Identification and characterization of the methyl arginines in the fragile X mental retardation protein Fmrp. - Wikidata - awgldk - TriplyDB

Identification and characterization of the methyl arginines in the fragile X mental retardation protein Fmrp.

Identification and characterization of the methyl arginines in the fragile X mental retardation protein Fmrp.

http://www.wikidata.org/entity/Q38318254

about

Accurate localization and relative quantification of arginine methylation using nanoflow liquid chromatography coupled to electron transfer dissociation and orbitrap mass spectrometry The new (dis)order in RNA regulation The pathophysiology of fragile X (and what it teaches us about synapses)The RNA-binding proteins FMR1, rasputin and caprin act together with the UBA protein lingerer to restrict tissue growth in Drosophila melanogaster Structure-function studies of FMRP RGG peptide recognition of an RNA duplex-quadruplex junction In vitro and in cellulo evidences for association of the survival of motor neuron complex with the fragile X mental retardation protein Fragile X mental retardation protein FMRP binds mRNAs in the nucleus Arginines of the RGG box regulate FMRP association with polyribosomes and mRNA.Fragile X protein family member FXR1P is regulated by microRNAs Influence of sequential guanidinium methylation on the energetics of the guanidinium...guanine dimer and guanidinium...guanine...cytosine trimer: implications for the control of protein...DNA interactions by arginine methyltransferases.Increasing our understanding of human cognition through the study of Fragile X Syndrome.Identification of a novel lipin homologue from the parasitic protozoan Trypanosoma brucei.A non-canonical start codon in the Drosophila fragile X gene yields two functional isoforms Arginine methylation regulates mitochondrial gene expression in Trypanosoma brucei through multiple effector proteins.A new regulatory function of the region proximal to the RGG box in the fragile X mental retardation protein Arginine methylation of RNA-binding proteins regulates cell function and differentiation Generation of polyclonal antiserum for the detection of methylarginine proteins.Crystal structure reveals specific recognition of a G-quadruplex RNA by a β-turn in the RGG motif of FMRP.The FMRP/GRK4 mRNA interaction uncovers a new mode of binding of the Fragile X mental retardation protein in cerebellum Specific sequences within arginine-glycine-rich domains affect mRNA-binding protein function.Top3β is an RNA topoisomerase that works with fragile X syndrome protein to promote synapse formation.Overexpression of Down syndrome cell adhesion molecule impairs precise synaptic targeting Arginine/lysine-methyl/methyl switches: biochemical role of histone arginine methylation in transcriptional regulation.Protein arginine methylation in Saccharomyces cerevisiae.Recombinant bacterial expression and purification of human fragile X mental retardation protein isoform 1.Conformational-dependent and independent RNA binding to the fragile x mental retardation protein.Evolutionarily divergent type II protein arginine methyltransferase in Trypanosoma brucei.Biophysical characterization of G-quadruplex forming FMR1 mRNA and of its interactions with different fragile X mental retardation protein isoforms.Insights into the post-translational methylation of arginine from studies of guanidinium-water nanodroplets.Protein arginine methylation modulates light-harvesting antenna translation in Chlamydomonas reinhardtii.Differential interaction of PRMT1 with RGG-boxes of the FET family proteins EWS and TAF15.Altered expression of the FMR1 splicing variants landscape in premutation carriers.Analysis of the Fragile X mental retardation protein isoforms 1, 2 and 3 interactions with the G-quadruplex forming semaphorin 3F mRNA.Post-Translational Modifications and RNA-Binding Proteins.Differential effects of arginine methylation on RBP16 mRNA binding, guide RNA (gRNA) binding, and gRNA-containing ribonucleoprotein complex (gRNP) formation.

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P2860

Identification and characterization of the methyl arginines in the fragile X mental retardation protein Fmrp.

http://www.wikidata.org/entity/Q38318254

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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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年學術文章

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2005年學術文章

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2005年學術文章

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Identification and characteriz ...... ntal retardation protein Fmrp.

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type

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Identification and characteriz ...... ntal retardation protein Fmrp.

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prefLabel

Identification and characteriz ...... ntal retardation protein Fmrp.

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Human Molecular Genetics

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Identification and characteriz ...... ntal retardation protein Fmrp.

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P2093

Anne Cheever

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

April Stetler

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Claudia Winograd

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Erin Patton

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Joyce Sayegh

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

Stephanie Ceman

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

Steven Clarke

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

Xing Zhang

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P2860

The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity

Spliceosome Sm proteins D1, D3, and B/B' are asymmetrically dimethylated at arginine residues in the nucleus

Ribosomal protein S2 is a substrate for mammalian PRMT3 (protein arginine methyltransferase 3)

PRMT 3, a type I protein arginine N-methyltransferase that differs from PRMT1 in its oligomerization, subcellular localization, substrate specificity, and regulation

Essential role for KH domains in RNA binding: impaired RNA binding by a mutation in the KH domain of FMR1 that causes fragile X syndrome

PRMT8, a new membrane-bound tissue-specific member of the protein arginine methyltransferase family

FMR1 protein: conserved RNP family domains and selective RNA binding

Protein arginine methyltransferase 6 specifically methylates the nonhistone chromatin protein HMGA1a

Isolation of an FMRP-associated messenger ribonucleoprotein particle and identification of nucleolin and the fragile X-related proteins as components of the complex

PRMT3 is a ribosomal protein methyltransferase that affects the cellular levels of ribosomal subunits

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87-96

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10.1093/HMG/DDI429

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1

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15

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7450120

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16319129

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