Aromatic amino acids at the surface of InlB are essential for host cell invasion by Listeria monocytogenes

Machner MP, Frese S, Schubert WD, Orian-Rousseau V, Gherardi E, Wehland J, Niemann H, Heinz DW (2003)
Mol Microbiol 48(6): 1525-1536.

Download
Es wurde kein Volltext hochgeladen. Nur Publikationsnachweis!
Zeitschriftenaufsatz | Veröffentlicht | Englisch
Autor
; ; ; ; ; ; ;
Erscheinungsjahr
Zeitschriftentitel
Mol Microbiol
Band
48
Zeitschriftennummer
6
Seite
1525-1536
PUB-ID

Zitieren

Machner MP, Frese S, Schubert WD, et al. Aromatic amino acids at the surface of InlB are essential for host cell invasion by Listeria monocytogenes. Mol Microbiol. 2003;48(6):1525-1536.
Machner, M. P., Frese, S., Schubert, W. D., Orian-Rousseau, V., Gherardi, E., Wehland, J., Niemann, H., et al. (2003). Aromatic amino acids at the surface of InlB are essential for host cell invasion by Listeria monocytogenes. Mol Microbiol, 48(6), 1525-1536. doi:10.1046/j.1365-2958.2003.03532.x
Machner, M. P., Frese, S., Schubert, W. D., Orian-Rousseau, V., Gherardi, E., Wehland, J., Niemann, H., and Heinz, D. W. (2003). Aromatic amino acids at the surface of InlB are essential for host cell invasion by Listeria monocytogenes. Mol Microbiol 48, 1525-1536.
Machner, M.P., et al., 2003. Aromatic amino acids at the surface of InlB are essential for host cell invasion by Listeria monocytogenes. Mol Microbiol, 48(6), p 1525-1536.
M.P. Machner, et al., “Aromatic amino acids at the surface of InlB are essential for host cell invasion by Listeria monocytogenes”, Mol Microbiol, vol. 48, 2003, pp. 1525-1536.
Machner, M.P., Frese, S., Schubert, W.D., Orian-Rousseau, V., Gherardi, E., Wehland, J., Niemann, H., Heinz, D.W.: Aromatic amino acids at the surface of InlB are essential for host cell invasion by Listeria monocytogenes. Mol Microbiol. 48, 1525-1536 (2003).
Machner, M. P., Frese, S., Schubert, W. D., Orian-Rousseau, V., Gherardi, E., Wehland, J., Niemann, Hartmut, and Heinz, D. W. “Aromatic amino acids at the surface of InlB are essential for host cell invasion by Listeria monocytogenes”. Mol Microbiol 48.6 (2003): 1525-1536.

30 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Adhesins and invasins of pathogenic bacteria: a structural view.
Niemann HH, Schubert WD, Heinz DW., Microbes Infect 6(1), 2004
PMID: 14738899
Folding and stability of the leucine-rich repeat domain of internalin B from Listeri monocytogenes.
Freiberg A, Machner MP, Pfeil W, Schubert WD, Heinz DW, Seckler R., J Mol Biol 337(2), 2004
PMID: 15003459
Characterization of the calcium-binding sites of Listeria monocytogenes InlB.
Marino M, Banerjee M, Copp J, Dramsi S, Chapman T, van der Geer P, Cossart P, Ghosh P., Biochem Biophys Res Commun 316(2), 2004
PMID: 15020228
GW domains of the Listeria monocytogenes invasion protein InlB are required for potentiation of Met activation.
Banerjee M, Copp J, Vuga D, Marino M, Chapman T, van der Geer P, Ghosh P., Mol Microbiol 52(1), 2004
PMID: 15049825

66 References

Daten bereitgestellt von Europe PubMed Central.

Structure of internalin, a major invasion protein of Listeria monocytogenes, in complex with its human receptor E-cadherin.
Schubert WD, Urbanke C, Ziehm T, Beier V, Machner MP, Domann E, Wehland J, Chakraborty T, Heinz DW., Cell 111(6), 2002
PMID: 12526809
InIB-dependent internalization of Listeria is mediated by the Met receptor tyrosine kinase.
Shen Y, Naujokas M, Park M, Ireton K., Cell 103(3), 2000
PMID: 11081636
Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha.
Garrett TP, McKern NM, Lou M, Elleman TC, Adams TE, Lovrecz GO, Zhu HJ, Walker F, Frenkel MJ, Hoyne PA, Jorissen RN, Nice EC, Burgess AW, Ward CW., Cell 110(6), 2002
PMID: 12297049
Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains.
Ogiso H, Ishitani R, Nureki O, Fukai S, Yamanaka M, Kim JH, Saito K, Sakamoto A, Inoue M, Shirouzu M, Yokoyama S., Cell 110(6), 2002
PMID: 12297050
Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization.
Schlessinger J, Plotnikov AN, Ibrahimi OA, Eliseenkova AV, Yeh BK, Yayon A, Linhardt RJ, Mohammadi M., Mol. Cell 6(3), 2000
PMID: 11030354
Structural basis for FGF receptor dimerization and activation.
Plotnikov AN, Schlessinger J, Hubbard SR, Mohammadi M., Cell 98(5), 1999
PMID: 10490103
[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, 1997
Isolation, cDNA cloning, and overexpression of a 33-kD cell surface glycoprotein that binds to the globular "heads" of C1q.
Ghebrehiwet B, Lim BL, Peerschke EI, Willis AC, Reid KB., J. Exp. Med. 179(6), 1994
PMID: 8195709
Crystal structure at 1.7 A resolution of VEGF in complex with domain 2 of the Flt-1 receptor.
Wiesmann C, Fuh G, Christinger HW, Eigenbrot C, Wells JA, de Vos AM., Cell 91(5), 1997
PMID: 9393862
Protein-protein interactions in receptor activation and intracellular signalling.
Blundell TL, Burke DF, Chirgadze D, Dhanaraj V, Hyvonen M, Innis CA, Parisini E, Pellegrini L, Sayed M, Sibanda BL., Biol. Chem. 381(9-10), 2000
PMID: 11076027
Characterization of hepatocyte-growth-factor receptors on Meth A cells.
Komada M, Miyazawa K, Ishii T, Kitamura N., Eur. J. Biochem. 204(2), 1992
PMID: 1311683
Human growth hormone and extracellular domain of its receptor: crystal structure of the complex.
de Vos AM, Ultsch M, Kossiakoff AA., Science 255(5042), 1992
PMID: 1549776
Entry of Listeria monocytogenes into hepatocytes requires expression of inIB, a surface protein of the internalin multigene family.
Dramsi S, Biswas I, Maguin E, Braun L, Mastroeni P, Cossart P., Mol. Microbiol. 16(2), 1995
PMID: 7565087

Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®

Quellen

PMID: 12791136
PubMed | Europe PMC

Suchen in

Google Scholar