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Typus
KomplettPlagiat
Bearbeiter
SleepyHollow02
Gesichtet
Yes.png
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

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