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Bio
Research in my group focuses on the molecular mechanisms of epigenetic regulation and phosphoinositide signaling. We apply high field NMR spectroscopy, X-ray crystallography and a wide array of biochemical and molecular biology approaches to characterize the atomic-resolution structures and functions of chromatin- and lipid-binding proteins implicated in cancer and other human diseases.
The study of epigenetics and deciphering the ‘epigenetic code/language’ is the major direction in the lab. The genetic material of eukaryotic cells is packaged into the nucleus in the form of chromatin. Chromatin is made up of building blocks called nucleosomes. Each nucleosomal particle contains an octamer of four histone proteins, H2A, H2B, H3 and H4, around which genomic DNA is wound almost twice. The nucleosomes undergo recurrent structural rearrangements and are subject to posttranslational modifications (PTMs). A particularly large number of PTMs, or epigenetic marks, have been identified on the histone tails that protrude from the nucleosomal core and are freely accessible to histone acetyltransferases (HATs), histone deacetylases (HDACs), histone lysine methyltransferases (HKMTs), kinases, phosphatases and other enzymes capable of depositing or removing PTMs. The list of PTMs is expanding rapidly and includes, among others, acetylation and methylation of lysine residues, methylation of arginine residues, and phosphorylation of serine and threonine residues.
The study of epigenetics and deciphering the ‘epigenetic code/language’ is the major direction in the lab. The genetic material of eukaryotic cells is packaged into the nucleus in the form of chromatin. Chromatin is made up of building blocks called nucleosomes. Each nucleosomal particle contains an octamer of four histone proteins, H2A, H2B, H3 and H4, around which genomic DNA is wound almost twice. The nucleosomes undergo recurrent structural rearrangements and are subject to posttranslational modifications (PTMs). A particularly large number of PTMs, or epigenetic marks, have been identified on the histone tails that protrude from the nucleosomal core and are freely accessible to histone acetyltransferases (HATs), histone deacetylases (HDACs), histone lysine methyltransferases (HKMTs), kinases, phosphatases and other enzymes capable of depositing or removing PTMs. The list of PTMs is expanding rapidly and includes, among others, acetylation and methylation of lysine residues, methylation of arginine residues, and phosphorylation of serine and threonine residues.
Research Interests
Papers共 194 篇Author StatisticsCo-AuthorSimilar Experts
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Biochimica et biophysica acta. Gene regulatory mechanismsno. 3 (2024): 195045-195045
Minh Chau Nguyen, Hosein Rostamian,Ana Raman,Pengcheng Wei,Dustin C Becht,Annette H Erbse,Brianna J Klein,Tonya M Gilbert, Gongyi Zhang,M Andres Blanco,Brian D Strahl,Sean D Taverna,
Nature communicationsno. 1 (2024): 5335-5335
Antiviral Research (2024): 105904-105904
Yi Zhang,Guojia Xie,Ji-Eun Lee,Mohamad Zandian,Deepthi Sudarshan,Benjamin Estavoyer,Caroline Benz, Tiina Viita, Golareh Asgaritarghi,Catherine Lachance,Clémence Messmer,Leandro Simonetti,
Nature communicationsno. 1 (2024): 4883-4883
Dustin C. Becht,Akinori Kanai, Soumi Biswas, Mohamed Halawa,Lei Zeng,Khan L. Cox,Michael G. Poirier,Ming-Ming Zhou,Xiaobing Shi,Akihiko Yokoyama,Tatiana G. Kutateladze
ISCIENCEno. 4 (2024): 109367-109367
Dustin C. Becht, Sk Abdul Mohid,Ji-Eun Lee,Mohamad Zandian,Caroline Benz, Soumi Biswas,Vikrant Kumar Sinha,Ylva Ivarsson,Kai Ge,Yi Zhang,Tatiana G. Kutateladze
Structureno. 6 (2024): 706-714.e3
Journal of molecular biologyno. 7 (2024): 168501-168501
Current Opinion in Chemical Biology (2023): 102252
Trends in biochemical sciencesno. 7 (2023): 610-617
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Author Statistics
#Papers: 185
#Citation: 7947
H-Index: 43
G-Index: 87
Sociability: 7
Diversity: 0
Activity: 2
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