Results 31 to 40 of about 44,168 (193)

Bench-to-Bedside Studies of Arginine Deprivation in Cancer

open access: yesMolecules, 2023
Arginine is a semi-essential amino acid which becomes wholly essential in many cancers commonly due to the functional loss of Argininosuccinate Synthetase 1 (ASS1).
George C. Field   +2 more
doaj   +1 more source

Supplementary Tables S1 & S2 from Reduced Argininosuccinate Synthetase Is a Predictive Biomarker for the Development of Pulmonary Metastasis in Patients with Osteosarcoma

open access: yes, 2010
Supplementary Tables S1 & S2 from Reduced Argininosuccinate Synthetase Is a Predictive Biomarker for the Development of Pulmonary Metastasis in Patients with ...
Reiko Satow (14926212)   +14 more
core   +2 more sources

Therapeutic arginine starvation in ASS1-deficient cancers inhibits the Warburg effect

open access: yesMolecular & Cellular Oncology, 2017
Argininosuccinate Synthetase 1 deficiency induces dependence on extracellular arginine for continued cellular growth and survival. Arginine starvation inhibits the Warburg effect and diverts glucose into serine biosynthesis, while simultaneously ...
Jeff C. Kremer, Brian A. Van Tine
doaj   +1 more source

Intracellular arginine-dependent translation sensor reveals the dynamics of arginine starvation response and resistance in ASS1-negative cells

open access: yesCancer & Metabolism, 2021
Background Many cancers silence the metabolic enzyme argininosuccinate synthetase 1 (ASS1), the rate-limiting enzyme for arginine biosynthesis within the urea cycle. Consequently, ASS1-negative cells are susceptible to depletion of extracellular arginine
Leonard C. Rogers   +5 more
doaj   +1 more source

Enzymes Involved in the Biosynthesis of Arginine from Ornithine in Maritime Pine (Pinus pinaster Ait.)

open access: yesPlants, 2020
The amino acids arginine and ornithine are the precursors of a wide range of nitrogenous compounds in all living organisms. The metabolic conversion of ornithine into arginine is catalyzed by the sequential activities of the enzymes ornithine ...
José Alberto Urbano-Gámez   +4 more
doaj   +1 more source

Generation of an ASS1 heterozygous knockout human embryonic stem cell line, WAe001-A-13, using CRISPR/Cas9

open access: yesStem Cell Research, 2018
The ASS1 gene encodes argininosuccinate synthetase-1, a cytosolic enzyme with a critical role in the urea cycle. Mutations are found in all ASS1 exons and cause the autosomal recessive disorder citrullinemia. Using CRISPR/Cas9-editing, we established the
Fang Yuan   +10 more
doaj   +1 more source

A transgenic approach to study argininosuccinate synthetase gene expression. [PDF]

open access: yesJ Biomed Sci, 2014
Argininosuccinate synthetase (ASS) participates in urea, nitric oxide and arginine production. Besides transcriptional regulation, a post-transcriptional regulation affecting nuclear precursor RNA stability has been reported. To study whether such post-transcriptional regulation underlines particular temporal and spatial ASS expression, and to ...
Shiue SC, Huang MZ, Su TS.
europepmc   +4 more sources

Substrate Induced Conformational Changes in Argininosuccinate Synthetase [PDF]

open access: yesJournal of Biological Chemistry, 2002
Argininosuccinate synthetase (AS) is the rate-limiting enzyme of both the urea and arginine-citrulline cycles. In mammals, deficiency of AS leads to citrullinemia, a debilitating and often fatal autosomal recessive urea cycle disorder, whereas its overexpression for sustained nitric oxide production via the arginine-citrulline cycle leads to the ...
Christopher T, Lemke, P Lynne, Howell
openaire   +2 more sources

RNA interference of argininosuccinate synthetase restores sensitivity to recombinant arginine deiminase (rADI) in resistant cancer cells

open access: yesJournal of Biomedical Science, 2011
Background Sensitivity of cancer cells to recombinant arginine deiminase (rADI) depends on expression of argininosuccinate synthetase (AS), a rate-limiting enzyme in synthesis of arginine from citrulline.
Yo Hao-Hsin   +5 more
doaj   +1 more source

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