14-3-3 interaction with histone H3 involves a dual modification pattern of phosphoacetylation.
about
Modulation of 14-3-3 interaction with phosphorylated histone H3 by combinatorial modification patternsLysine acetylation: codified crosstalk with other posttranslational modificationsA peek into the complex realm of histone phosphorylationThe GCKIII kinase Sps1 and the 14-3-3 isoforms, Bmh1 and Bmh2, cooperate to ensure proper sporulation in Saccharomyces cerevisiae.Comprehensive histone phosphorylation analysis and identification of Pf14-3-3 protein as a histone H3 phosphorylation reader in malaria parasitesCrosstalk in inflammation: the interplay of glucocorticoid receptor-based mechanisms and kinases and phosphatasesQuantitative mass spectrometry of histones H3.2 and H3.3 in Suz12-deficient mouse embryonic stem cells reveals distinct, dynamic post-translational modifications at Lys-27 and Lys-36Sensing core histone phosphorylation - a matter of perfect timing.14-3-3 binding sites in the snail protein are essential for snail-mediated transcriptional repression and epithelial-mesenchymal differentiationEpigenetic regulation of estrogen-dependent memory.Histone code pathway involving H3 S28 phosphorylation and K27 acetylation activates transcription and antagonizes polycomb silencingMitogen- and stress-activated protein kinases 1 and 2 are required for maximal trefoil factor 1 inductionReaders of histone modifications.Identification of the Acetylation and Ubiquitin-Modified Proteome during the Progression of Skeletal Muscle Atrophy.Surf the post-translational modification network of p53 regulationGenome-wide phosphoacetylation of histone H3 at Drosophila enhancers and promotersHistone H3 phosphorylation - a versatile chromatin modification for different occasions.14-3-3 (Bmh) proteins regulate combinatorial transcription following RNA polymerase II recruitment by binding at Adr1-dependent promoters in Saccharomyces cerevisiae.Perceiving the epigenetic landscape through histone readers.Nuclear CaMKII enhances histone H3 phosphorylation and remodels chromatin during cardiac hypertrophy.H3 phosphorylation: dual role in mitosis and interphase.Combinatorial H3K9acS10ph histone modification in IgH locus S regions targets 14-3-3 adaptors and AID to specify antibody class-switch DNA recombination.The yeast 14-3-3 proteins BMH1 and BMH2 differentially regulate rapamycin-mediated transcription.Dynamic interplay between histone H3 modifications and protein interpreters: emerging evidence for a "histone language".Histone H3 phosphorylation, immediate-early gene expression, and the nucleosomal response: a historical perspective.Integrated mechanisms of CaMKII-dependent ventricular remodeling.A brief histone in time: understanding the combinatorial functions of histone PTMs in the nucleosome context.Citrullination/Methylation Crosstalk on Histone H3 Regulates ER-Target Gene Transcription.Beyond transcription factors: how oncogenic signalling reshapes the epigenetic landscape.Greater Than the Sum of Parts: Complexity of the Dynamic Epigenome.Elucidating combinatorial histone modifications and crosstalks by coupling histone-modifying enzyme with biotin ligase activity.Histone Post-Translational Modifications and Nucleosome Organisation in Transcriptional Regulation: Some Open Questions.A phosphorylation switch regulates the transcriptional activation of cell cycle regulator p21 by histone deacetylase inhibitors.Lack of 14-3-3 proteins in Saccharomyces cerevisiae results in cell-to-cell heterogeneity in the expression of Pho4-regulated genes SPL2 and PHO84.Molecular Modeling of Differentially Phosphorylated Serine 10 and Acetylated lysine 9/14 of Histone H3 Regulates their Interactions with 14-3-3ζ, MSK1, and MKP1.Proteomic analyses reveal that Sky1 modulates apoptosis and mitophagy in Saccharomyces cerevisiae cells exposed to cisplatin.Mitogen and stress-activated protein kinase 1 is required for gonadotropin-releasing hormone-mediated activation of gonadotropin α subunit expression.Control of histone H3 phosphorylation by CaMKIIδ in response to haemodynamic cardiac stress.Nuclear localization of 14-3-3epsilon inversely correlates with poor long-term survival of patients with colorectal cancer.Epigenomic Modifications Mediating Antibody Maturation.
