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Membrane androgen receptor activation triggers pro-apoptotic responses in vitro and in vivo and blocks migration in colon cancer

von S. G.

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[1.] Shg/Fragment 035 01 - Diskussion
Zuletzt bearbeitet: 2014-11-02 01:26:58 Hindemith
Fragment, Gesichtet, KomplettPlagiat, SMWFragment, Saarikangas et al 2010, Schutzlevel sysop, Shg

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KomplettPlagiat
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Graf Isolan
Gesichtet
Yes.png
Untersuchte Arbeit:
Seite: 35, Zeilen: 1-3
Quelle: Saarikangas et al 2010
Seite(n): 271, Zeilen: li.Sp. 1-9
[RhoA induces actin polymerization at focal adhesions by activating the Dia1 formin and inhibits actin filament disassembly by initiating a signaling cascade that leads to phosphorylation and subsequent inactivation of the ADF/cofilin family of actin filament severing/depolymerizing proteins through the action of LIM kinases [Hotulainen P, Lappalainen P. 2006, Mahaffy] RE, Pollard TD. 2008, Watanabe N, et al. 1999, Vardouli et al 2005]. Furthermore, RhoA promotes contractility by activating the myosin light-chain kinase through ROCK kinase [Totsukawa G, et al. 2000].

Hotulainen P, Lappalainen P. (2006). Stress fibers are generated by two distinct actin assembly mechanisms in motile cells. J Cell Biol 173: 383–394.

Mahaffy RE, Pollard TD. (2008). Influence of phalloidin on the formation of actin filament branches by Arp2/3 complex. Biochemistry 47: 6460–6467.

Totsukawa G, Yamakita Y, Yamashiro S, Hartshorne DJ, Sasaki Y, Matsumura F. (2000). Distinct roles of ROCK (Rho-kinase) and MLCK in spatial regulation of MLC phosphorylation for assembly of stress fibers and focal adhesions in 3T3 fibroblasts. J Cell Biol 150: 797–806.

Watanabe N, Kato T, Fujita A, Ishizaki T, Narumiya S. (1999). Cooperation between mDia1 and ROCK in Rho-induced actin reorganization. Nat Cell Biol 1: 136–143.

RhoA induces actin polymerization at focal adhesions by activating the Dia1 formin and inhibits actin filament disassembly by initiating a signaling cascade that leads to phosphorylation and subsequent inactivation of the ADF/cofilin family of actin filament severing/depolymerizing proteins through the action of LIM kinases (146, 230, 383). Furthermore, RhoA promotes contractility by activating the myosin light-chain kinase through ROCK kinase (364).

146. Hotulainen P, Lappalainen P. Stress fibers are generated by two distinct actin assembly mechanisms in motile cells. J Cell Biol 173: 383–394, 2006.

230. Maekawa M, Ishizaki T, Boku S, Watanabe N, Fujita A, Iwamatsu A, Obinata T, Ohashi K, Mizuno K, Narumiya S. Signaling from Rho to the actin cytoskeleton through protein kinases ROCK and LIM-kinase. Science 285: 895–898, 1999.

231. Mahaffy RE, Pollard TD. Influence of phalloidin on the formation of actin filament branches by Arp2/3 complex. Biochemistry 47: 6460–6467, 2008.

364. Totsukawa G, Yamakita Y, Yamashiro S, Hartshorne DJ, Sasaki Y, Matsumura F. Distinct roles of ROCK (Rho-kinase) and MLCK in spatial regulation of MLC phosphorylation for assembly of stress fibers and focal adhesions in 3T3 fibroblasts. J Cell Biol 150: 797–806, 2000.

383. Watanabe N, Kato T, Fujita A, Ishizaki T, Narumiya S. Cooperation between mDia1 and ROCK in Rho-induced actin reorganization. Nat Cell Biol 1: 136–143, 1999.

Anmerkungen

Ohne Hinweis auf eine Übernahme. Schließt die auf der vorangegangenen Seite begonnene Übernahme ab.

Im Literaturverzeichnis von Shg findet sich keine Referenz für "Vardouli et al 2005". Beim Versuch, die Referenz [230] zu kopieren, hat sich Shg vertan und stattdessen die unter [231] stehende Referenz übernommen.

