scispace - formally typeset
W

Walter W. Chen

Researcher at Massachusetts Institute of Technology

Publications -  39
Citations -  9579

Walter W. Chen is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: Serine & Mitochondrion. The author has an hindex of 23, co-authored 39 publications receiving 7415 citations. Previous affiliations of Walter W. Chen include Harvard University & Howard Hughes Medical Institute.

Papers
More filters
Journal ArticleDOI

An essential role of the mitochondrial electron transport chain in cell proliferation is to enable aspartate synthesis

TL;DR: A CRISPR-based genetic screen was used to identify genes whose loss sensitizes human cells to phenformin, a complex I inhibitor, and yielded GOT1, the cytosolic aspartate aminotransferase, loss of which kills cells upon ETC inhibition.
Journal ArticleDOI

A Tumor Suppressor Complex with GAP Activity for the Rag GTPases That Signal Amino Acid Sufficiency to mTORC1

TL;DR: In this article, the authors identify GATOR as a complex that interacts with the Rags and is composed of two sub-complexes called GATOR1 and -2, and reveal that, like other mTORC1 regulators, Rag function can be deregulated in cancer.

An Essential Role of the Mitochondrial Electron Transport Chain in Cell Proliferation Is to Enable Aspartate Synthesis

TL;DR: In this article, the authors used a CRISPR-based genetic screen to identify genes whose loss sensitizes human cells to phenformin, a complex I inhibitor, and yielded GOT1, the cytosolic aspartate aminotransferase, loss of which kills cells upon ETC inhibition.
Journal ArticleDOI

Metabolic determinants of cancer cell sensitivity to glucose limitation and biguanides

TL;DR: In this article, a continuous-flow culture apparatus is used to maintain proliferating cancer cells in low-glucose conditions, demonstrating that mitochondrial oxidative phosphorylation (OXPHOS) is essential for optimal proliferation in these conditions; the most sensitive cell lines are defective in OXPHOS upregulation and may therefore be sensitive to current antidiabetic drugs that inhibit OPHOS.