A novel protein domain induces high affinity selenocysteine insertion sequence binding and elongation factor recruitment. - Test2 - elhamkhani - TriplyDB

A novel protein domain induces high affinity selenocysteine insertion sequence binding and elongation factor recruitment.

A novel protein domain induces high affinity selenocysteine insertion sequence binding and elongation factor recruitment.

http://www.wikidata.org/entity/Q42713881

about

The molecular biology of selenocysteine Synthesis and decoding of selenocysteine and human health Crystallization and preliminary X-ray structure analysis of human ribosomal protein L30e Nucleolin binds to a subset of selenoprotein mRNAs and regulates their expression Secisbp2 is essential for embryonic development and enhances selenoprotein expression The selenocysteine-specific elongation factor contains a novel and multi-functional domain Threading the needle: getting selenocysteine into proteins Selenoproteins: molecular pathways and physiological roles.The efficiency of selenocysteine incorporation is regulated by translation initiation factors.Selenocysteine insertion sequence binding protein 2L is implicated as a novel post-transcriptional regulator of selenoprotein expression.Selenocysteine insertion sequence (SECIS)-binding protein 2 alters conformational dynamics of residues involved in tRNA accommodation in 80 S ribosomes.The Selenocysteine-Specific Elongation Factor Contains Unique Sequences That Are Required for Both Nuclear Export and Selenocysteine Incorporation.Biochemical and pathological studies on peroxidases -an updated review.Characterization of the UGA-recoding and SECIS-binding activities of SECIS-binding protein 2 Reconstitution of selenocysteine incorporation reveals intrinsic regulation by SECIS elements.SECIS-binding protein 2 interacts with the SMN complex and the methylosome for selenoprotein mRNP assembly and translation.A novel insight into the mechanism of mammalian selenoprotein synthesis.A short motif in Drosophila SECIS Binding Protein 2 provides differential binding affinity to SECIS RNA hairpins Evolutionary history of selenocysteine incorporation from the perspective of SECIS binding proteins The SBP2 protein central to selenoprotein synthesis contacts the human ribosome at expansion segment 7L of the 28S rRNA.On elongation factor eEFSec, its role and mechanism during selenium incorporation into nascent selenoproteins.Eukaryotic Mechanisms of Selenocysteine Incorporation and Its Reconstitution In Vitro

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P2860

A novel protein domain induces high affinity selenocysteine insertion sequence binding and elongation factor recruitment.

http://www.wikidata.org/entity/Q42713881

description

2008 nî lūn-bûn

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2008年の論文

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2008年学术文章

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2008年学术文章

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2008年学术文章

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2008年学术文章

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2008年学术文章

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2008年學術文章

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2008年學術文章

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2008年學術文章

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name

A novel protein domain induces ...... elongation factor recruitment.

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A novel protein domain induces ...... elongation factor recruitment.

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A novel protein domain induces ...... elongation factor recruitment.

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A novel protein domain induces ...... elongation factor recruitment.

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A novel protein domain induces ...... elongation factor recruitment.

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A novel protein domain induces ...... elongation factor recruitment.

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A novel protein domain induces ...... elongation factor recruitment.

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P2093

Jesse Donovan

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

Jonathan N Gonzalez-Flores

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Kelvin Caban

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P2860

An improved definition of the RNA-binding specificity of SECIS-binding protein 2, an essential component of the selenocysteine incorporation machinery

The SBP2 and 15.5 kD/Snu13p proteins share the same RNA binding domain: identification of SBP2 amino acids important to SECIS RNA binding.

A novel RNA binding protein, SBP2, is required for the translation of mammalian selenoprotein mRNAs

Characterization of the SECIS binding protein 2 complex required for the co-translational insertion of selenocysteine in mammals

The selenocysteine incorporation machinery: interactions between the SECIS RNA and the SECIS-binding protein SBP2

Decoding apparatus for eukaryotic selenocysteine insertion.

Ribosomal protein L30 is a component of the UGA-selenocysteine recoding machinery in eukaryotes

Insight into mammalian selenocysteine insertion: domain structure and ribosome binding properties of Sec insertion sequence binding protein 2

Supramolecular complexes mediate selenocysteine incorporation in vivo

Efficiency of mammalian selenocysteine incorporation.

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35129-35139

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scholarly article

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10.1074/JBC.M806008200

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50

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283

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Paul R. Copeland

Ruchira Ranaweera

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2008-10-23T00:00:00Z

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18948268

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L-selenocysteine

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3073842

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