Sichter
(Graf Isolan), SleepyHollow02

[2.] Shg/Fragment 035 04 - Diskussion
Zuletzt bearbeitet: 2014-11-03 14:57:14 Hindemith
Bailly 2003, Fragment, Gesichtet, KomplettPlagiat, SMWFragment, Schutzlevel sysop, Shg

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SleepyHollow02
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Untersuchte Arbeit:
Seite: 35, Zeilen: 4-18
Quelle: Bailly 2003
Seite(n): 163, 165, Zeilen: 163: left col., 27 ff.; 165: left col., 10 ff.
Focal complexes are regulated by signaling via Rac1 or cdc42 small GTPases and are marked by the early recruitment of vinculin [J.V. Small et al. 2002 and C.D. Nobes and A. Hall. 1995]. Vinculin is a large protein that contains binding domains for multiple cytoskeletal proteins, including actin, α-actinin, talin, paxillin, VASP, ponsin, vinexin and protein kinase C (PKC) [D.R. Critchley. 2000 and B. Geiger et al. 2001]. Its head and tail regions physically interact in a resting state to mask most binding sites [D.R. Critchley. 2000]. The open, ‘activated’, conformation of vinculin is revealed by exposure to PIP2 and exposes all binding sites. Past studies have revealed that vinculin plays a central role in mechanical coupling of integrins to the cytoskeleton, as well as in the control of cytoskeletal mechanics, cell shape, and protrusion amplitude and cell motility. Vinculin binding to the arp2/3 complex might be but one way that the actin-nucleation machinery can be coupled to new sites of adhesion, and testing this hypothesis now presents cell biologists from different fields with a fascinating new challenge.

Small JV, Stradal T, Vignal E, Rottner K. (2002). The lamellipodium: where motility begins. Trends Cell Biol. 12, pp. 112–120.

D.R. Critchley, (2000). Focal adhesions – the cytoskeletal connection. Curr. Opin. Cell Biol. 12, pp. 133–139.

C.D. Nobes and A. Hall, (1995). Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81, pp. 53–62.

Geiger B, Bershadsky A, Pankov R, Yamada KM. (2001).Transmembrane crosstalk between the extracellular matrix–cytoskeleton crosstalk. Nat. Rev. Mol. Cell Biol. 2, pp. 793–805.

Focal complexes are regulated by signaling via Rac1 or cdc42 small GTPases and are marked by the early recruitment of vinculin [3,6]. Vinculin is a large protein that contains binding domains for multiple cytoskeletal proteins, including actin, α-actinin, talin, paxillin, VASP, ponsin, vinexin and protein kinase C (PKC) [7,8]. Its head and tail regions physically interact in a resting state to mask most binding sites [7]. The open, ‘activated’, conformation of vinculin is revealed by exposure to phosphatidylinositol (4,5)-bisphosphate (PIP2) and exposes all binding sites. Past studies have revealed that vinculin plays a central role in mechanical coupling of integrins to the cytoskeleton, as well as in the control of cytoskeletal mechanics, cell shape, protrusion amplitude and cell motility [7].

[Seite 165]

Vinculin binding to the arp2/3 complex might be but one way that the actin-nucleation machinery can be coupled to new sites of adhesion, and testing this hypothesis now presents cell biologists from different fields with a fascinating new challenge.


3 Small, J.V. et al. (2002) The lamellipodium: where motility begins. Trends Cell Biol. 12, 112–120

6 Nobes, C.D. and Hall, A. (1995) Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81, 53–62

7 Critchley, D.R. (2000) Focal adhesions – the cytoskeletal connection. Curr. Opin. Cell Biol. 12, 133–139

8 Geiger, B. et al. (2001) Transmembrane crosstalk between the extracellular matrix–cytoskeleton crosstalk. Nat. Rev. Mol. Cell Biol. 2, 793–805

Anmerkungen

Ein Verweis auf die Quelle fehlt.

Sichter
(SleepyHollow02), Hindemith

[3.] Shg/Fragment 035 20 - Diskussion
Zuletzt bearbeitet: 2014-12-13 20:28:05 Hindemith
Fragment, Gesichtet, KomplettPlagiat, SMWFragment, Schutzlevel sysop, Shg, Wikipedia Caco-2 2009

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Graf Isolan
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Untersuchte Arbeit:
Seite: 35, Zeilen: 20-22
Quelle: Wikipedia Caco-2 2009
Seite(n): 1 (Internetquelle), Zeilen: -
The Caco-2 cell line is an immortalized line of heterogeneous human epithelial colorectal adenocarcinoma cells, developed by the Sloan-Kettering Institute for Cancer Research through research conducted by Dr. Jorgen Fogh. The Caco-2 cell line is an immortalized line of heterogeneous human epithelial colorectal adenocarcinoma cells, developed by the Sloan-Kettering Institute for Cancer Research through research conducted by Dr. Jorgen Fogh.
Anmerkungen

Ohne Hinweis auf eine Übernahme. Bemerkenswert ist die Übernahme des akademischen Grads aus der WP in die Dissertation, ein sonst in wissenschaftlichen Texten ganz unübliches Verfahren, das sich auch in der Diss an keiner anderen Stelle findet.

Sichter
(Graf Isolan), SleepyHollow02


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