Core histone-DNA interactions in sea urchin sperm chromatin. The N-terminal tail of H2B interacts with linker DNA.
about
What determines the folding of the chromatin fiber?Assembly of CENP-A into centromeric chromatin requires a cooperative array of nucleosomal DNA contact sitesPhosphorylation-induced rearrangement of the histone H3 NH2-terminal domain during mitotic chromosome condensation.The A- and B-type cyclin associated cdc2 kinases in Xenopus turn on and off at different times in the cell cycle.Identification of a non-basic domain in the histone H4 N-terminus required for repression of the yeast silent mating loci.Histone H3 N-terminal mutations allow hyperactivation of the yeast GAL1 gene in vivo.Linker histone tails and N-tails of histone H3 are redundant: scanning force microscopy studies of reconstituted fibers.Phosphorylation of histone variant regions in chromatin: unlocking the linker?Histone and histone gene compilation and alignment update.Histone tails and the H3 alphaN helix regulate nucleosome mobility and stability.Identification of two DNA-binding sites on the globular domain of histone H5.Periodic binding of individual core histones to DNA: inadvertent purification of the core histone H2B as a putative enhancer-binding factorThe N-terminal tail of histone H2A binds to two distinct sites within the nucleosome core.Histone N-terminal tails interfere with nucleosome traversal by RNA polymerase II.Intrinsically disordered regions as affinity tuners in protein-DNA interactions.Regulation by phosphorylation of the zinc finger protein KRC that binds the kappaB motif and V(D)J recombination signal sequences.DNA looping by the HMG-box domains of HMG1 and modulation of DNA binding by the acidic C-terminal domain.Differential repression of transcription factor binding by histone H1 is regulated by the core histone amino termini.Histone-DNA interactions and their modulation by phosphorylation of -Ser-Pro-X-Lys/Arg- motifs.Two kinase activities are sufficient for sea urchin sperm chromatin decondensation in vitro.
P2860
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P2860
Core histone-DNA interactions in sea urchin sperm chromatin. The N-terminal tail of H2B interacts with linker DNA.
description
1990 nî lūn-bûn
@nan
1990年の論文
@ja
1990年学术文章
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1990年学术文章
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1990年学术文章
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1990年学术文章
@zh-hans
1990年学术文章
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1990年学术文章
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1990年學術文章
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1990年學術文章
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name
Core histone-DNA interactions ...... H2B interacts with linker DNA.
@en
Core histone-DNA interactions ...... H2B interacts with linker DNA.
@nl
type
label
Core histone-DNA interactions ...... H2B interacts with linker DNA.
@en
Core histone-DNA interactions ...... H2B interacts with linker DNA.
@nl
prefLabel
Core histone-DNA interactions ...... H2B interacts with linker DNA.
@en
Core histone-DNA interactions ...... H2B interacts with linker DNA.
@nl
P2860
P1433
P1476
Core histone-DNA interactions ...... H2B interacts with linker DNA.
@en
P2093
J O Thomas
P2860
P304
P356
10.1111/J.1432-1033.1990.TB15288.X
P407
P577
1990-01-01T00:00:00Z