Brr2 plays a role in spliceosomal activation in addition to U4/U6 unwinding. - Wikidata - wikimedia - TriplyDB

Brr2 plays a role in spliceosomal activation in addition to U4/U6 unwinding.

Brr2 plays a role in spliceosomal activation in addition to U4/U6 unwinding.

http://www.wikidata.org/entity/Q35237021

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The organization and contribution of helicases to RNA splicing RNA-Binding Proteins: Splicing Factors and Disease Prp8 retinitis pigmentosa mutants cause defects in the transition between the catalytic steps of splicing.FgPrp4 Kinase Is Important for Spliceosome B-Complex Activation and Splicing Efficiency in Fusarium graminearum.Structural Analysis of Multi-Helical RNAs by NMR-SAXS/WAXS: Application to the U4/U6 di-snRNA.Retinitis Pigmentosa Mutations in Bad Response to Refrigeration 2 (Brr2) Impair ATPase and Helicase Activity RNA and Proteins: Mutual Respect.Functions and regulation of the Brr2 RNA helicase during splicing.The large N-terminal region of the Brr2 RNA helicase guides productive spliceosome activation.Structural and functional analyses of the spliceosome requires a multi-disciplinary approach.

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Brr2 plays a role in spliceosomal activation in addition to U4/U6 unwinding.

http://www.wikidata.org/entity/Q35237021

description

2015 nî lūn-bûn

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2015 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2015 թվականի փետրվարին հրատարակված գիտական հոդված

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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name

Brr2 plays a role in spliceosomal activation in addition to U4/U6 unwinding.

@ast

Brr2 plays a role in spliceosomal activation in addition to U4/U6 unwinding.

@en

type

label

Brr2 plays a role in spliceosomal activation in addition to U4/U6 unwinding.

@ast

Brr2 plays a role in spliceosomal activation in addition to U4/U6 unwinding.

@en

prefLabel

Brr2 plays a role in spliceosomal activation in addition to U4/U6 unwinding.

@ast

Brr2 plays a role in spliceosomal activation in addition to U4/U6 unwinding.

@en

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Brr2 plays a role in spliceosomal activation in addition to U4/U6 unwinding.

@en

P2093

Kirk C Hansen

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

Lingdi Zhang

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

Rui Zhao

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

Ryan C Hill

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

Wenzheng Zhang

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Xueni Li

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Yan Qiu

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P2860

An efficient one-step site-directed deletion, insertion, single and multiple-site plasmid mutagenesis protocol.

Structural basis for functional cooperation between tandem helicase cassettes in Brr2-mediated remodeling of the spliceosome

The human U5-200kD DEXH-box protein unwinds U4/U6 RNA duplices in vitro

The HeLa 200 kDa U5 snRNP-specific protein and its homologue in Saccharomyces cerevisiae are members of the DEXH-box protein family of putative RNA helicases

Prp8 protein: at the heart of the spliceosome

Biochemical and genetic analyses of the U5, U6, and U4/U6 x U5 small nuclear ribonucleoproteins from Saccharomyces cerevisiae

Structural evidence for consecutive Hel308-like modules in the spliceosomal ATPase Brr2

Structural Basis of Brr2-Prp8 Interactions and Implications for U5 snRNP Biogenesis and the Spliceosome Active Site

RNA unwinding in U4/U6 snRNPs requires ATP hydrolysis and the DEIH-box splicing factor Brr2

Comprehensive in vivo RNA-binding site analyses reveal a role of Prp8 in spliceosomal assembly.

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3286-3297

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scholarly article

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10.1093/NAR/GKV062

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43

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272190959

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25670679

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4381053

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