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3 ungesichtete Fragmente: Plagiat

[1.] Rlm/Fragment 034 16 - Diskussion
Bearbeitet: 4. December 2014, 20:20 (SleepyHollow02)
Erstellt: 4. December 2014, 20:20 SleepyHollow02
BauernOpfer, Fragment, Rlm, Ryo et al 2005, SMWFragment, Schutzlevel, ZuSichten

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Untersuchte Arbeit:
Seite: 34, Zeilen: 16-18
Quelle: Ryo et al 2005
Seite(n): 7523, Zeilen: right col.: 31 ff..
Ayala et al. have shown that Pin1 expression levels were tightly correlated with both a higher probability and a shorter period of tumor recurrence following radical [prostatectomy by a comprehensive immunohistochemical analysis.] Ayala et al. (12) have shown that Pin1 expression levels were tightly correlated with both a higher probability and a shorter period of tumor recurrence following radical prostatectomy by a comprehensive immunohistochemical analysis.

12. Ayala G,Wang D,Wulf G, et al.The prolyl isomerase Pin1is a novel prognostic marker in human prostate cancer. Cancer Res 2003;63:6244^51.

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(SleepyHollow02)

[2.] Rlm/Fragment 029 02 - Diskussion
Bearbeitet: 5. December 2014, 19:33 (SleepyHollow02)
Erstellt: 5. December 2014, 19:33 SleepyHollow02
Fragment, Rlm, Ryo et al 2002, SMWFragment, Schutzlevel, Verschleierung, ZuSichten

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Untersuchte Arbeit:
Seite: 29, Zeilen: 2-4
Quelle: Ryo et al 2002
Seite(n): 5281, Zeilen: left col: 1 ff.
Phosphorylation of proteins on serine/threonine residues preceding proline (pSer/Thr-Pro) is a key regulatory mechanism for the control of cell proliferation and transformation (49).

49) Blume-Jensen, P., and Hunter, T. Oncogenic kinase signalling. Nature (Lond.), 411:355–365, 2001.

Phosphorylation of proteins on serine/threonine residues preceding proline (pSer/Thr-Pro) is a key regulatory mechanism for the control of cell proliferation and transformation (6, 18, 22, 31).

6. Blume-Jensen, P., and T. Hunter. 2001. Oncogenic kinase signalling. Nature 411:355–365.

18. Hanahan, D., and R. A. Weinberg. 2000. The hallmarks of cancer. Cell 100:57–70.

22. Hunter, T. 1998. Prolyl isomerase and nuclear function. Cell 92:141–143.

31. Lu, K. P., Y. C. Liou, and X. Z. Zhou. 2002. Pinning down the prolinedirected phosphorylation signaling. Trends Cell Biol. 12:164–172.

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[3.] Rlm/Fragment 008 06 - Diskussion
Bearbeitet: 12. December 2014, 12:22 (SleepyHollow02)
Erstellt: 12. December 2014, 12:22 SleepyHollow02
BauernOpfer, Fragment, Landes, Rlm, SMWFragment, Schutzlevel, ZuSichten

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Seite: 8, Zeilen: 6-18
Quelle: Landes
Seite(n): 132, Zeilen: 14 ff.
Structural analysis of AR revealed that it contains three major functional domains. The N-terminal activation function (AF)-1 domain (residues 1–555) contains different binding sites for transcriptional regulators including coactivators of the p160 family coactivators, acetyltransferases such as cAMP response element (CREB)-binding protein/p300 acetyltransferases, nuclear receptor corepressor and silencing mediator of retinoid and thyroid hormone receptor . Downstream of the AF-1 lies the DNA-binding domain (DBD) (residues 556–624), which mediates sequence-specific binding to promoters and enhancers of target genes. The hinge region (residues 625–670) links the DBD to the C-terminal domain(8,9).

8) Beato M Gene regulation by steroid hormones. Cell.1989 Feb 10;56(3):335-44.

9) Griffin, J. E. & Wilson, J. D. in Williams Testbook of Endocrinology 9th edn (eds Wilson, J. D., Foster, D. W., Kronenberg, H. M. & Larsen, P. R.) 819–876 (W. B. Saunders & Co., Philadelphia, 1998).

AR contains three major functional domains. The N-terminal activation function-1 (AF-1) domain (residues 1-555) contains binding sites for transcriptional regulators including coactivators of the p 160 family, acetyltransferases including CBP / p300, and corepressors including N-CoR and SMRT (Glass and Rosenfeld, 2000; Heemers and Tindall, 2007; Lonard and O'malley, 2007). Downstream of the AF-1 lies the DNA-binding domain (DBD) (residues 556-624), which mediates sequence-specific binding to promoters and enhancers of target genes. The hinge region (residues 625-670) links the DBD to the C-terminal activation function 2 (AF-2), which resides within the AR ligand-binding domain (LBD) (residues 671-919).
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