Peter Breslin
Loyola University Chicago
33 Papers
110 Citations
Peter Breslin is an academic researcher from Loyola University Chicago. The author has contributed to research in topics: Haematopoiesis & Stem cell. The author has an hindex of 14, co-authored 27 publications. Previous affiliations of Peter Breslin include Loyola University Medical Center.
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Papers
c-Myc-mediated control of cell fate in megakaryocyte-erythrocyte progenitors.
Yinshi Guo,Chao Niu,Peter Breslin,Peter Breslin,Minghui Tang,Shubin Zhang,Wei Wei,Ameet R. Kini,Gladell P. Paner,Serhan Alkan,Stephan W. Morris,Manuel O. Diaz,Patrick J. Stiff,Jiwang Zhang +13 more
TL;DR: In this article, it has been found that c-Myc protein plays a critical role in controlling self-renewal versus differentiation in hematopoietic stem cells.
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c-Myc is a target of RNA-binding motif protein 15 in the regulation of adult hematopoietic stem cell and megakaryocyte development.
TL;DR: It is reported that Rbm15 may function in part through regulation of expression of the proto-oncogene c-Myc, which appears to be required for normal HSC-niche interactions, for the ability of HSCs to contribute normally to adult hematopoiesis, and for normal megakaryocyte development.
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FAK Mediates a Compensatory Survival Signal Parallel to PI3K-AKT in PTEN-Null T-ALL Cells
Dewen You,Junping Xin,Andrew Volk,Wei Wei,Rachel Schmidt,Gina Scurti,Sucha Nand,Sucha Nand,Eun-Kyoung Breuer,Paul C. Kuo,Peter Breslin,Ameet R. Kini,Michael I. Nishimura,Nancy J. Zeleznik-Le,Jiwang Zhang +14 more
TL;DR: Fak, a protein substrate of Pten, also contributes to T-ALL development in Pten-null mice and significantly sensitizes both murine and human PTEN-null T-all cells to PI3K/AKT/mTOR inhibition.
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Molecular and cellular mechanisms of aging in hematopoietic stem cells and their niches.
TL;DR: The most recent advances in research into HSC aging are reviewed and the role of HSC-intrinsic events, as well as those that relate to the aging bone marrow niche microenvironment in the overall processes of H SC aging are discussed.
Caspase-3 suppresses diethylnitrosamine-induced hepatocyte death, compensatory proliferation and hepatocarcinogenesis through inhibiting p38 activation
TL;DR: Overall, the data suggest that Caspase-3 inhibits chemical-induced hepatocarcinogenesis by suppressing p38 activation and hepatocyte death and inhibition of p38 by SB202190 abrogated enhanced hepatocytes death, compensatory proliferation and HCC induced by DEN in Casp enzyme-3-deficient mice.