Related references
Note: Only part of the references are listed.The fork protection complex recruits FACT to reorganize nucleosomes during replication
Barbara Safaric et al.
NUCLEIC ACIDS RESEARCH (2022)
Electron microscopy analysis of ATP-independent nucleosome unfolding by FACT
Anastasiia L. Sivkina et al.
COMMUNICATIONS BIOLOGY (2022)
Structure of a backtracked hexasomal intermediate of nucleosome transcription
Lucas Farnung et al.
MOLECULAR CELL (2022)
Structural basis of nucleosome disassembly and reassembly by RNAPII elongation complex with FACT
Haruhiko Ehara et al.
SCIENCE (2022)
The lane-switch mechanism for nucleosome repositioning by DNA translocase
Fritz Nagae et al.
NUCLEIC ACIDS RESEARCH (2021)
The kinetic landscape of nucleosome assembly: A coarse-grained molecular dynamics study
Giovanni B. Brandani et al.
PLOS COMPUTATIONAL BIOLOGY (2021)
Rad54 Drives ATP Hydrolysis-Dependent DNA Sequence Alignment during Homologous Recombination
J. Brooks Crickard et al.
CELL (2020)
The role of FACT in managing chromatin: disruption, assembly, or repair?
Tim Formosa et al.
NUCLEIC ACIDS RESEARCH (2020)
Characterization of Caenorhabditis elegans Nucleosome Assembly Protein 1 Uncovers the Role of Acidic Tails in Histone Binding
Prithwijit Sarkar et al.
BIOCHEMISTRY (2019)
Structural Insights into ceNAP1 Chaperoning Activity toward ceH2A-H2B
Yongrui Liu et al.
STRUCTURE (2019)
Fuzziness in Protein Interactions-A Historical Perspective
Monika Fuxreiter
JOURNAL OF MOLECULAR BIOLOGY (2018)
Functions of FACT in Breaking the Nucleosome and Maintaining Its Integrity at the Single-Nucleosome Level
Ping Chen et al.
MOLECULAR CELL (2018)
High precision FRET studies reveal reversible transitions in nucleosomes between microseconds and minutes
Alexander Gansen et al.
NATURE COMMUNICATIONS (2018)
Understanding nucleosome dynamics and their links to gene expression and DNA replication
William K. M. Lai et al.
NATURE REVIEWS MOLECULAR CELL BIOLOGY (2017)
Histone chaperone networks shaping chromatin function
Colin M. Hammond et al.
NATURE REVIEWS MOLECULAR CELL BIOLOGY (2017)
Sequence-dependent nucleosome sliding in rotation-coupled and uncoupled modes revealed by molecular simulations
Toru Niina et al.
PLOS COMPUTATIONAL BIOLOGY (2017)
Structural evidence for Nap1-dependent H2A-H2B deposition and nucleosome assembly
Carmen Aguilar-Gurrieri et al.
EMBO JOURNAL (2016)
C-terminal acidic domain of histone chaperone human NAP1 is an efficient binding assistant for histone H2A-H2B, but not H3-H4
Hideaki Ohtomo et al.
GENES TO CELLS (2016)
Modeling Structural Dynamics of Biomolecular Complexes by Coarse-Grained Molecular Simulations
Shoji Takada et al.
ACCOUNTS OF CHEMICAL RESEARCH (2015)
Histone exchange, chromatin structure and the regulation of transcription
Swaminathan Venkatesh et al.
NATURE REVIEWS MOLECULAR CELL BIOLOGY (2015)
Coarse-grained modeling of DNA curvature
Gordon S. Freeman et al.
JOURNAL OF CHEMICAL PHYSICS (2014)
RESPAC: Method to Determine Partial Charges in Coarse-Grained Protein Model and Its Application to DNA-Binding Proteins
Tsuyoshi Terakawa et al.
JOURNAL OF CHEMICAL THEORY AND COMPUTATION (2014)
Energy landscape views for interplays among folding, binding, and allostery of calmodulin domains
Wenfei Li et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2014)
Chaperone Nap1 Shields Histone Surfaces Used in a Nucleosome and Can Put H2A-H2B in an Unconventional Tetrameric Form
Sheena D'Arcy et al.
MOLECULAR CELL (2013)
Structural Analysis of the Hexasome, Lacking One Histone H2A/H2B Dimer from the Conventional Nucleosome
Yasuhiro Arimura et al.
BIOCHEMISTRY (2012)
Multiscale Ensemble Modeling of Intrinsically Disordered Proteins: p53 N-Terminal Domain
Tsuyoshi Terakawa et al.
BIOPHYSICAL JOURNAL (2011)
CafeMol: A Coarse-Grained Biomolecular Simulator for Simulating Proteins at Work
Hiroo Kenzaki et al.
JOURNAL OF CHEMICAL THEORY AND COMPUTATION (2011)
Crystal Structures of Nucleosome Core Particles Containing the '601' Strong Positioning Sequence
Dileep Vasudevan et al.
JOURNAL OF MOLECULAR BIOLOGY (2010)
The Histone Chaperone Nap1 Promotes Nucleosome Assembly by Eliminating Nonnucleosomal Histone DNA Interactions
Andrew J. Andrews et al.
MOLECULAR CELL (2010)
Fluorescence Quenching by Photoinduced Electron Transfer: A Reporter for Conformational Dynamics of Macromolecules
Soren Doose et al.
CHEMPHYSCHEM (2009)
Standard Free Energy of Binding from a One-Dimensional Potential of Mean Force
Slimane Doudou et al.
JOURNAL OF CHEMICAL THEORY AND COMPUTATION (2009)
A Thermodynamic Model for Nap1-Histone Interactions
Andrew J. Andrews et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2008)
A β-hairpin comprising the nuclear localization sequence sustains the self-associated states of nucleosome assembly protein 1
Young-Jun Park et al.
JOURNAL OF MOLECULAR BIOLOGY (2008)
On the mechanism of nucleosome assembly by histone chaperone NAP1
Jacek Mazurkiewicz et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2006)
Chromatin remodeling by nucleosome disassembly in vitro
Y Lorch et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2006)
The structure of nucleosome assembly protein 1
YJ Park et al.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2006)
Association states of nucleosome assembly protein 1 and its complexes with histones
KF Tóth et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2005)
Histone release during transcription: displacement of the two H2A-H2B dimers in the nucleosome is dependent on different levels of transcription-induced positive stress
V Levchenko et al.
BIOCHEMISTRY (2005)
Nucleosome assembly protein 1 exchanges histone H2A-H2B dimers and assists nucleosome sliding
YJ Park et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2005)
Preferential binding of the histone (H3-H4)2 tetramer by NAP1 is mediated by the amino-terminal histone tails
SJ McBryant et al.
JOURNAL OF BIOLOGICAL CHEMISTRY (2003)
Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 Å resolution
CA Davey et al.
JOURNAL OF MOLECULAR BIOLOGY (2002)
Share Paper