P2860
Q24322623-AB2DA51F-BC1F-485E-9003-19F476099F21Q24644959-28BA8DBC-7D0C-48D9-AD56-0D9AD8F4B483Q26992357-107B80CB-3AA8-4B8A-87A2-ECCDCDF26316Q27935625-5A6CE314-5DAA-4E51-AD64-6A24B7919E2EQ27973893-07982EBC-2502-4465-A272-4F836E9290CCQ33636430-5AD08F68-2963-4784-95E1-4EF5E7C2C5B5Q33854968-ED59DB05-4157-46B4-8BA1-6314F249899BQ33920071-074B67C0-FE96-423F-8DE4-E489DAFC9D36Q33951080-5C742695-8DC0-40F6-9118-81C1749A1091Q34243105-FD69324F-9005-44C7-BF9D-5A642654902EQ34582928-8B08E84C-5C3D-4E1F-A807-A2A66C7CBA6FQ34722767-E12293EA-71E2-49AD-9331-DD2E205BC301Q35092783-F856010D-0A6F-4026-A715-DA4068F27B21Q35753878-A4BE16CF-9D56-4BE9-9AC3-F089A79E1AC6Q35967111-DA442EA3-B2F1-44F9-8C0E-E2B023D26497Q36021740-2308D4C1-0C9E-43CA-B3B6-6FB0BC39AC36Q36345651-17D0FCA1-DA3A-482B-BFF8-988D9FBA5B88Q36606989-068896D3-0550-47BC-9A52-188758A03F8BQ36821309-29A41215-672E-44D2-BCF1-84F6C3B11F93Q37148474-7791EDFC-5F4E-4611-9413-C2AB8A1288C6Q37629610-FA887851-6D5F-4C49-AE29-E68719F35ED8Q37634047-C121D9CC-B6DE-43E8-BE06-A073D3C3ABBDQ37644127-CCE03CC9-DC40-4C30-8ADC-D4949C66799BQ37829706-2473AEF4-2B11-4E3D-8533-7CBFC6A3BC0BQ37976424-99F0E991-0DCF-438E-8670-D0605C955CDCQ38198633-9E0859A9-B9E6-4867-A72E-1215C1C1EAA5Q38551630-83A880AE-FFA9-417E-82C4-71AF434BCB59Q38796261-E0CCC990-91EE-460A-AC1E-81095E29D54DQ38843250-919AC2CB-37C3-4858-A14A-9F6AF8CE5738Q38853113-19A5A6E4-3DA7-4C91-AAC4-9139B96CE276Q39222596-51467DA2-6E3D-4960-A2DA-0B30D7515AA3Q39390193-8518837D-C2BD-4770-9891-3ADA122F4CEEQ41198504-854017F3-3872-48B9-AACC-3122D15425C7Q41591473-EF85C739-CBC3-440E-9C8F-EE76A52B091DQ41858644-8A49641F-A467-4A93-B1E7-E50D5594B97AQ41960307-32F58CEB-4833-4FA6-83D4-9896B228EB4FQ42517177-0DE62BA3-77BE-4F2E-9F81-13C6D5433978Q43214561-131C2BA9-71ED-4C1B-AF4C-AA0B3A371E28Q44239731-6A84DBB6-9858-4470-91DB-FB38F0380A91Q55011560-A9A2B2A6-316C-4B5A-95A7-3B6703239939
P2860
14-3-3 interaction with histone H3 involves a dual modification pattern of phosphoacetylation.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
14-3-3 interaction with histon ...... pattern of phosphoacetylation.
@en
type
label
14-3-3 interaction with histon ...... pattern of phosphoacetylation.
@en
prefLabel
14-3-3 interaction with histon ...... pattern of phosphoacetylation.
@en
P2093
P2860
P356
P1476
14-3-3 interaction with histon ...... pattern of phosphoacetylation
@en
P2093
Jane Mellor
Ronen Marmorstein
Wendy Walter
P2860
P304
P356
10.1128/MCB.01457-07
P407
P577
2008-02-11T00:00:00Z