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 > Arbeitsgruppe H. Niemann
Fakultät für Chemie > Biochemie IV
Centrum für Biotechnologie > Institut für Biochemie und Biotechnik
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.
Niemann HH., Biochim Biophys Acta 1834(10), 2013
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Rhodocetin-αβ-induced neuropilin-1-cMet association triggers restructuring of matrix contacts in endothelial cells.
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Reassessment of the Listeria monocytogenes pan-genome reveals dynamic integration hotspots and mobile genetic elements as major components of the accessory genome.
Kuenne C, Billion A, Mraheil MA, Strittmatter A, Daniel R, Goesmann A, Barbuddhe S, Hain T, Chakraborty T., BMC Genomics 14(), 2013
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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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