In this issue of Cell, English et al. present the first crystal structure of a histone chaperone (Asf1) bound to histones (the H3/H4 heterodimer). The structure provides insights into how histone chaperones participate in nucleosome disassembly. It reveals that Asf1 physically blocks (H3/H4)(2) tetramer formation and that the C terminus of H4 undergoes a dramatic conformational change upon binding to Asf1.
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Higher isoform of hnRNPA1 confer Temozolomide resistance in U87MG & LN229 glioma cells.
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Molecular Cancer Genetics and Signal Transduction Laboratory, Dr. B.R Ambedkar Center for Biomedical Research, University of Delhi, North Campus, Gate No. 1, Vishwavidyalaya Marg, Mall Road, 44, AH2, Delhi, 110007, India.
Background: Gliblastoma is a malignant brain tumor; despite available treatment modalities, the tumor reoccurrence rate persist in the currently prescribed Temozolomide chemotherapy. Study aimed to study the inquisitive role of RNA binding splice factor protein hnRNPA1 in promoting glioma resistance against Temozolomide drug and therapeutic insights.
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Department of Biochemistry and Molecular Biology, The Pennsylvania State University College of Medicine, Hershey, PA 17033, USA.
Article Synopsis
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Mendel Centre for Plant Genomics and Proteomics, CEITEC, Masaryk University, Brno, CZ-62500, Czech Republic.
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College of Veterinary Medicine, Vietnam National University of Agriculture (VNUA), Hanoi, Vietnam.
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