Zobrazeno 1 - 10
of 113
pro vyhledávání: '"Folkers, G.E."'
Akademický článek
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The nucleotide excision repair protein complex ERCC1-XPF is required for incision of DNA upstream of DNA damage. Functional studies have provided insights into the binding of ERCC1-XPF to various DNA substrates. However, because no structure for the
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https://explore.openaire.eu/search/publication?articleId=core_ac_uk__::68c8110ba3ebbd1559ca1f60e25435fe
Akademický článek
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Autor:
Huang, A., de Jong, R.N., Folkers, G.E., Boelens, R., NMR Spectroscopy, Sub NMR Spectroscopy, Dep Scheikunde
Publikováno v:
Journal of Structural Biology, 172(1), 120. Academic Press Inc.
We summarize the use of NMR spectroscopy in the production and the screening of stability and foldedness of protein domains, and apply it to the RING domains of E3 ubiquitin-ligases. RING domains are involved in specific interactions with E2 ubiquiti
Akademický článek
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To maintain the integrity of the genome, multiple DNA repair systems exist to repair damaged DNA. Recognition of altered DNA, including bulky adducts, pyrimidine dimers and interstrand crosslinks (ICL), partially depends on proteins containing helix-
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______101::12350f8f5c42d5c74d5ecdd6a9ae5ceb
https://dspace.library.uu.nl/handle/1874/290383
https://dspace.library.uu.nl/handle/1874/290383
Autor:
Das, D., Folkers, G.E., van Dijk, M., Jaspers, N.G.J., Hoeijmakers, J.H.J., Kaptein, R., Boelens, R., NMR Spectroscopy, Dep Scheikunde, Sub NMR Spectroscopy
Publikováno v:
Das, D, Folkers, G, van Dijk, M, Jaspers, N G J, Hoeijmakers, J H J, Kaptein, R & Boelens, R 2012, ' The structure of the XPF-ssDNA complex underscores the distinct roles of the XPF and ERCC1 helix-hairpin-helix domains in ss/ds DNA recognition ', Structure, vol. 20, no. 4, pp. 667-75 . https://doi.org/10.1016/j.str.2012.02.009
Structure, 20(4), 667-675. Cell Press
Structure, 20(4), 667-75. Cell Press
Structure, 20(4), 667. Cell Press
Structure
Structure, 20(4), 667-675. Cell Press
Structure, 20(4), 667-75. Cell Press
Structure, 20(4), 667. Cell Press
Structure
SummaryHuman XPF/ERCC1 is a structure-specific DNA endonuclease that nicks the damaged DNA strand at the 5′ end during nucleotide excision repair. We determined the structure of the complex of the C-terminal domain of XPF with 10 nt ssDNA. A positi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ab80c0b680c3a6b6ffe3861ddcc36eee
https://research.vu.nl/en/publications/72e213d4-9b4f-4c24-8bd0-6ab0d952717b
https://research.vu.nl/en/publications/72e213d4-9b4f-4c24-8bd0-6ab0d952717b
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
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
http://hdl.handle.net/11581/234478
Autor:
Berger, I., Blanco, A.G., Boelens, R., Cavarelli, J., Coll, M., Folkers, G.E., Nie, Y., Pogenberg, V., Schultz, P., Wilmanns, M., Moras, D., Poterszman, A., NMR Spectroscopy, Sub NMR Spectroscopy
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
Journal of Structural Biology, 175(2), 135. Academic Press Inc.
instname
Journal of Structural Biology, 175(2), 135. Academic Press Inc.
Control of transcription allows the regulation of cell activity in response to external stimuli and research in the field has greatly benefited from efforts in structural biology. In this review, based on specific examples from the European SPINE2-CO
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc9b4672cc741d2e8d8b91d7af51f983
http://hdl.handle.net/10261/87719
http://hdl.handle.net/10261/87719
Escherichia coli (E. coli) remains the most commonly used host for recombinant protein expression. It is well known that a variety of experimental factors influence the protein production level as well as the solubility profile of over-expressed prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=od_______101::b0f4e7546f41b500bc6906a40acd2ae5
https://dspace.library.uu.nl/handle/1874/213123
https://dspace.library.uu.nl/handle/1874/213123