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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Country report INDONESIA - MFS II EVALUATIONS
Klaver, D.C. ; Kusters, C.S.L. ; Pradhan, M. ; Vigh, M. ; Groot Bruinderink, M. ; Rossum, I. van; Böhnke, L. ; Wallaart, K. ; Malamas, S. ; Berkhout, E. ; Ni Wayan Suriasatini, ; Sikoki, B. ; Ginting, M.B. ; Mulia, M. ; Ningsih, K. ; Pujiastuti, S. ; Dwi Andari, B. ; Suprobo, N. ; Priyahita, W. ; Sihombing, R.R. ; Rokhmatulloh, S.W. ; Rosita, I. ; Wieriks, M. ; Smidt, H. ; Nugroho, K. ; Prasetyo, K. ; Larastiti, C. ; Amir, S. ; Sutikno, - \ 2015
Wageningen : Centre for Development Innovation, Wageningen UR (CDI rapporten )
This report on Indonesia is one of a series of evaluation reports, consisting of ten reports in total, reflecting the results of the jointly-organised MFS II evaluation: - eight country reports (India, Bangladesh, Ethiopia, Uganda, Indonesia, DR Congo, Liberia, Pakistan); - a synthesis report (covering the eight country studies); and - a report with the results of the international lobbying and advocacy programmes. This series of reports assessed the 2011-2015 contribution of the Dutch Co-Financing System (MFS II) towards achieving the Millennium Development Goals, strengthening international civil society, setting the international agenda and changing decision-makers’ policy and practice, with the ultimate goal of reducing structural poverty. On July 2nd, 2015, the reports were approved by the independent steering committee (see below), which concluded that they meet the quality standards of validity, reliability and usefulness set by the Ministry of Foreign Affairs.
Isolation and characterization of two germacrene A synthase cDNA clones from chicory1
Bouwmeester, H.J. ; Kodde, J. ; Verstappen, F.W.A. ; Altug, I.G. ; Kraker, J.W. de; Wallaart, T.E. - \ 2002
Plant Physiology 129 (2002). - ISSN 0032-0889 - p. 134 - 144.
Isolation and characterization of two germacrene A synthase genes from chicory (Cichorium intybus L)
Bouwmeester, H.J. ; Kodde, J. ; Verstappen, F.W.A. ; Altug, I.G. ; Kraker, J.W. de; Wallaart, E.T. - \ 2002
Plant Physiology 129 (2002). - ISSN 0032-0889 - p. 134 - 144.
Chicory (Cichorium intybus) sesquiterpene lactones were recently shown to be derived from a common sesquiterpene intermediate, ( )-germacrene A. Germacrene A is of interest because of its key role in sesquiterpene lactone biosynthesis and because it is an enzyme-bound intermediate in the biosynthesis of a number of phytoalexins. Using polymerase chain reaction with degenerate primers, we have isolated two sesquiterpene synthases from chicory that exhibited 72 amino acid identity. Heterologous expression of the genes in Escherichia coli has shown that they both catalyze exclusively the formation of ( )-germacrene A, making this the first report, to our knowledge, on the isolation of ( )-germacrene A synthase (GAS)-encoding genes. Northern analysis demonstrated that both genes were expressed in all chicory tissues tested albeit at varying levels. Protein isolation and partial purification from chicory heads demonstrated the presence of two GAS proteins. On MonoQ, these proteins co-eluted with the two heterologously produced proteins. The Km value, pH optimum, and MonoQ elution volume of one of the proteins produced in E. coli were similar to the values reported for the GAS protein that was recently purified from chicory roots. Finally, the two deduced amino acid sequences were modeled, and the resulting protein models were compared with the crystal structure of tobacco (Nicotiana tabacum) 5-epi-aristolochene synthase, which forms germacrene A as an enzyme-bound intermediate en route to 5-epi-aristolochene. The possible involvement of a number of amino acids in sesquiterpene synthase product specificity is discussed.
Amorpha-4,11-diene synthase: cloning and functional expression of a key enzyme in the biosynthetic pathway of the novel antimalarial drug artemisinin
Wallaart, T.E. ; Bouwmeester, H.J. ; Hille, J. ; Poppinga, L. ; Maijers, N.C.A. - \ 2001
Planta 212 (2001)3. - ISSN 0032-0935 - p. 460 - 465.
