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Typus
KomplettPlagiat
Bearbeiter
Hindemith
Gesichtet
Yes.png
Untersuchte Arbeit:
Seite: 5, Zeilen: 20-30
Quelle: Wanken 2003
Seite(n): 11, Zeilen: 5ff
In addition to point mutations that are unique to individual strains, large gene clusters are present in some strains but not in others (Gressmann et al., 2005). Early studies revealed that about 60% of H. pylori isolates produce an immunodominant 120-140 kDa protein of unknown function (CagA) (Cover et al., 1990; Crabtree et al., 1991). The cagA gene is located within an approximately 40 kb DNA segment called the cag pathogenicity island (PAI) (Akopyants et al., 1998; Censini et al., 1996). Many of the genes within the cag PAI help H. pylori activate proinflammatory signal transduction pathways in gastric epithelial cells (Segal et al., 1996, 1997), contributing to the host inflammatory response. Infection with strains that contain the cag PAI is more likely to result in clinical disease than is colonization with cag-negative strains (Covacci et al., 1993; Cover et al., [1990; Crabtree et al., 1991).]

Akopvants, N. S,, S. W, Clifton, D. Kersulvte, J. E. Crabtree, B. E. Youree, C. A. Reece, N. O. Bukanov, E. S. Drazek, B. A. Roe, and D. E. Berg, Analyses of the eag pathogenicity island of Helicobacter pylori, Mol Microbiol, 28, 37-53, 1998.

Censini, S,, C, Lange, Z, Xiang, J, E, Crabtree, P, Ghiara, M, Borodovskv, R, Rap- puoli, and A, Covaeei, cag, a pathogenicity island of Helicobacter pylori, encodes type I-speeihe and disease-associated virulence factors, Proc Natl Acad Sci U S A, 93, 14,648-14,653, 1996.

Covacci, A,, S, Censini, M, Bugnoli, E, Petracca, D, Burroni, G, Macchia, A, Mas- sone, E, Papini, Z, Xiang, and N, Figura, Molecular characterization of the 128- kda immunodominant antigen of Helicobacter pylori associated with cytotoxicity and duodenal ulcer, Proc Natl Acad Sci U S A, 90, 5791-5795, 1993,

Cover, T, L,, C, P, Dooley, and M, J, Blaser, Characterization of and human serologic response to proteins in Helicobacter pylori broth culture supernatants with vacuolizing cytotoxin activity, Infect Immun, 58, 603-610, 1990,

Crabtree, J, E,, J, D, Taylor, J, I, Wyatt, E, V, Heatlev, T, M, Shalleross, D, S, Tompkins, and B, J, Eathbone, Mucosal iga recognition of Helicobacter pylori 120 kda protein, peptic ulceration, and gastric pathology, Lancet, 338, 332-335, 1991,

Gressmann, H,, B, Linz, R, Ghai, K, P, Pleissner, R, Sehlapbaeh, Y, Yamaoka, C. Kraft, S. Suerbaum, T, F, Meyer, and M, Aehtman, Gain and loss of multiple genes during the evolution of Helicobacter pylori, PLoS Genet, 1, 2005.

Segal, E. D,, S. Falkow, and L. S. Tompkins, Helicobacter pylori attachment to gastric cells induces evtoskeletal rearrangements and tyrosine phosphorylation of host cell proteins, Proc Natl Acad Sci U S A, 93, 1259-1264, 1996.

Segal, E. D,, C. Lange, A. Covaeei, L. S. Tompkins, and S. Falkow, Induction of host signal transduction pathways by Helicobacter pylori, Proc Natl Acad Sci U S A, 94, 7595-7599, 1997.

In addition to point mutations that are unique to individual strains, large gene clusters are present in some strains but not in others. Early studies revealed that about 60% of H. pylori isolates produce an immunodominant 120-140 kDa protein of unknown function (CagA) (35, 36). The cagA gene is located within an approximately 40 kb DNA segment called the cag pathogenicity island (PAI) (2, 23). Many of the genes within the cag PAI help H. pylori activate proinflammatory signal transduction pathways in gastric epithelial cells (145, 146), contributing to the host inflammatory response. Infection with strains that contain the cag PAI is more likely to result in clinical disease than is colonization with cag-negative strains (33, 35, 36). Therefore, the presence or absence of the cag PAI is an important characteristic among H. pylori strains.

2. Akopyants, N. S., S. W. Clifton, D. Kersulyte, J. E. Crabtree, B. E. Youree, C. A. Reece, N. O. Bukanov, E. S. Drazek, B. A. Roe, and D. E. Berg. 1998. Analyses of the cag pathogenicity island of Helicobacter pylori. Mol. Microbiol. 28:37-53.

23. Censini, S., C. Lange, Z. Xiang, J. E. Crabtree, P. Ghiara, M. Borodovsky, R. Rappuoli, and A. Covacci. 1996. cag, a pathogenicity island of Helicobacter pylori, encodes type I-specific and disease-associated virulence factors. Proc. Natl. Acad. Sci. U.S.A. 93:14648-14653.

33. Covacci, A., S. Censini, M. Bugnoli, R. Petracca, D. Burroni, G. Macchia, A. Massone, E. Papini, Z. Xiang, N. Figura, and e. al. 1993. Molecular characterization of the 128-kDa immunodominant antigen of Helicobacter pylori associated with cytotoxicity and duodenal ulcer. Proc. Natl. Acad. Sci. U.S.A. 90:5791-5795.

35. Cover, T. L., C. P. Dooley, and M. J. Blaser. 1990. Characterization of and human serologic response to proteins in Helicobacter pylori broth culture supernatants with vacuolizing cytotoxin activity. Infect. Immun. 58:603-610.

36. Crabtree, J. E., J. D. Taylor, J. I. Wyatt, R. V. Heatley, T. M. Shallcross, L. S. Tompkins, and B. J. Rathbone. 1991. Mucosal IgA recognition of Helicobacter pylori 120 kDa protein, peptic ulceration, and gastric pathology. Lancet 338:332-335.

145. Segal, E. D., S. Falkow, and L. S. Tompkins. 1995. Helicobacter pylori attachment to gastric cells induces cytoskeletal rearrangements and tyrosine phosphorylation of host cell proteins. Proc. Natl. Acad. Sci. U.S.A. 93:1259-1264.

146. Segal, E. D., C. Lange, A. Covacci, L. S. Tompkins, and S. Falkow. 1997. Induction of host signal transduction pathways by Helicobacter pylori. Proc. Natl. Acad. Sci. U.S.A. 94:7595-7599.

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