Results 11 to 20 of about 1,411,447 (295)

Histone variants at a glance. [PDF]

open access: yesJ Cell Sci, 2021
Eukaryotic nucleosomes organize chromatin by wrapping 147 bp of DNA around a histone core particle comprising two molecules each of histone H2A, H2B, H3 and H4. The DNA entering and exiting the particle may be bound by the linker histone H1.
Talbert PB, Henikoff S.
europepmc   +4 more sources

The Role of MacroH2A Histone Variants in Cancer. [PDF]

open access: yesCancers (Basel), 2021
Simple Summary The structural unit of chromatin is the nucleosome that is composed of DNA wrapped around a core of eight histone proteins. Histone variants can replace ‘standard’ histones at specific sites of the genome.
Hsu CJ, Meers O, Buschbeck M, Heidel FH.
europepmc   +2 more sources

Short H2A histone variants are expressed in cancer. [PDF]

open access: yesNat Commun, 2021
Short H2A (sH2A) histone variants are primarily expressed in the testes of placental mammals. Their incorporation into chromatin is associated with nucleosome destabilization and modulation of alternate splicing. Here, we show that sH2As innately possess
Chew GL   +6 more
europepmc   +2 more sources

LSH catalyzes ATP-driven exchange of histone variants macroH2A1 and macroH2A2. [PDF]

open access: yesNucleic Acids Res, 2021
LSH, a homologue of the ISWI/SNF2 family of chromatin remodelers, is required in vivo for deposition of the histone variants macroH2A1 and macroH2A2 at specific genomic locations.
Ni K, Muegge K.
europepmc   +2 more sources

Histone variants and chromatin structure, update of advances [PDF]

open access: yesComputational and Structural Biotechnology Journal, 2023
Histone proteins are highly conserved among all eukaryotes. They have two important functions in the cell: to package the genomic DNA and to regulate gene accessibility.
Vladyslava Sokolova   +2 more
doaj   +2 more sources

HIRA complex presets transcriptional potential through coordinating depositions of the histone variants H3.3 and H2A.Z on the poised genes in mESCs. [PDF]

open access: yesNucleic Acids Res, 2022
Histone variants have been implicated in regulating chromatin dynamics and genome functions. Previously, we have shown that histone variant H3.3 actively marks enhancers and cooperates with H2A.Z at promoters to prime the genes into a poised state in ...
Yang Y   +11 more
europepmc   +2 more sources

Histone variants: key regulators of inflammation in cell dedifferentiation and transdifferentiation [PDF]

open access: yesFrontiers in Immunology
Histone variants are specialized isoforms of histone proteins that play crucial roles in regulating chromatin structure and function, influencing transcription, DNA repair, and cell cycle progression.
Manlio Vinciguerra, Desislava K. Tsoneva
doaj   +2 more sources

Structural basis of nucleosome dynamics modulation by histone variants H2A.B and H2A.Z.2.2. [PDF]

open access: yesEMBO J, 2021
Nucleosomes are dynamic entities with wide‐ranging compositional variations. Human histone variants H2A.B and H2A.Z.2.2 play critical roles in multiple biological processes by forming unstable nucleosomes and open chromatin structures, but how H2A.B and ...
Zhou M   +8 more
europepmc   +2 more sources

Histone variants in archaea and the evolution of combinatorial chromatin complexity. [PDF]

open access: yesProc Natl Acad Sci U S A, 2020
Significance Chromatin in eukaryotes is built around histone–DNA complexes, which act as platforms for the integration of regulatory information. Different layers of information are integrated in a combinatorial fashion, for example by exchanging core ...
Stevens KM   +6 more
europepmc   +2 more sources

Elucidating the influence of linker histone variants on chromatosome dynamics and energetics. [PDF]

open access: yesNucleic Acids Res, 2020
Linker histones are epigenetic regulators that bind to nucleosomes and alter chromatin structures and dynamics. Biophysical studies have revealed two binding modes in the linker histone/nucleosome complex, the chromatosome, where the linker histone is ...
Woods DC, Wereszczynski J.
europepmc   +2 more sources

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