The hypusine-containing translation factor eIF5A. - Test2 - elhamkhani - TriplyDB

The hypusine-containing translation factor eIF5A.

The hypusine-containing translation factor eIF5A.

http://www.wikidata.org/entity/Q34283037

about

Ribosomal frameshifting and transcriptional slippage: From genetic steganography and cryptography to adventitious use Structure of the hypusinylated eukaryotic translation factor eIF-5A bound to the ribosome Crystal Structure of Hypusine-Containing Translation Factor eIF5A Bound to a Rotated Eukaryotic Ribosome eIF5A facilitates translation termination globally and promotes the elongation of many non polyproline-specific tripeptide sequences Genome-wide analyses and functional classification of proline repeat-rich proteins: potential role of eIF5A in eukaryotic evolution Mechanism of cytoplasmic mRNA translation.Deoxyhypusine Modification of Eukaryotic Translation Initiation Factor 5A (eIF5A) Is Essential for Trypanosoma brucei Growth and for Expression of Polyprolyl-containing Proteins Evidence for a Negative Cooperativity between eIF5A and eEF2 on Binding to the Ribosome The translation factor eIF5A and human cancer.Mechanism and Regulation of Protein Synthesis in Saccharomyces cerevisiae.Global quantitative proteomics reveal up-regulation of endoplasmic reticulum stress response proteins upon depletion of eIF5A in HeLa cells.Improved Synthesis of MDL 73811 - a Potent AdoMetDC Inhibitor and Anti-Trypanosomal Compound.Deciphering the Translation Initiation Factor 5A Modification Pathway in Halophilic Archaea.Relief of autoinhibition by conformational switch explains enzyme activation by a catalytically dead paralog The translation factors of Drosophila melanogaster Stall no more at polyproline stretches with the translation elongation factors EF-P and IF-5A.A new non-radioactive deoxyhypusine synthase assay adaptable to high throughput screening.Modifying the maker: Oxygenases target ribosome biology.eIF5A-PEAK1 Signaling Regulates YAP1/TAZ Protein Expression and Pancreatic Cancer Cell Growth.Hydroxylation and translational adaptation to stress: some answers lie beyond the STOP codon.eIF5A Functions Globally in Translation Elongation and Termination.Functions of Polyamines in Mammals The molecular choreography of protein synthesis: translational control, regulation, and pathways.Polyamines and Their Role in Virus Infection.Different polyamine pathways from bacteria have replaced eukaryotic spermidine biosynthesis in ciliates Tetrahymena thermophila and Paramecium tetaurelia.Translational stalling at polyproline stretches is modulated by the sequence context upstream of the stall site.Regulation of gene expression by translation factor eIF5A: Hypusine-modified eIF5A enhances nonsense-mediated mRNA decay in human cells.Synthesis and evaluation of analogs of 5'-(((Z)-4-amino-2-butenyl)methylamino)-5'-deoxyadenosine (MDL 73811, or AbeAdo) - An inhibitor of S-adenosylmethionine decarboxylase with antitrypanosomal activity.MsmiR156 affects global gene expression and promotes root regenerative capacity and nitrogen fixation activity in alfalfa.Evolutionary analysis of polyproline motifs in Escherichia coli reveals their regulatory role in translation.Molecular events leading to death of Leishmania donovani under spermidine starvation after hypericin treatment.KRAS oncoprotein expression is regulated by a self-governing eIF5A-PEAK1 feed-forward regulatory loop.Amino acid substrates impose polyamine, eIF5A, or hypusine requirement for peptide synthesis.Breaking the Silos of Protein Synthesis.Cytosolic iron chaperones: Proteins delivering iron cofactors in the cytosol of mammalian cells.Alternative Start Codon Connects eIF5A to Mitochondria.Hypusination of eIF5A as a Target for Antiviral Therapy.The role of polyproline motifs in the histidine kinase EnvZ.Modification of translation factor aIF5A from Sulfolobus solfataricus Differential Mechanisms for the Involvement of Polyamines and Hypusinated eIF5A in Ebola Virus Gene Expression

P2860

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P2860

The hypusine-containing translation factor eIF5A.

http://www.wikidata.org/entity/Q34283037

description

2014 nî lūn-bûn

@nan

2014 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի հուլիսին հրատարակված գիտական հոդված

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2014年の論文

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2014年論文

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2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

The hypusine-containing translation factor eIF5A.

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The hypusine-containing translation factor eIF5A.

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The hypusine-containing translation factor eIF5A.

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type

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The hypusine-containing translation factor eIF5A.

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The hypusine-containing translation factor eIF5A.

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The hypusine-containing translation factor eIF5A.

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The hypusine-containing translation factor eIF5A.

@ast

The hypusine-containing translation factor eIF5A.

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The hypusine-containing translation factor eIF5A.

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10409238.2014.939608

P1433

Critical Reviews in Biochemistry and Molecular Biology

P1476

The hypusine-containing translation factor eIF5A.

@en

P2093

Byung-Sik Shin

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

Erik Gutierrez

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

P2860

Specificity of the deoxyhypusine hydroxylase-eukaryotic translation initiation factor (eIF5A) interaction: identification of amino acid residues of the enzyme required for binding of its substrate, deoxyhypusine-containing eIF5A

Molecular cloning, expression, and structural prediction of deoxyhypusine hydroxylase: a HEAT-repeat-containing metalloenzyme.

Inhibition of HIV-1 replication in lymphocytes by mutants of the Rev cofactor eIF-5A

Crystal structure of elongation factor P from Thermus thermophilus HB8

Post-translational modification by β-lysylation is required for activity of Escherichia coli elongation factor P (EF-P)

Slow peptide bond formation by proline and other N-alkylamino acids in translation

The post-translational synthesis of a polyamine-derived amino acid, hypusine, in the eukaryotic translation initiation factor 5A (eIF5A)

Mutational analyses of human eIF5A-1--identification of amino acid residues critical for eIF5A activity and hypusine modification

Cofactor requirements for nuclear export of Rev response element (RRE)- and constitutive transport element (CTE)-containing retroviral RNAs. An unexpected role for actin.

Eukaryotic initiation factor 5A is a cellular target of the human immunodeficiency virus type 1 Rev activation domain mediating trans-activation

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413-425

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scholarly article

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10.3109/10409238.2014.939608

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5

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49

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2014-07-17T00:00:00Z

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4183722

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