Catalytic Mechanism Investigation of Lysine-Specific Demethylase 1 (LSD1): A Computational Study
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Title
Catalytic Mechanism Investigation of Lysine-Specific Demethylase 1 (LSD1): A Computational Study
Authors
Keywords
Hydrides, Histones, Biochemical simulations, Flavin, Lysine, Potential energy, Simulation and modeling, Electrostatics
Journal
PLoS One
Volume 6, Issue 9, Pages e25444
Publisher
Public Library of Science (PLoS)
Online
2011-10-01
DOI
10.1371/journal.pone.0025444
References
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Related references
Note: Only part of the references are listed.- Molecular Mimicry and Ligand Recognition in Binding and Catalysis by the Histone Demethylase LSD1-CoREST Complex
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- (2009) Michelle Henderson Pozzi et al. BIOCHEMISTRY
- Use of pH and Kinetic Isotope Effects To Establish Chemistry as Rate-Limiting in Oxidation of a Peptide Substrate by LSD1
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- Mechanistic Studies ofpara-SubstitutedN,N′-Dibenzyl-1,4-diaminobutanes as Substrates for a Mammalian Polyamine Oxidase
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- LSD1-mediated epigenetic modification is required for TAL1 function and hematopoiesis
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- The pH dependence of kinetic isotope effects in monoamine oxidase A indicates stabilization of the neutral amine in the enzyme-substrate complex
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- p53-Targeted LSD1 Functions in Repression of Chromatin Structure and Transcription In Vivo
- (2008) W.-W. Tsai et al. MOLECULAR AND CELLULAR BIOLOGY
- The lysine demethylase LSD1 (KDM1) is required for maintenance of global DNA methylation
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