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Amit K. Das

Researcher at University of Texas Southwestern Medical Center

Publications -  16
Citations -  860

Amit K. Das is an academic researcher from University of Texas Southwestern Medical Center. The author has contributed to research in topics: Epidermal growth factor receptor & Population. The author has an hindex of 11, co-authored 16 publications receiving 778 citations. Previous affiliations of Amit K. Das include State University of New York System.

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Non–Small Cell Lung Cancers with Kinase Domain Mutations in the Epidermal Growth Factor Receptor Are Sensitive to Ionizing Radiation

TL;DR: The majority of mutant EGFR NSCLCs, including those that contain the secondary gefitinib resistance T790M mutation, exhibit characteristics consistent with a radiosensitive phenotype, which include delayed DNA repair kinetics, defective IR-induced arrest in DNA synthesis or mitosis, and pronounced increases in apoptosis or micronuclei.
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Molecular genetics of palmitoyl-protein thioesterase deficiency in the U.S.

TL;DR: In 29 of the families, PPT deficiency was found to be responsible for the neurodegenerative disorder, and mutations were identified in 57 out of 58 PPT alleles, resulting in a broader spectrum of clinical presentations than previously seen in the Finnish population.
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Somatic mutations in the tyrosine kinase domain of Epidermal Growth Factor Receptor (EGFR) abrogate EGFR-mediated radioprotection in non-small cell lung carcinoma

TL;DR: This study has identified a subset of naturally occurring EGFR mutations that lack a critical radioprotective function of EGFR, providing valuable insights on how the EGFR mediates cell survival in response to radiation in NSCLC cell lines.
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Jumonji Inhibitors Overcome Radioresistance in Cancer through Changes in H3K4 Methylation at Double-Strand Breaks

TL;DR: In human patients, lung squamous cell carcinomas highly ex-pressing KDM5B respond poorly to radiation, so the use of Jumonji KDM inhibitors as potent radiosensitizers is proposed.
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Structural basis for the insensitivity of a serine enzyme (palmitoyl-protein thioesterase) to phenylmethylsulfonyl fluoride.

TL;DR: It is shown that the active site serine in PPT1 is modified by a substrate analog of PMSF, hexadecylsulfonylfluoride (HDSF) in a specific and site-directed manner, suggesting a structural explanation as to why certain serine lipases are resistant to modification by commonly used serine-modifying reagents.