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Angaben zur Quelle [Bearbeiten]

Autor     Lere Bao, Amy Kimzey, Guido Sauter, Janusz M. Sowadski, Kun Ping Lu, Da-Gong Wang
Titel    Prevalent Overexpression of Prolyl Isomerase Pin1 in Human Cancers
Zeitschrift    American Journal of Pathology
Ausgabe    164
Datum    May 2004
Nummer    5
Seiten    1727-1737
URL    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1615639/pdf/JPATH164001727.pdf

Literaturverz.   

no
Fußnoten    no
Fragmente    3


Fragmente der Quelle:
[1.] Rlm/Fragment 030 01 - Diskussion
Zuletzt bearbeitet: 2014-12-01 17:31:44 Singulus
Bao et al 2004, Fragment, Gesichtet, Rlm, SMWFragment, Schutzlevel sysop, Verschleierung

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Quelle: Bao et al 2004
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Pin1 is normally expressed at very low levels in most normal tissues, although significant levels of Pin1 are often found in cell types that normally undergo active cell division. Pin1 is overexpressed in some human malignancies and that its expression closely correlates with the level of cyclin D1 in human breast cancer (54).

54) Wulf, G. M., Ryo, A., Wulf, G. G., Lee, S. W., Niu, T., and Lu, K. P. Pin1 is overexpressed in breast cancer and potentiates the transcriptional activity of phosphorylatedc-Jun towards the cyclin D1 gene. EMBO J., 20: 3459–3472, 2001.

Recently, it has been reported that Pin1 is overexpressed in human breast cancer cell lines and breast cancer tissues, and its expression closely correlates with the level of cyclin D1 in tumors.15

[page 1731]

These results indicate that Pin1 is normally expressed at very low levels in most normal tissues, although significant levels of Pin1 are often found in cell types that normally undergo active cell division.


15. Wulf GM, Ryo A, Wulf GG, Lee SW, Niu T, Lu KP: Pin1 is overexpressed in breast cancer and potentiates the transcriptional activity of phosphorylated c-Jun towards the cyclin D1 gene. EMBO J 2001, 20:3459–3472

Anmerkungen

The source is not mentioned.

Sichter
(Hindemith), SleepyHollow02

[2.] Rlm/Fragment 048 01 - Diskussion
Zuletzt bearbeitet: 2014-12-01 16:33:13 SleepyHollow02
Bao et al 2004, Fragment, Gesichtet, KeineWertung, Rlm, SMWFragment, Schutzlevel

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Untersuchte Arbeit:
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Quelle: Bao et al 2004
Seite(n): 1727, Zeilen: 1227: r.col: 29 ff.  ; 1731: l.col: 6 ff.
Recently, it has been reported that Pin1 is overexpressed in human prostate cancer cell lines and prostate cancer tissues, and its expression closely correlates with the level of cyclin D1 in tumors. Recently, it has been reported that Pin1 is overexpressed in human breast cancer cell lines and breast cancer tissues, and its expression closely correlates with the level of cyclin D1 in tumors.15

15. Wulf GM, Ryo A, Wulf GG, Lee SW, Niu T, Lu KP: Pin1 is overexpressed in breast cancer and potentiates the transcriptional activity of phosphorylated c-Jun towards the cyclin D1 gene. EMBO J 2001, 20:3459–3472

Anmerkungen

The source is not mentioned.

By copying the passage from a seven year old source, the meaning of "recently" is somewhat stretched.

Sichter
(Hindemith), SleepyHollow02

[3.] Rlm/Fragment 049 01 - Diskussion
Zuletzt bearbeitet: 2015-02-08 20:46:57 Schumann
Bao et al 2004, Fragment, Gesichtet, Rlm, SMWFragment, Schutzlevel sysop, Verschleierung

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Untersuchte Arbeit:
Seite: 49, Zeilen: 1-11
Quelle: Bao et al 2004
Seite(n): 1727, Zeilen: r. col: 11 ff.
[It is well known that one major regulatory] mechanism in cell proliferation and transformation is phosphorylation of proteins on serine or threonine residues preceding proline (pSer/Thr- Pro) by various prodirected protein kinases, such as MAP kinases, cyclin-dependent kinases, JNK, and GSK3β. Interestingly, the pSer/Thr-Pro motifs in proteins exist in two completely distinct cis and trans conformations, whose conversion is normally restrained by phosphorylation, but catalyzed specifically by the essential prolyl isomerase Pin1. By isomerizing pSer81, Pin1 induce conformational changes in androgen receptor. This, phosphorylation- dependent prolyl isomerization is a critical mechanism in phosphorylation signaling. One major regulatory mechanism in cell proliferation and transformation is phosphorylation of proteins on serine or threonine residues preceding proline (pSer/Thr- Pro) by various prodirected protein kinases, such as MAP kinases, cyclin-dependent kinases, JNK, and GSK3β.1–3 Interestingly, the pSer/Thr-Pro motifs in proteins exist in two completely distinct cis and trans conformations, whose conversion is normally restrained by phosphorylation, but catalyzed specifically by the essential prolyl isomerase Pin1.3–6 By isomerizing specific pSer/Thr-Pro bonds, Pin1 has been shown to catalytically induce conformational changes in proteins after phosphorylation, thereby having profound effects on their catalytic activity, dephosphorylation, protein-protein interactions, subcellular location, and/or turnover.4,5,7–18 Thus, phosphorylation- dependent prolyl isomerization is a critical postphosphorylation regulatory mechanism in phosphorylation signaling.3

[...]

Anmerkungen

The source is not mentioned.

Sichter
(Hindemith), SleepyHollow02

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