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Fragment-derived modulators of an industrial β-glucosidase

Autor: Makraki, E., Darby, J.F., Carneiro, M.G., Firth, J.D., Heyam, A., AB, E., O'Brien, P., Siegal, G., Hubbard, R.E.

A fragment screen of a library of 560 commercially available fragments using a kinetic assay identified a small molecule that increased the activity of the fungal glycoside hydrolase TrBgl2. An analogue by catalogue approach and detailed kinetic anal

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=core_ac_uk__::087b4070e6f8c49dd9001b707afee89c
https://eprints.whiterose.ac.uk/167686/8/bcj-2020-0507.pdf

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Akademický článek

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Catalysis by a rigid enzyme

Autor: Sybrin P. Schröder, Codée Jdc, Christopher A. Waudby, Ab E, Aerts Jmfg, van Ingen H, Alexander N. Volkov, Fredj Ben Bdira, Hermen S. Overkleeft, Marcellus Ubbink

Many enzymes are dynamic entities, sampling conformational states that are relevant for catalytic activity. Crystal structures of catalytic intermediates suggest, however, that not all enzymes require structural changes for activity. The single-domai

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1cf2046dc7c2858d32bbcbe42f6bc170
https://doi.org/10.1101/815415

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Akademický článek

NMR in the SPINE Structural Proteomics project.

Autor: AB, E.¹, Atkinson, A. R.², Banci, L.³, Bertini, I.³, Ciofi-Baffoni, S.³, Brunner, K.⁴, Diercks1, T., Dötsch, V.⁵, Engelke, F.⁶, Folkers, G. E.¹, Griesinger, C.⁷, Gronwald, W.⁴, Günther, U.⁵, Habeck, M.⁸, de Jong, R. N.¹, Kalbitzer, H. R.⁴, Kieffer, B.⁸, Leeflang, B. R.¹, Loss, S.⁹, Luchinat, C.³

Publikováno v: Acta Crystallographica: Section D (Wiley-Blackwell). Oct2006, Vol. 62 Issue 10, p1150-1161. 12p.

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Structure of the DNA-bound BRCA1 C-terminal Region from Human Replication Factor C p140 and Model of the Protein-DNA Complex

Autor: Kobayashi, M., AB, E., Bonvin, A.M.J.J., Siegal, G., NMR Spectroscopy, Dep Scheikunde, Sub NMR Spectroscopy

Publikováno v: Journal of Biological Chemistry, 285(13), 10087. American Society for Biochemistry and Molecular Biology Inc.
Journal of Biological Chemistry
Journal of Biological Chemistry, 285(13), 10087-10097

BRCA1 C-terminal domain (BRCT)-containing proteins are found widely throughout the animal and bacteria kingdoms where they are exclusively involved in cell cycle regulation and DNA metabolism. Whereas most BRCT domains are involved in protein-protein

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d08a71d510dfcc6346fcdbc430efa888
https://doi.org/10.1074/jbc.m109.054106

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Structure and DNA binding of the human Rtf1 Plus3 domain

Autor: de Jong, R.N., Truffault, V.P.M., Diercks, T., AB, E., Daniels, M.A., Kaptein, R., Folkers, G.E., NMR-spectroscopie, Dep Scheikunde

Publikováno v: Structure, 16(1), 149. Cell Press

The yeast Paf1 complex consists of Paf1, Rtf1, Cdc73, Ctr9, and Leo1 and regulates histone H2B ubiquitination, histone H3 methylation, RNA polymerase II carboxy-terminal domain (CTD) Ser2 phosphorylation, and RNA 3′ end processing. We provide struc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=narcis______::87982efb9c4385a487e524f7f4a13461
https://dspace.library.uu.nl/handle/1874/33204

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Solution structure and characterization of the DNA-binding activity of the B3BP–Smr domain

Autor: Diercks, T., AB, E., Daniels, M.A., de Jong, R.N., Besseling, R., Kaptein, R., Folkers, G.E.

The MutS1 protein recognizes unpaired bases and initiates mismatch repair, which are essential for high-fidelity DNA replication. The homologous MutS2 protein does not contribute to mismatch repair, but suppresses homologous recombination. MutS2 lack

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od_______101::8a48ad5b3824217e9bb8add99537402e
https://dspace.library.uu.nl/handle/1874/33233

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Direct use of unassigned resonances in NMR structure calculations with proxy residues

Autor: AB, E., Pugh, D.J.R., Kaptein, R., Boelens, R., Bonvin, A.M.J.J., NMR-spectroscopie, Dep Scheikunde

Publikováno v: Journal of the American Chemical Society, 128(23), 7566. American Chemical Society
Journal of the American Chemical Society

We present a method that significantly enhances the robustness of (automated) NMR structure determination by allowing the NOE data corresponding to unassigned NMR resonances to be used directly in the calculations. The unassigned resonances are repre

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f21213bae66ac6f71f8f3b84b7bb3438
https://pubmed.ncbi.nlm.nih.gov/16756312

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