G
Gerburg M. Wulf
Researcher at Beth Israel Deaconess Medical Center
Publications - 125
Citations - 10318
Gerburg M. Wulf is an academic researcher from Beth Israel Deaconess Medical Center. The author has contributed to research in topics: Cancer & Breast cancer. The author has an hindex of 46, co-authored 106 publications receiving 8720 citations. Previous affiliations of Gerburg M. Wulf include Harvard University & Heidelberg University.
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Journal ArticleDOI
The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein.
TL;DR: Pin1 can restore the ability of phosphorylated tau to bind microtubules and promote microtubule assembly in vitro, and provide a new insight into the pathogenesis of Alzheimer's disease.
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Regulation of NF-κB Signaling by Pin1-Dependent Prolyl Isomerization and Ubiquitin-Mediated Proteolysis of p65/RelA
Akihide Ryo,Futoshi Suizu,Yasuhiro Yoshida,Kilian Perrem,Yih-Cherng Liou,Gerburg M. Wulf,Robert Rottapel,Shoji Yamaoka,Kun Ping Lu +8 more
TL;DR: It is demonstrated that NF-kappaB function is regulated by Pin1-mediated prolyl isomerization and ubiquitin-mediated proteolysis of its p65/RelA subunit, enabling new insight into the pathogenesis and treatment of some human diseases such as cancers.
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Pin1 is overexpressed in breast cancer and cooperates with Ras signaling in increasing the transcriptional activity of c-Jun towards cyclin D1
TL;DR: It is reported that Pin1 is strikingly overexpressed in human breast cancers, and that its levels correlate with cyclin D1 levels in tumors, and the results suggest that overexpression of Pin1 may promote tumor growth.
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Pin1 regulates turnover and subcellular localization of β-catenin by inhibiting its interaction with APC
TL;DR: It is shown that Pin1 regulates β-catenin turnover and subcellular localization by interfering with its interaction with adenomatous polyposis coli protein (APC) and its overexpression might contribute to the upregulation of β- catenin in tumours such as breast cancer.
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The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloid-β production
Lucia Pastorino,Anyang Sun,Anyang Sun,Pei Jung Lu,Xiao Zhen Zhou,Martin Balastik,Greg Finn,Gerburg M. Wulf,Jormay Lim,Shihua Li,Xiao-Jiang Li,Weiming Xia,Linda K. Nicholson,Kun Ping Lu +13 more
TL;DR: It is found that Pin1 binds to the phosphorylated Thr 668-Pro motif in APP and accelerates its isomerization by over 1,000-fold, regulating the APP intracellular domain between two conformations, as visualized by NMR.