3 research outputs found
The Role of HIV-Related Knowledge and Ethnicity in Determining HIV Risk Perception and Willingness to Undergo HIV Testing Among Rural Women in Burkina Faso
We conducted a random community based survey of 300 young (15–29 years) rural women in Nouna, Burkina Faso. Only one-third of women were aware that a person could have HIV without having symptoms and these women were significantly more likely to classify themselves to be at high risk for getting HIV. Furthermore, multiple partners, Bwaba ethnicity and having mentioned a health worker as a source of HIV information were significantly associated with perceived high personal risk. Perceived willingness to participate in VCT was high (69%). The dissemination of information on the asymptomatic nature of HIV infection could potentially be very important in forming risk perception, awareness, and their willingness to participate in HIV interventions.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/44011/1/10461_2005_Article_3905.pd
Functional and Structural Characterization of a Cation-dependent O-Methyltransferase from the Cyanobacterium Synechocystis sp. Strain PCC 6803*S⃞
The coding sequence of the cyanobacterium Synechocystis sp. strain
PCC 6803 slr0095 gene was cloned and functionally expressed in
Escherichia coli. The corresponding enzyme was classified as a
cation- and S-adenosyl-l-methionine-dependent
O-methyltransferase (SynOMT), consistent with considerable amino acid
sequence identities to eukaryotic O-methyltransferases (OMTs). The
substrate specificity of SynOMT was similar with those of plant and mammalian
CCoAOMT-like proteins accepting a variety of hydroxycinnamic acids and
flavonoids as substrates. In contrast to the known mammalian and plant
enzymes, which exclusively methylate the meta-hydroxyl position of
aromatic di- and trihydroxy systems, Syn-OMT also methylates the
para-position of hydroxycinnamic acids like 5-hydroxyferulic and
3,4,5-trihydroxycinnamic acid, resulting in the formation of novel compounds.
The x-ray structure of SynOMT indicates that the active site allows for two
alternative orientations of the hydroxylated substrates in comparison to the
active sites of animal and plant enzymes, consistent with the observed
preferred para-methylation and position promiscuity. Lys3
close to the N terminus of the recombinant protein appears to play a key role
in the activity of the enzyme. The possible implications of these results with
respect to modifications of precursors of polymers like lignin are
discussed