scispace - formally typeset
T

Takashi Tsukamoto

Researcher at Johns Hopkins University

Publications -  91
Citations -  4465

Takashi Tsukamoto is an academic researcher from Johns Hopkins University. The author has contributed to research in topics: Glutamate carboxypeptidase II & Glutaminase. The author has an hindex of 29, co-authored 78 publications receiving 3802 citations. Previous affiliations of Takashi Tsukamoto include Johns Hopkins University School of Medicine & Chiba University.

Papers
More filters
Journal ArticleDOI

The Metabolic Profile of Tumors Depends on Both the Responsible Genetic Lesion and Tissue Type

TL;DR: The results suggest that the metabolic profiles of tumors are likely to depend on both the genotype and tissue of origin and have implications regarding the design of therapies targeting tumor metabolism.
Journal ArticleDOI

Inhibition of glutaminase preferentially slows growth of glioma cells with mutant IDH1.

TL;DR: The ability to selectively slow growth in cells with IDH1 mutations by inhibiting glutaminase suggests a unique reprogramming of intermediary metabolism and a potential therapeutic strategy.
Journal ArticleDOI

Novel mechanism of inhibition of rat kidney-type glutaminase by bis-2-(5-phenylacetamido-1,2,4-thiadiazol-2-yl)ethyl sulfide (BPTES)

TL;DR: BPTES is a unique and potent inhibitor of rat KGA and elucidates a novel mechanism of inactivation, which established that BPTES prevents the formation of large phosphate-induced oligomers and instead promotes theformation of a single oligomeric species with distinct physical properties.
Journal ArticleDOI

Metabolic shifts toward glutamine regulate tumor growth, invasion and bioenergetics in ovarian cancer

TL;DR: It is found that low‐invasive ovarian cancer (OVCA) cells are glutamine independent, whereas high-invasive OVCA cells are markedly glutamine dependent, and the ratio of gene expression associated with glutamine anabolism versus catabolism has emerged as a novel biomarker for patient prognosis.
Journal ArticleDOI

Structure of glutamate carboxypeptidase II, a drug target in neuronal damage and prostate cancer.

TL;DR: Three‐dimensional structures presented here reveal an induced‐fit substrate‐binding mode of this key enzyme and provide essential information for the design of GCPII inhibitors useful in the treatment of neuronal diseases and prostate cancer.