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William C. Hahn

Researcher at Harvard University

Publications -  515
Citations -  85047

William C. Hahn is an academic researcher from Harvard University. The author has contributed to research in topics: Cancer & Medicine. The author has an hindex of 130, co-authored 448 publications receiving 72191 citations. Previous affiliations of William C. Hahn include Brigham and Women's Hospital & University of Washington.

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Capturing the swelling of solid-electrolyte interphase in lithium metal batteries

TL;DR: A thin film vitrification method is adopted to preserve the sensitive yet critical interfaces in batteries at native liquid electrolyte environments to enable cryo–electron microscopy and spectroscopy and to report substantial swelling of the SEI on lithium metal anode in various electrolytes.
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Wilms tumor 1 (WT1) regulates KRAS-driven oncogenesis and senescence in mouse and human models

TL;DR: An unexpected role for WT1 is identified as a key regulator of the genetic network of oncogenic KRAS and important insight is provided into the mechanisms that regulate proliferation or senescence in response to oncogens signals.
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Control of Cyclin D1 and Breast Tumorigenesis by the EglN2 Prolyl Hydroxylase

TL;DR: It is found that EglN2 inactivation decreases Cyclin D1 levels and suppresses mammary gland proliferation in vivo and support the exploration of Egln2 inhibitors as therapeutics for estrogen-dependent breast cancer and other malignancies.
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Nucleolin interacts with telomerase.

TL;DR: It is shown that nucleolin, a major nucleolar phosphoprotein, interacts with telomerase and alters its subcellular localization and indicates that interaction of hTERT and nucleolin participates in the dynamic intracellular localization of telomersase complex.
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RSK3/4 mediate resistance to PI3K pathway inhibitors in breast cancer

TL;DR: It is demonstrated that overexpression of RSK3 or RSK4 supports proliferation upon PI3K inhibition both in vitro and in vivo, in part through the attenuation of the apoptotic response and upregulation of protein translation.