Structural changes of TasA in biofilm formation of Bacillus subtilis

Autor: Anne Diehl, Yvette Roske, Daniel Stöppler, Catherine L. Worth, Daniel Lopez, Linda J. Ball, Anup Chowdhury, Natalja Erdmann, Regina Kramer, Heike Stephanowitz, Martina Leidert, Eberhard Krause, Udo Heinemann, Ümit Akbey, Hartmut Oschkinat, Peter Schmieder, Barth-Jan van Rossum, Matthias Hiller, Kürşad Turgay, Noël Molière, Brigitte Schlegel, Nils Cremer

Publikováno v: Diehl, A, Roske, Y, Ball, L, Chowdhury, A, Hiller, M, Moliere, N, Kramer, R, Stoeppler, D, Worth, C L, Schlegel, B, Leidert, M, Cremer, N, Erdmann, N, Lopez, D, Stephanowitz, H, Krause, E, van Rossum, B-J, Schmieder, P, Heinemann, U, Turgay, K, Akbey, U & Oschkinat, H 2018, ' Structural changes of TasA in biofilm formation of Bacillus subtilis ', Proceedings of the National Academy of Sciences, vol. 115, no. 13, pp. 3237-3242 . https://doi.org/10.1073/pnas.1718102115
Proceedings of the National Academy of Sciences
Proceedings of the National Academy of Sciences of the United States of America 115 (2018), Nr. 13

Microorganisms form surface-attached communities, termed biofilms, which can serve as protection against host immune reactions or antibiotics. Bacillus subtilis biofilms contain TasA as major proteinaceous component in addition to exopolysaccharides.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c34ccb8f3a15688d594d5bfc646c50c
https://pure.au.dk/ws/files/171886691/3237.full.pdf

Structural insight into protein-aided bacterial biofilm formation

Autor: Yvette Roske, Udo Heinemann, Hartmut Oschkinat, Kürşad Turgay, Anne Diehl, Ümit Akbey, Linda J. Ball

Publikováno v: Acta Crystallographica Section A Foundations and Advances. 74:e206-e206

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::276ef4535d189b904699ac8e0232cabb
https://doi.org/10.1107/s2053273318092057

The scientific impact of the Structural Genomics Consortium: a protein family and ligand-centered approach to medically-relevant human proteins

Autor: Oppermann Uct., Michael Sundström, Brian D. Marsden, Declan A. Doyle, F. von Delft, Frank H. Niesen, Stefan Knapp, Susanne Müller, Linda J. Ball, Opher Gileadi, Wen Hwa Lee, Kathryn L. Kavanagh

Publikováno v: Journal of Structural and Functional Genomics

As many of the structural genomics centers have ended their first phase of operation, it is a good point to evaluate the scientific impact of this endeavour. The Structural Genomics Consortium (SGC), operating from three centers across the Atlantic,

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a695f629f294d1cba917f758cd6d881f
https://doi.org/10.1007/s10969-007-9027-2

Solution Structure of Human Cofilin

Autor: Alan G. Weeds, Karen M. Zierler-Gould, Brian Pope, Linda J. Ball, Ronald Kühne

Publikováno v: Journal of Biological Chemistry. 279:4840-4848

Human actin-depolymerizing factor (ADF) and cofilin are pH-sensitive, actin-depolymerizing proteins. Although 72% identical in sequence, ADF has a much higher depolymerizing activity than cofilin at pH 8. To understand this, we solved the structure o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::0dd72c7f86446d3c409af22da51ad927
https://doi.org/10.1074/jbc.m310148200

Normalization of nomenclature for peptide motifs as ligands of modular protein domains

Autor: Ulrich Walter, Makoto Nagai, Thomas Jarchau, Marius Sudol, Rune Linding, Mark A. Lemmon, Gianni Cesareni, Christophe Ampe, James H. Hurley, Steve J. Winder, Rein Aasland, Mark T. Bedford, Charles S. Abrams, Linda J. Ball, Mario Gimona, Bruce J. Mayer, Veli-Pekka Lehto

Publikováno v: FEBS Letters. 513:141-144

We propose a normalization of symbols and terms used to describe, accurately and succinctly, the detailed interactions between amino acid residues of pairs of interacting proteins at protein:protein (or protein:peptide) interfaces. Our aim is to unif

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97b3c2892dc5a48a3e8ab5cb1daa5370
https://doi.org/10.1016/s0014-5793(01)03295-1