The structure of mouse HP1 suggests a unique mode of single peptide recognition by the shadow chromo domain dimer
about
The Heterochromatin Protein 1 familyDynamic associations of heterochromatin protein 1 with the nuclear envelopeThe middle region of an HP1-binding protein, HP1-BP74, associates with linker DNA at the entry/exit site of nucleosomal DNAThe histone methyltransferase SUV420H2 and Heterochromatin Proteins HP1 interact but show different dynamic behavioursA BEN-domain-containing protein associates with heterochromatin and represses transcriptionIsoform-specific interaction of HP1 with human TAFII130.Selective interaction between the chromatin-remodeling factor BRG1 and the heterochromatin-associated protein HP1alpha.Binding of EMSY to HP1beta: implications for recruitment of HP1beta and BS69Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27Set9, a novel histone H3 methyltransferase that facilitates transcription by precluding histone tail modifications required for heterochromatin formation.Recruitment of Tat to heterochromatin protein HP1 via interaction with CTIP2 inhibits human immunodeficiency virus type 1 replication in microglial cellsPositive selection drives the evolution of rhino, a member of the heterochromatin protein 1 family in DrosophilaMechanisms of functional promiscuity by HP1 proteinsEpigenetic inheritance: histone bookmarks across generationsEpigenetic virtues of chromodomainsPlasmodium falciparum heterochromatin protein 1 marks genomic loci linked to phenotypic variation of exported virulence factorsTALE-light imaging reveals maternally guided, H3K9me2/3-independent emergence of functional heterochromatin in Drosophila embryos.Arabidopsis DNA polymerase ϵ recruits components of Polycomb repressor complex to mediate epigenetic gene silencing.Structure of the HP1 chromodomain bound to histone H3 methylated at lysine 9Structural basis of HP1/PXVXL motif peptide interactions and HP1 localisation to heterochromatinThe HP1a disordered C terminus and chromo shadow domain cooperate to select target peptide partners.Plasmodium falciparum heterochromatin protein 1 binds to tri-methylated histone 3 lysine 9 and is linked to mutually exclusive expression of var genesBinding of heterochromatin protein 1 to the nuclear envelope is regulated by a soluble form of tubulinHistones H3/H4 form a tight complex with the inner nuclear membrane protein LBR and heterochromatin protein 1KRAB-zinc finger proteins and KAP1 can mediate long-range transcriptional repression through heterochromatin spreadingHP1 recruits activity-dependent neuroprotective protein to H3K9me3 marked pericentromeric heterochromatin for silencing of major satellite repeatsMethylation-independent binding to histone H3 and cell cycle-dependent incorporation of HP1beta into heterochromatinStructure of human MRG15 chromo domain and its binding to Lys36-methylated histone H3.Structure of the chromo barrel domain from the MOF acetyltransferase.Specificity of the HP1 chromo domain for the methylated N-terminus of histone H3.Does heterochromatin protein 1 always follow code?Phosphorylation site mutations in heterochromatin protein 1 (HP1) reduce or eliminate silencing activity.Direct interaction with a nuclear protein and regulation of gene silencing by a variant of the Ca2+-channel beta 4 subunit.Phosphorylation at Ser473 regulates heterochromatin protein 1 binding and corepressor function of TIF1beta/KAP1.HP1α mediates defective heterochromatin repair and accelerates senescence in Zmpste24-deficient cells.A heterochromatin protein 1 homologue in Caenorhabditis elegans acts in germline and vulval development.The hinge and chromo shadow domain impart distinct targeting of HP1-like proteinsThe MIS12 complex is a protein interaction hub for outer kinetochore assembly.Chromatin proteins are determinants of centromere function.Heterochromatin protein 1 (HP1) connects the FACT histone chaperone complex to the phosphorylated CTD of RNA polymerase II.
