Structural Studies of the Tandem Tudor Domains of Fragile X Mental Retardation Related Proteins FXR1 and FXR2 - Test2 - elhamkhani - TriplyDB

Structural Studies of the Tandem Tudor Domains of Fragile X Mental Retardation Related Proteins FXR1 and FXR2

Structural Studies of the Tandem Tudor Domains of Fragile X Mental Retardation Related Proteins FXR1 and FXR2

http://www.wikidata.org/entity/Q27665857

about

Recognition of multivalent histone states associated with heterochromatin by UHRF1 protein Sgf29 binds histone H3K4me2/3 and is required for SAGA complex recruitment and histone H3 acetylation.PHF20 is an effector protein of p53 double lysine methylation that stabilizes and activates p53 RNA Secondary Structure Modulates FMRP's Bi-Functional Role in the MicroRNA Pathway Structure and function of WD40 domain proteins Structural and Histone Binding Ability Characterizations of Human PWWP Domains Crystal Structure of TDRD3 and Methyl-Arginine Binding Characterization of TDRD3, SMN and SPF30 The amino-terminal structure of human fragile X mental retardation protein obtained using precipitant-immobilized imprinted polymers Fragile X mental retardation protein: A paradigm for translational control by RNA-binding proteins Subcellular fractionation and localization studies reveal a direct interaction of the fragile X mental retardation protein (FMRP) with nucleolin A chromatin-dependent role of the fragile X mental retardation protein FMRP in the DNA damage response Differential increases of specific FMR1 mRNA isoforms in premutation carriers Fragile X mental retardation protein regulates translation by binding directly to the ribosome The tandem Agenet domain of fragile X mental retardation protein interacts with FUS.dFmr1 Plays Roles in Small RNA Pathways of Drosophila melanogaster.Human FMRP contains an integral tandem Agenet (Tudor) and KH motif in the amino terminal domain.Fmr1 KO and fenobam treatment differentially impact distinct synapse populations of mouse neocortex.FXR1 regulates transcription and is required for growth of human cancer cells with TP53/FXR2 homozygous deletion.Regulation of Adult Neurogenesis by the Fragile X Family of RNA Binding Proteins

P2860

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P2860

Structural Studies of the Tandem Tudor Domains of Fragile X Mental Retardation Related Proteins FXR1 and FXR2

http://www.wikidata.org/entity/Q27665857

description

2010 nî lūn-bûn

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2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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2010 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

Structural Studies of the Tand ...... Related Proteins FXR1 and FXR2

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Structural Studies of the Tand ...... Related Proteins FXR1 and FXR2

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Structural Studies of the Tand ...... Related Proteins FXR1 and FXR2

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type

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Structural Studies of the Tand ...... Related Proteins FXR1 and FXR2

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Structural Studies of the Tand ...... Related Proteins FXR1 and FXR2

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Structural Studies of the Tand ...... Related Proteins FXR1 and FXR2

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Structural studies of the tand ...... related proteins FXR1 and FXR2

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Structural Studies of the Tand ...... Related Proteins FXR1 and FXR2

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Structural Studies of the Tand ...... Related Proteins FXR1 and FXR2

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Structural Studies of the Tand ...... Related Proteins FXR1 and FXR2

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Structural Studies of the Tand ...... Related Proteins FXR1 and FXR2

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ChuanBing Bian

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Jinrong Min

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Maria F Amaya

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Melanie A Adams-Cioaba

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Robert Lam

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

Yahong Guo

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P2860

Structural studies of a four-MBT repeat protein MBTD1

The structure of the N-terminal domain of the fragile X mental retardation protein: a platform for protein-protein interaction

Structural basis for molecular recognition and presentation of histone H3 by WDR5

The fragile X mental retardation syndrome protein interacts with novel homologs FXR1 and FXR2

Methylation-state-specific recognition of histones by the MBT repeat protein L3MBTL2

FXR1, an autosomal homolog of the fragile X mental retardation gene

Fragile X syndrome: loss of local mRNA regulation alters synaptic development and function

PHENIX: a comprehensive Python-based system for macromolecular structure solution

Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27

Processing of X-ray diffraction data collected in oscillation mode

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11

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Gregory A Wasney

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