Fold and Function of the InlB B-repeat

Ebbes M, Bleymüller W, Cernescu M, Noelker R, Brutschy B, Niemann H (2011)
Journal of Biological Chemistry 286(17): 15496-15506.

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DOI
Autor*in
Ebbes, MariaUniBi; Bleymüller, WillemUniBi; Cernescu, Mihaela; Noelker, Rolf; Brutschy, Bernd; Niemann, HartmutUniBi
Einrichtung
Centrum für Biotechnologie > Institut für Biochemie und Biotechnik
Fakultät für Chemie > Biochemie IV
Centrum für Biotechnologie > Arbeitsgruppe H. Niemann
Erscheinungsjahr
2011
Zeitschriftentitel
Journal of Biological Chemistry
Band
286
Ausgabe
17
Seite(n)
15496-15506
ISSN
0021-9258
eISSN
1083-351X
Page URI
https://pub.uni-bielefeld.de/record/2093288

Zitieren

Ebbes M, Bleymüller W, Cernescu M, Noelker R, Brutschy B, Niemann H. Fold and Function of the InlB B-repeat. Journal of Biological Chemistry. 2011;286(17):15496-15506.
Ebbes, M., Bleymüller, W., Cernescu, M., Noelker, R., Brutschy, B., & Niemann, H. (2011). Fold and Function of the InlB B-repeat. Journal of Biological Chemistry, 286(17), 15496-15506. https://doi.org/10.1074/jbc.M110.189951
Ebbes, Maria, Bleymüller, Willem, Cernescu, Mihaela, Noelker, Rolf, Brutschy, Bernd, and Niemann, Hartmut. 2011. “Fold and Function of the InlB B-repeat”. Journal of Biological Chemistry 286 (17): 15496-15506.
Ebbes, M., Bleymüller, W., Cernescu, M., Noelker, R., Brutschy, B., and Niemann, H. (2011). Fold and Function of the InlB B-repeat. Journal of Biological Chemistry 286, 15496-15506.
Ebbes, M., et al., 2011. Fold and Function of the InlB B-repeat. Journal of Biological Chemistry, 286(17), p 15496-15506.
M. Ebbes, et al., “Fold and Function of the InlB B-repeat”, Journal of Biological Chemistry, vol. 286, 2011, pp. 15496-15506.
Ebbes, M., Bleymüller, W., Cernescu, M., Noelker, R., Brutschy, B., Niemann, H.: Fold and Function of the InlB B-repeat. Journal of Biological Chemistry. 286, 15496-15506 (2011).
Ebbes, Maria, Bleymüller, Willem, Cernescu, Mihaela, Noelker, Rolf, Brutschy, Bernd, and Niemann, Hartmut. “Fold and Function of the InlB B-repeat”. Journal of Biological Chemistry 286.17 (2011): 15496-15506.

17 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

The Novel Internalins InlP1 and InlP4 and the Internalin-Like Protein InlP3 Enhance the Pathogenicity of Listeria monocytogenes.
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Etzold S, Kober OI, Mackenzie DA, Tailford LE, Gunning AP, Walshaw J, Hemmings AM, Juge N., Environ Microbiol 16(3), 2014
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Structural basis of MET receptor dimerization by the bacterial invasion protein InlB and the HGF/SF splice variant NK1.
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Rhodocetin-αβ-induced neuropilin-1-cMet association triggers restructuring of matrix contacts in endothelial cells.
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Single-molecule photobleaching reveals increased MET receptor dimerization upon ligand binding in intact cells.
Dietz MS, Haße D, Ferraris DM, Göhler A, Niemann HH, Heilemann M., BMC Biophys 6(1), 2013
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Engineered variants of InlB with an additional leucine-rich repeat discriminate between physiologically relevant and packing contacts in crystal structures of the InlB:MET complex.
Niemann HH, Gherardi E, Bleymüller WM, Heinz DW., Protein Sci 21(10), 2012
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Entry of Listeria monocytogenes in mammalian epithelial cells: an updated view.
Pizarro-Cerdá J, Kühbacher A, Cossart P., Cold Spring Harb Perspect Med 2(11), 2012
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