Novel mono-, di-, and trimethylornithine membrane lipids in northern wetland planctomycetes

Autor: Moore, E.K., Hopmans, E.C., Rijpstra, W.I.C., Villanueva, L., Dedysh, S.N., Kulichevskaya, I.S., Wienk, H.L.J., Schoutsen, F., Sinninghe Damsté, J.S., NMR Spectroscopy, non-UU output of UU-AW members, Sub NMR Spectroscopy, Organic geochemistry

Publikováno v: Applied and Environmental Microbiology, 79(22), 6874. American Society for Microbiology

Northern peatlands represent a significant global carbon store and commonly originate from Sphagnum moss-dominated wetlands. These ombrotrophic ecosystems are rain fed, resulting in nutrient-poor, acidic conditions. Members of the bacterial phylum Pl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed834b7024f81a1d23094c39730c12aa
https://pubmed.ncbi.nlm.nih.gov/23995937

Structure and function of a unique pore-forming protein from a pathogenic acanthamoeba

Autor: Michalek, M., Sönnichsen, F.D., Wechselberger, R.W., Wienk, H.L.J., Leippe, M., et al., [No Value]

Human pathogens often produce soluble protein toxins that generate pores inside membranes, resulting in the death of target cells and tissue damage. In pathogenic amoebae, this has been exemplified with amoebapores of the enteric protozoan parasite E

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______101::0c352ec8a753d292e985f70741165e7d
https://dspace.library.uu.nl/handle/1874/290300

Biophysical characterization of mutants of Bacillus subtilis lipase evolved for thermostability: Factors contributing to increased activity retention

Autor: Augustyniak, W., Brzezinska, A.A., Pijning, Tjaard, Wienk, H.L.J., Boelens, R., Dijkstra, Bauke W., Reetz, M.T., NMR Spectroscopy, Sub NMR Spectroscopy

Publikováno v: Protein Science, 21(4), 487. Cold Spring Harbor Laboratory Press

Previously, Lipase A from Bacillus subtilis was subjected to in vitro directed evolution using iterative saturation mutagenesis, with randomization sites chosen on the basis of the highest B-factors available from the crystal structure of the wild-ty

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=narcis______::e0aad8cea9fef4b233cdcc7415450ddf
https://dspace.library.uu.nl/handle/1874/256776

Structural dynamics of bacterial translation initiation factor IF2

Autor: Wienk, H.L.J., Tishchenko, E., Belardinelli, R., Tomaselli, S., Dongre, R., Spurio, R., Folkers, G.E., Gualerzi, C.O., Boelens, R., NMR Spectroscopy, Sub NMR Spectroscopy

Publikováno v: Journal of Biological Chemistry, 287(14), 10922. American Society for Biochemistry and Molecular Biology Inc.
Journal of biological chemistry (Online) 287 (2012): 10922–10932. doi:10.1074/jbc.M111.333393
info:cnr-pdr/source/autori:Wienk H., Tishchenko E., Belardinelli R., Tomaselli S., Dongre R., Spurio R., Folkers G.E., Gualerzi C.O., Boelens R.,/titolo:Structural dynamics of bacterial translation initiation factor IF2/doi:10.1074%2Fjbc.M111.333393/rivista:Journal of biological chemistry (Online)/anno:2012/pagina_da:10922/pagina_a:10932/intervallo_pagine:10922–10932/volume:287

Bacterial translation initiation factor IF2 promotes ribosomal subunit association, recruitment, and binding of fMet-tRNA to the ribosomal P-site and initiation dipeptide formation. Here, we present the solution structures of GDP-bound and apo-IF2-G2

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e868669c9a22b9b0ee4bc7f5edc2232b
http://hdl.handle.net/11581/234478

The tandem zinc-finger region of human ZHX adopts a novel C2H2 zinc finger structure with a C-terminal extension

Autor: Wienk, H.L.J., Lammers, I., Hotze, A.C.G., Wu, J., Wechselberger, R.W., Owens, R., Stammers, D.K., Stuart, D., Kaptein, R., Folkers, G.E., NMR Spectroscopy, NMR-spectroscopie, Sub NMR Spectroscopy, Dep Scheikunde

Publikováno v: Biochemistry, 48(21), 4431. American Chemical Society : Division of Carbohydrate Chemistry

Binding of the nuclear factor-Y complex (NF-Y) to the inverted CCAAT-box interferes with transcription activation through nucleosome reorganization. The three homologous proteins forming the zincfingers and homeoboxes (ZHX) family interact with the a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=narcis______::df250b0ab4de69ad98d8b3680bf22839
https://dspace.library.uu.nl/handle/1874/43889