O
Olli A. Jänne
Researcher at University of Helsinki
Publications - 269
Citations - 17398
Olli A. Jänne is an academic researcher from University of Helsinki. The author has contributed to research in topics: Androgen receptor & Receptor. The author has an hindex of 71, co-authored 268 publications receiving 16804 citations. Previous affiliations of Olli A. Jänne include University of Oulu & Population Council.
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Journal ArticleDOI
Androgen receptor regulates a distinct transcription program in androgen-independent prostate cancer
Qianben Wang,Wei Li,Yong Zhang,Xin Yuan,Kexin Xu,Jindan Yu,Zhong Chen,Rameen Beroukhim,Rameen Beroukhim,Hongyun Wang,Mathieu Lupien,Tao Wu,Meredith M. Regan,Clifford A. Meyer,Jason S. Carroll,Arjun K. Manrai,Olli A. Jänne,Steven P. Balk,Rohit Mehra,Bo Han,Arul M. Chinnaiyan,Mark A. Rubin,Lawrence D. True,Michelangelo Fiorentino,Christopher Fiore,Massimo Loda,Philip W. Kantoff,X. Shirley Liu,Myles Brown +28 more
TL;DR: The role of AR in androgen-independent cancer cells is not to direct the androgen -dependent gene expression program without androgen, but rather to execute a distinct program resulting in androgens-independent growth.
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A Hierarchical Network of Transcription Factors Governs Androgen Receptor-Dependent Prostate Cancer Growth
Qianben Wang,Wei Li,X. Shirley Liu,Jason S. Carroll,Olli A. Jänne,Erika Krasnickas Keeton,Arul M. Chinnaiyan,Kenneth J. Pienta,Myles Brown +8 more
TL;DR: The majority of AR binding regions contain noncanonical AR-responsive elements (AREs) and are identified as a cis-regulatory target of AR action in TMPRSS2, a gene fused to ETS transcription factors in the majority of prostate cancers.
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Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1)
TL;DR: It is shown that AR is covalently modified by SUMO-1 (sumoylated) in an androgen-enhanced fashion and the principal acceptor site in the N-terminal domain of AR is identified, suggesting that reversible sumoylation is a mechanism for regulation of steroid receptor function.
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PIAS Proteins Modulate Transcription Factors by Functioning as SUMO-1 Ligases
TL;DR: The results imply that PIAS proteins function as SUMO-1-tethering proteins and zinc finger-dependent E3 SUMO protein ligases, and these properties are likely to explain their ability to modulate the activities of various transcription factors.
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Interaction between the Amino- and Carboxyl-terminal Regions of the Rat Androgen Receptor Modulates Transcriptional Activity and Is Influenced by Nuclear Receptor Coactivators *
TL;DR: Interplay between the N-terminal region and LBD of rAR results in the formation of a transactivation complex that includes coregulators and that is mandatory for optimal activation of androgen-induced promoters.