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David H. Hawke

Researcher at University of Texas MD Anderson Cancer Center

Publications -  163
Citations -  11680

David H. Hawke is an academic researcher from University of Texas MD Anderson Cancer Center. The author has contributed to research in topics: Phosphorylation & Peptide sequence. The author has an hindex of 50, co-authored 157 publications receiving 9824 citations. Previous affiliations of David H. Hawke include University of California, Los Angeles & University of Texas Health Science Center at Houston.

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Phosphorylation of β-Catenin by AKT Promotes β-Catenin Transcriptional Activity *

TL;DR: In this paper, the authors demonstrated that AKT-activated downstream from epidermal growth factor receptor signaling, phosphorylates β-catenin at Ser552 in vitro and in vivo.
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A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response

TL;DR: It is suggested that the acetylation of histone H3 K56 creates a favourable chromatin environment for DNA repair and that a key component of the DNA damage response is to preserve this acetylations.
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PKM2 phosphorylates histone H3 and promotes gene transcription and tumorigenesis.

TL;DR: It is shown that PKM2 directly binds to histone H3 and phosphorylates hist one H3 at T11 upon EGF receptor activation and this phosphorylation is required for the dissociation of HDAC3 from the CCND1 and MYC promoter regions and subsequent acetylation of histoneH3 at K9.
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Tumor suppressor ARF degrades B23, a nucleolar protein involved in ribosome biogenesis and cell proliferation.

TL;DR: It is shown that ARF interacts with B23, a multifunctional nucleolar protein involved in ribosome biogenesis, and promotes its polyubiquitination and degradation, and suggests a nucleolar role of ARF in surveillance of oncogenic insults.
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The LINK-A lncRNA activates normoxic HIF1α signalling in triple-negative breast cancer

TL;DR: A cytoplasmic lncRNA is identified, LINK-A, which mediates HB-EGF-triggered, EGFR:GPNMB heterodimer-dependent HIF1α phosphorylation at Tyr 565 and Ser 797 by BRK and LRRK2, respectively, and correlates with triple-negative breast cancer (TNBC), promoting breast cancer glycolysis reprogramming and tumorigenesis.