements of contemporary biomedicine and biotechnology are now widely communicated across the globe. Yet, across different cultures and belief systems, the relationship between the possible and the acceptable when it comes to biomedical advance is highly variable and draws justification from a wide range of sources: culture, religion, 'common sense', family values, ideas of what is 'natural', ideas of what is progress etc. Students' attitudes towards science and by extension toward the new biotechnologies have been extensively researched western contexts. However, relatively little is known about how this relationship plays out in different cultural contexts and there is even less by way of empirical research in this area. In this paper, we are interested in two related questions, the answers to which, we hope will begin to fill these gaps. First, we consider how culture and religion feed into bioethical deliberation among an emerging generation of 'bioethical citizens' drawn from Sri Lanka; the contrast that we go on to make with students from the UK is both illuminating and instructive. Second, we consider the points of bioethical conver-gence and divergence between the two groups. We conclude by offering some observations about what we have coine centres of ethical gravity' and what these might tell us about cultural relativism and the operation of bioethical sensibilities in different cultural contexts.
S.N. Arseculeratne,R. Simpson,P.D. Premasiri,P.V.R. Kumarasiri EWHA INSTITUTE FOR BIOMEDICAL LAW & ETHICS 2008 BIOMEDICAL LAW & ETHICS Vol.2 No.1
This paper is the first of two that set out to explore issues that arise at the interface between globalised systems of biomedicine and bioethics on the one hand and non-western traditions of medicine, healing and ethics on the other. At this interface, fundamental questions of relativism and context are in evidence. Here we offer a preliminary overview of these questions in relation to medical education in Sh Lanka and attempts by local scholars to develop curricula that incorporate indigenous traditions in ways that are both appropriate and realistic, In the paper, we argue for approaches that go beyond simply accumulating and juxtaposing knowledge of different traditions. The strategy we advocate takes the experience of the medical student as the starting point for pedagogical enquiry into different ethical traditions with an emphasis placed on their translation, evaluation and comparison. The promise of such an approach is a bioethics that makes beneficence, respect for life, honesty, truthfulness, dignity and respect central but, through on-going dialogue, connects these values to the local moralities that inform all cultures of healing and care.
Cryogenic photoluminescence imaging system for nanoscale positioning of single quantum emitters
Liu, Jin,Davanç,o, Marcelo I.,Sapienza, Luca,Konthasinghe, Kumarasiri,De Miranda Cardoso, José,Viní,cius,Song, Jin Dong,Badolato, Antonio,Srinivasan, Kartik American Institute of Physics 2017 Review of scientific instruments Vol.88 No.2
Park, Jeong Soon,Lee, Woo Cheol,Yeo, Kwon Joo,Ryu, Kyoung‐,Seok,Kumarasiri, Malika,Hesek, Dusan,Lee, Mijoon,Mobashery, Shahriar,Song, Jung Hyun,Kim, Seung Il,Lee, Je Chul,Cheong, Chaejoon,Jeon, Federation of American Society for Experimental Bi 2012 The FASEB Journal Vol.26 No.1
<P>The outer membrane protein A (OmpA) plays important roles in anchoring of the outer membrane to the bacterial cell wall. The C-terminal periplasmic domain of OmpA (OmpA-like domain) associates with the peptidoglycan (PGN) layer noncovalently. However, there is a paucity of information on the structural aspects of the mechanism of PGN recognition by OmpA-like domains. To elucidate this molecular recognition process, we solved the high-resolution crystal structure of an OmpA-like domain from Acinetobacter baumannii bound to diaminopimelate (DAP), a unique bacterial amino acid from the PGN. The structure clearly illustrates that two absolutely conserved Asp271 and Arg286 residues are the key to the binding to DAP of PGN. Identification of DAP as the central anchoring site of PGN to OmpA is further supported by isothermal titration calorimetry and a pulldown assay with PGN. An NMR-based computational model for complexation between the PGN and OmpA emerged, and this model is validated by determining the crystal structure in complex with a synthetic PGN fragment. These structural data provide a detailed glimpse of how the anchoring of OmpA to the cell wall of gram-negative bacteria takes place in a DAP-dependent manner.</P>