P2860
Q21999710-702EADED-61FD-44AA-BBE5-6322CA1CB51AQ24290572-3D7ED213-F5BA-4EAA-A03A-7A6BEB2051C7Q24293591-B6F2EA0C-0A82-47C5-BD76-593D21477573Q24315914-69C8A24B-636B-4554-8296-517719F8F2A3Q24337843-41CF8314-1F23-453D-8B48-3DCAC33C1CB9Q24534176-88B55851-6434-41E4-92E3-E4089D0B3D5DQ24539001-A30D7483-D6F3-422C-A4BF-731E34FAB2A9Q24539082-5934DF54-64E3-4FF8-BE98-59269C0CF6B1Q24672052-9DEF8136-AC6E-416C-BF93-45A58E24477FQ24672514-AA9B2805-CD91-46A6-AE99-1A7AA7F67116Q24679559-E7E2EF9B-7B72-46D4-A61C-81E4FCEFFF64Q24811626-78866DD7-5197-4FD2-9CB1-1CC62AC5E983Q26853658-9535858F-3A40-42E9-93DE-607AFECDC3FFQ27015080-07C80272-B8F5-4EC0-8BDF-C315BBA2EA39Q27016161-976771BD-49AA-40A6-8459-2C75235995CAQ27316324-F7D6EB0C-3648-4C64-8E52-34F2D8D482DDQ27322533-C9B0299D-B4A2-491B-8858-E0BDEB1D46E8Q27324008-07060CD9-0436-4B7B-A15E-9E82DB318953Q27638208-50BAA51E-26DD-4B9E-9C0A-F60DD4BDFA86Q27643095-60EAFAD7-DBA1-4474-9F0B-21A8D0812D6EQ27667453-EACF136F-D0DB-45BE-9FAF-565B1A554A63Q27974685-D7CB1E9E-F66A-4C45-A617-A764595AD506Q28207723-4A95F892-D949-4554-B027-5A09B2F5D5F7Q28360319-CB76D9D5-B3D4-4FC5-805C-AB69D246C6B8Q28473103-6F64A77C-4942-4DDA-9C08-EA5A51AD7F81Q28476760-1C3FCBE2-B49A-4AD3-B1D2-F276FFE3270FQ28593291-8055C9CE-7DA4-420A-A91C-F02F4B451A9DQ30159543-15B8370A-48E1-4438-A00B-158B2BC19418Q30160207-EA92BF19-8914-4BCB-9B66-FCCDDDC7D57EQ30307942-C2FA80AB-A757-4CBC-9EF5-A3DE2A1A881BQ30452367-23AED58C-E2B8-4CBB-8169-102E65F273DFQ30635763-3D63BDBA-57B1-4C04-8572-A5E2678BB932Q31125242-73F39DC3-A3E0-4023-AE3E-7BD2AE35AB31Q33347938-83E9B8F3-C0D9-42C0-BAE7-AF5269A7AAC3Q33728360-FDEAF223-B0A1-4E5E-AD17-367AC55A35A4Q33757634-F53E1798-97D2-4C7A-B2F5-AC9B1D19EABBQ33967856-8F5882C6-1D81-4D5D-A41D-7D99D73879C4Q34111005-9148AD99-66F4-4E9A-B8DB-435CECC17F02Q34131328-39FAA1AB-05AF-4C62-AAC8-A44DDEB1ED4AQ34164889-D640CEDA-B49E-4592-BD41-BF8752A8E4FA
P2860
The structure of mouse HP1 suggests a unique mode of single peptide recognition by the shadow chromo domain dimer
description
2000 nî lūn-bûn
@nan
2000 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
The structure of mouse HP1 sug ...... the shadow chromo domain dimer
@ast
The structure of mouse HP1 sug ...... the shadow chromo domain dimer
@en
The structure of mouse HP1 sug ...... the shadow chromo domain dimer
@nl
type
label
The structure of mouse HP1 sug ...... the shadow chromo domain dimer
@ast
The structure of mouse HP1 sug ...... the shadow chromo domain dimer
@en
The structure of mouse HP1 sug ...... the shadow chromo domain dimer
@nl
prefLabel
The structure of mouse HP1 sug ...... the shadow chromo domain dimer
@ast
The structure of mouse HP1 sug ...... the shadow chromo domain dimer
@en
The structure of mouse HP1 sug ...... the shadow chromo domain dimer
@nl
P2093
P2860
P356
P1433
P1476
The structure of mouse HP1 sug ...... the shadow chromo domain dimer
@en
P2093
D Nietlispach
N V Murzina
P R Nielsen
R W Broadhurst
S V Brasher
P2860
P304
P356
10.1093/EMBOJ/19.7.1587
P407
P577
2000-04-03T00:00:00Z