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Angaben zur Quelle [Bearbeiten]

Autor     Maofu Fu, Mahadev Rao, Kongming Wu, Chenguang Wang, Xueping Zhang, Mohamed Hessien, Yee-Guide Yeung, Daniel Gioeli, Michael J. Weber, and Richard G. Pestell
Titel    The Androgen Receptor Acetylation Site Regulates cAMP and AKT but Not ERK-induced Activity
Zeitschrift    J Biol Chem.
Ausgabe    279
Datum    9. Juli 2004
Nummer    28
Seiten    29436–29449
Anmerkung    Epub 2004 Apr 30
DOI    10.1074/jbc.M313466200
URL    http://www.jbc.org/content/279/28/29436.full.pdf+html

Literaturverz.   

no
Fußnoten    no
Fragmente    1


Fragmente der Quelle:
[1.] Rlm/Fragment 009 01 - Diskussion
Zuletzt bearbeitet: 2014-12-01 17:33:22 Singulus
Fragment, Fu et al 2004, Gesichtet, KomplettPlagiat, Rlm, SMWFragment, Schutzlevel sysop

Typus
KomplettPlagiat
Bearbeiter
Graf Isolan
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Untersuchte Arbeit:
Seite: 9, Zeilen: 1-12
Quelle: Fu et al 2004
Seite(n): 29436, Zeilen: right col. 10-24
The C-terminal region of the AR, the hinge region and ligand-binding domain (LBD) is responsible for ligand binding and receptor dimerization. The well conserved DNA binding domain consists of 68 amino acids with two zinc finger structures. In contrast to several other hormone-regulated nuclear receptors, the AR lacks an intrinsic activation function 2 in the LBD domain. The LBD domain, which consists of twelve α-helices, projects away from the hormone-binding pocket in the absence of ligand and undergoes substantial conformational changes in the presence of ligand . [sic] The folding of the most C-terminal helix 12 (H12) over the ligand-binding pocket in turn creates new structural surfaces that bind coactivators required for efficient trans-activation. The C-terminal region of the AR, including the hinge region and ligand-binding domain (LBD) is responsible for ligand binding and dimerization. The well conserved DNA binding domain consists of 68 amino acids with two zinc finger structures. The N-terminal region contributes to transcriptional activation through its activation function 1 (2). In contrast to several other hormone-regulated nuclear receptors, the AR lacks an intrinsic activation function 2 function in the LBD. The LBD, which consists of twelve α-helices, projects away from the hormone-binding pocket in the absence of ligand and undergoes substantial conformational changes in the presence of ligand (3). The folding of the most C-terminal helix 12 (H12) over the ligand-binding pocket in turn creates new structural surfaces that bind coactivators required for efficient trans-activation.

2. Alen, P., Claessens, F., Verhoeven, G., Rombauts, W., and Peeters, B. (1999) Mol. Cell. Biol. 19, 6085–6097

3. Marhefka, C. A., Moore, B. M., 2nd, Bishop, T. C., Kirkovsky, L., Mukherjee, A., Dalton, J. T., and Miller, D. D. (2001) J. Med. Chem. 44, 1729–1740

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(Graf Isolan), SleepyHollow02

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