Evidence supporting a critical contribution of intrinsically disordered regions to the biochemical behavior of full-length human HP1γ
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Title
Evidence supporting a critical contribution of intrinsically disordered regions to the biochemical behavior of full-length human HP1γ
Authors
Keywords
HP1, HP1γ, CBX3, Molecular modeling, Molecular dynamics, Epigenetics, Chromatin
Journal
JOURNAL OF MOLECULAR MODELING
Volume 22, Issue 1, Pages -
Publisher
Springer Nature
Online
2015-12-17
DOI
10.1007/s00894-015-2874-z
References
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- Prediction of disordered regions in proteins based on the meta approach
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- (2008) Shunichi Kosugi et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Linking Heterochromatin Protein 1 (HP1) to cancer progression
- (2008) George K. Dialynas et al. MUTATION RESEARCH-FUNDAMENTAL AND MOLECULAR MECHANISMS OF MUTAGENESIS
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