Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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    Everyday social dynamics and cultural drivers of women's experiences with HIV/AIDS : voices from Buhaya, Tanzania
    Foster Githinji, V.E. - \ 2015
    Wageningen University. Promotor(en): Paul Richards, co-promotor(en): Todd Crane; Harro Maat. - Wageningen : Wageningen University - ISBN 9789462575806 - 124
    gezondheidszorg - humane immunodeficiëntievirussen - acquired immune deficiency syndrome - huishoudens - man-vrouwrelaties - vrouwen - voedselzekerheid - tanzania - oost-afrika - afrika - health care - human immunodeficiency viruses - acquired immune deficiency syndrome - households - gender relations - women - food security - tanzania - east africa - africa

    Everyday social dynamics and cultural drivers of women’s experiences with HIV/AIDS: voices from Buhaya, Tanzania is based on ethnographic research conducted in the village of Nsisha in northwestern Tanzania. Like most households in this region, Nsisha has been indirectly or directly affected by HIV/AIDS, meaning that either household members have been infected by HIV/AIDS, or households have absorbed children from their extended family and clan who have been orphaned by HIV/AIDS. In whole, the tiers of research and the in-depth questions asked and detailed answers recorded yield four different cross-sectional analyses of the ‘ecology’ of poverty and HIV/AIDS in Buhaya: (1) one which cuts across social stratification within the community, arguing who has more social capital and how this affects their vulnerability; (2) a second which focuses primarily on food and agricultural issues, and more specifically – bananas; (3) a third cross sectional category which centers on climate factors; (4) and a fourth and final category for this thesis which cuts across age categories and focuses on the social variation of widowhood.

    The NADH oxidase from Pyrococcus furiosus: implications for the protection of anaerobic hyperthermophiles against oxidative stress
    Ward, D.E. ; Donnelly, C. ; Mullendore, M.E. ; Oost, J. van der; Vos, W.M. de; Crane III, E.J. - \ 2001
    European Journal of Biochemistry 268 (2001). - ISSN 0014-2956 - p. 5816 - 5823.
    A wealth of H2O-producing NADH oxidase (NOX) homologues have been discovered in the genomes of the hyperthermophilic Archaea, including two homologues in the genome of Pyrococcus furiosus which have been designated as NOX1 and NOX2. In order to investigate the function of NOX1, the structural gene encoding NOX1 was cloned from the genome of P. furiosus and expressed in Escherichia coli, and the resulting recombinant enzyme (rNOX1) was purified to homogeneity. The enzyme is a thermostable flavoprotein that can be reconstituted only with FAD. rNOX1 catalyzes the oxidation of NADH, producing both H2O2 and H2O as reduction products of O2 (O2 1-2NADH 1-2H 1-2NAD H2O2 or 2H2O). To our knowledge, this is the first NADH oxidase found to produce both H2O2 and H2O. The enzyme exhibits a low Km for NADH (< 4 ?m), and shows little or no reaction with NADPH. Transcriptional analyses demonstrated that NOX1 is constitutively expressed regardless of the carbon source and a single promoter was identified 25 bp upstream of the nox1 gene by primer extension. Although P. furiosus is a strict anaerobe, it may tolerate oxygen to some extent and we anticipate NOX1 to be involved in the response to oxygen at high temperatures.
    13C NMR analysis of the cysteine-sulfenic acid redox center of enterococcal NADH peroxidase.
    Crane Iii, E.J. ; Vervoort, J. ; Claiborne, A. - \ 1997
    Biochemistry 36 (1997). - ISSN 0006-2960 - p. 8611 - 8618.
    NADPH peroxidase from Enterococcus faecalis: Crystal structure, 13C NMR analysis, and mechanism.
    Claiborne, A. ; Crane Iii, E.J. ; Parsonage, D. ; Yeh, J.I. ; Hol, W.G.J. ; Vervoort, J. - \ 1997
    In: Flavins and flavoproteins XII / Stevenson, K.J., Massey, V., Williams, C.H., Calgary : University Press - p. 731 - 740.
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