The sesquiterpenoid artemisinin, isolated from the plant Artemisia annua L., and its semi-synthetic derivatives are a new and very effective group of antimalarial drugs. A branch point in the biosynthesis of this compound is the cyclisation of the ubiquitous precursor farnesyl diphosphate into the first specific precursor of artemisinin, namely amorpha-4,11-diene. Here we describe the isolation of a cDNA clone encoding amorpha-4,11-diene synthase. The deduced amino acid sequence exhibits the highest identity (50%) with a putative sesquiterpene cyclase of A. annua. When expressed in Escherichia coli, the recombinant enzyme catalyses the formation of amorpha-4,11-diene from farnesyl diphosphate. Introduction of the gene into tobacco (Nicotiana tabacum L.) resulted in the expression of an active enzyme and the accumulation of amorpha-4,11-diene ranging from 0.2 to 1.7 ng per g fresh weight.
Characterization of the first step in the biosynthesis of artemisinin, an antimalarial drug from Artemisia annua L
Bouwmeester, H.J. ; Janssen, M.H.A. ; Wallaart, E. ; Loo, B. van; Jansen, B.J.M. ; Posthumus, M.A. ; Schmidt, C.O. ; Kraker, J.W. de; König, W.A. ; Franssen, M.C.R. - \ 2000
In: Exploration of biosynthetic pathways in nature-based drug research : 24th LOF-Symposium, Groningen, 24 maart, 2000
Amorpha-4,11-diene synthase catalyses the first probable step in artemisinin biosynthesis
Bouwmeester, H.J. ; Wallaart, T.E. ; Janssen, M.H.A. ; Loo, B. van; Jansen, B.J.M. ; Posthumus, M.A. ; Schmidt, C.O. ; Kraker, J.W. de; König, W.A. ; Franssen, M.C.R. - \ 1999
Phytochemistry 52 (1999). - ISSN 0031-9422 - p. 843 - 854.
The endoperoxide sesquiterpene lactone artemisinin and its derivatives are a promising new group of drugs against malaria. Artemisinin is a constituent of the annual herb Artemisia annua L. So far only the later steps in artemisinin biosynthesis — from artemisinic acid — have been elucidated and the expected olefinic sesquiterpene intermediate has never been demonstrated. In pentane extracts of A. annua leaves we detected a sesquiterpene with the mass spectrum of amorpha-4,11-diene. Synthesis of amorpha-4,11-diene from artemisinic acid confirmed the identity. In addition we identified several sesquiterpene synthases of which one of the major activities catalysed the formation of amorpha-4,11-diene from farnesyl diphosphate. This enzyme was partially purified and shows the typical characteristics of sesquiterpene synthases, such as a broad pH optimum around 6.5–7.0, a molecular mass of 56 kDa, and a Km of 0.6 μM. The structure and configuration of amorpha-4,11-diene, its low content in A. annua and the high activity of amorpha-4,11-diene synthase all support that amorpha-4,11-diene is the likely olefinic sesquiterpene intermediate in the biosynthesis of artemisinin.
Characterization of the first step in the biosynthesis of artemisinin, an antimalarial drug from Artemisia annua L
Bouwmeester, H.J. ; Janssen, M.H.A. ; Wallaart, E. ; Loo, B. van; Jansen, B.J.M. ; Posthumus, M.A. ; Schmidt, C.O. ; Kraker, J.W. de; König, W.A. ; Franssen, M.C.R. - \ 1999
In: Joint meeting of the ASP, AFERP, GA and PSE 2000 Years of Natural Product Research - Past, Present and Future, Amsterdam, 26-30 juli 1999. - [S.l.] : [s.n.], 1999
Characterization of the first step in the biosynthesis of artemisinin, an antimalarial drug from Artemisia annua L
Bouwmeester, H.J. ; Janssen, M.H.A. ; Wallaart, E. ; Loo, B. van; Jansen, B.J.M. ; Posthumus, M.A. ; Schmidt, C.O. ; Kraker, J.W. de; König, W.A. ; Franssen, M.C.R. - \ 1999
In: 4th European Symposium on Plant isoprenoids, Barcelona, 21-23 April, 1999. - [S.l.]: [s.n.], 1999
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