Structural organization of a Sex-comb-on-midleg/polyhomeotic copolymer. - Wikidata - wikimedia - TriplyDB

Structural organization of a Sex-comb-on-midleg/polyhomeotic copolymer.

Structural organization of a Sex-comb-on-midleg/polyhomeotic copolymer.

http://www.wikidata.org/entity/Q46307097

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SAMHD1 is a nucleic-acid binding protein that is mislocalized due to aicardi-goutières syndrome-associated mutations Molecular recognition of histone lysine methylation by the Polycomb group repressor dSfmbt SFMBT1 functions with LSD1 to regulate expression of canonical histone genes and chromatin-related factors The quest for mammalian Polycomb response elements: are we there yet?Chromatin topology is coupled to Polycomb group protein subnuclear organization.CNK and HYP form a discrete dimer by their SAM domains to mediate RAF kinase signaling Crystal Structure of the Central Coiled-Coil Domain from Human Liprin-β2 Solution NMR Structure of the DNA-binding Domain from Scml2 (Sex Comb on Midleg-like 2)Characterization of the SAM domain of the PKD-related protein ANKS6 and its interaction with ANKS3 Multiple polymer architectures of human polyhomeotic homolog 3 sterile alpha motif A critical perspective of the diverse roles of O-GlcNAc transferase in chromatin A new mode of SAM domain mediated oligomerization observed in the CASKIN2 neuronal scaffolding protein.The NMR structure of the murine DLC2 SAM domain reveals a variant fold that is similar to a four-helix bundle A human sterile alpha motif domain polymerizome.Small ubiquitin-like modifier (SUMO) conjugation impedes transcriptional silencing by the polycomb group repressor Sex Comb on Midleg Sex comb on midleg (Scm) is a functional link between PcG-repressive complexes in Drosophila LIN-61, one of two Caenorhabditis elegans malignant-brain-tumor-repeat-containing proteins, acts with the DRM and NuRD-like protein complexes in vulval development but not in certain other biological processes.The relationship between long-range chromatin occupancy and polymerization of the Drosophila ETS family transcriptional repressor Yan Heterotypic Sam-Sam association between Odin-Sam1 and Arap3-Sam: binding affinity and structural insights MBT domain proteins in development and disease Are we there yet? Initial targeting of the Male-Specific Lethal and Polycomb group chromatin complexes in Drosophila.Chromatin in the nuclear landscape.Epigenetics meets mathematics: towards a quantitative understanding of chromatin biology.Chromatin regulation: how complex does it get?Identification and characterization of Polycomb group genes in the silkworm, Bombyx mori.Zinc binding drives sheet formation by the SAM domain of diacylglycerol kinase δ.Sterile alpha motif domain-mediated self-association plays an essential role in modulating the activity of the Drosophila ETS family transcriptional repressor Yan.Human polyhomeotic homolog 3 (PHC3) sterile alpha motif (SAM) linker allows open-ended polymerization of PHC3 SAM.Molecular basis of PRC1 targeting to Polycomb response elements by PhoRC.The growth-suppressive function of the polycomb group protein polyhomeotic is mediated by polymerization of its sterile alpha motif (SAM) domain Structural insights into SAM domain-mediated tankyrase oligomerization.Identifying polymer-forming SAM domains.Mae inhibits Pointed-P2 transcriptional activity by blocking its MAPK docking site.Characterization of the near native conformational states of the SAM domain of Ste11 protein by NMR spectroscopy.Polycomb and Trithorax Group Genes in Drosophila.Sequence-specific recognition of RNA hairpins by the SAM domain of Vts1p.Samd7 is a cell type-specific PRC1 component essential for establishing retinal rod photoreceptor identity.Influence of the R823W mutation on the interaction of the ANKS6-ANKS3: insights from molecular dynamics simulation and free energy analysis.

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P2860

Structural organization of a Sex-comb-on-midleg/polyhomeotic copolymer.

http://www.wikidata.org/entity/Q46307097

description

2005 nî lūn-bûn

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2005年の論文

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2005年学术文章

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name

Structural organization of a Sex-comb-on-midleg/polyhomeotic copolymer.

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Structural organization of a Sex-comb-on-midleg/polyhomeotic copolymer.

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type

label

Structural organization of a Sex-comb-on-midleg/polyhomeotic copolymer.

@en

Structural organization of a Sex-comb-on-midleg/polyhomeotic copolymer.

@nl

prefLabel

Structural organization of a Sex-comb-on-midleg/polyhomeotic copolymer.

@en

Structural organization of a Sex-comb-on-midleg/polyhomeotic copolymer.

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Journal of Biological Chemistry

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Structural organization of a Sex-comb-on-midleg/polyhomeotic copolymer.

@en

P2093

Chongwoo A Kim

http://www.w3.org/2001/XMLSchema#string

Duilio Cascio

http://www.w3.org/2001/XMLSchema#string

James U Bowie

http://www.w3.org/2001/XMLSchema#string

Michael R Sawaya

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Woojae Kim

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P2860

BAR: An apoptosis regulator at the intersection of caspases and Bcl-2 family proteins

A domain shared by the Polycomb group proteins Scm and ph mediates heterotypic and homotypic interactions

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Processing of X-ray diffraction data collected in oscillation mode

Polymerization of the SAM domain of TEL in leukemogenesis and transcriptional repression

RNA recognition via the SAM domain of Smaug

The CCP4 suite: programs for protein crystallography

The RNA-binding SAM domain of Smaug defines a new family of post-transcriptional regulators.

The polycomb protein Pc2 is a SUMO E3

Advances in direct methods for protein crystallography

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27769-27775

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scholarly article

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10.1074/JBC.M503055200

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30

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280

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2005-05-19T00:00:00Z

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15905166

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