Identification of a soluble protein that stimulates peptide bond synthesis. - Wikidata - awgldk - TriplyDB

Identification of a soluble protein that stimulates peptide bond synthesis.

Identification of a soluble protein that stimulates peptide bond synthesis.

http://www.wikidata.org/entity/Q37458526

about

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 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)The post-translational synthesis of a polyamine-derived amino acid, hypusine, in the eukaryotic translation initiation factor 5A (eIF5A)Structure of the hypusinylated eukaryotic translation factor eIF-5A bound to the ribosome Formation of the First Peptide Bond: The Structure of EF-P Bound to the 70S Ribosome Hypusine-containing protein eIF5A promotes translation elongation Neisseria meningitidis Translation Elongation Factor P and Its Active-Site Arginine Residue Are Essential for Cell Viability tRNA mimicry in translation termination and beyond.Novel genes associated with enhanced motility of Escherichia coli ST131.Functional significance of eIF5A and its hypusine modification in eukaryotes Nascent peptide as sole attachment of polysomes to membranes in bacteria.The chvH locus of Agrobacterium encodes a homologue of an elongation factor involved in protein synthesis.Crystallization and preliminary X-ray crystallographic study of GenX, a lysyl-tRNA synthetase paralogue from Escherichia coli, in complex with translation elongation factor P.Lys34 of translation elongation factor EF-P is hydroxylated by YfcM.The hypusine-containing translation factor eIF5A.Biochemistry. Getting past polyproline pauses Production of active recombinant eIF5A: reconstitution in E.coli of eukaryotic hypusine modification of eIF5A by its coexpression with modifying enzymes.Evolutionary conservation of reactions in translation Virus evolution toward limited dependence on nonessential functions of the host: the case of bacteriophage SPP1.The roles of RNA in the synthesis of protein.Loss of elongation factor P disrupts bacterial outer membrane integrity Elongation factor P mediates a novel post-transcriptional regulatory pathway critical for bacterial virulence Cloning, sequencing and overexpression of the gene for prokaryotic factor EF-P involved in peptide bond synthesis.Deoxyhypusine hydroxylase is a Fe(II)-dependent, HEAT-repeat enzyme. Identification of amino acid residues critical for Fe(II) binding and catalysis [corrected].The elongation, termination, and recycling phases of translation in eukaryotes.The translation factor eIF5A and human cancer.The weird and wonderful world of bacterial ribosome regulation.Global quantitative proteomics reveal up-regulation of endoplasmic reticulum stress response proteins upon depletion of eIF5A in HeLa cells.eIF5A promotes translation of polyproline motifs.Structural modeling and mutational analysis of yeast eukaryotic translation initiation factor 5A reveal new critical residues and reinforce its involvement in protein synthesis Isolation and point of action of a factor from Escherichia coli required to reconstruct translation.Strategies to ameliorate abiotic stress-induced plant senescence.eIF5A and EF-P: two unique translation factors are now traveling the same road.Stall no more at polyproline stretches with the translation elongation factors EF-P and IF-5A.tRNAPro -mediated downregulation of elongation factor P is required for mgtCBR expression during Salmonella infection.eIF5A Functions Globally in Translation Elongation and Termination.Mapping surface residues of eIF5A that are important for binding to the ribosome using alanine scanning mutagenesis.Oxazolidinone antibiotics target the P site on Escherichia coli ribosomes.Nonribosomal incorporation of amino acids into the troponin-like protein from synaptosomes.

P2860

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P2860

Identification of a soluble protein that stimulates peptide bond synthesis.

http://www.wikidata.org/entity/Q37458526

description

1975 nî lūn-bûn

@nan

1975年の論文

@ja

1975年学术文章

@wuu

1975年学术文章

@zh-cn

1975年学术文章

@zh-hans

1975年学术文章

@zh-my

1975年学术文章

@zh-sg

1975年學術文章

@yue

1975年學術文章

@zh

1975年學術文章

@zh-hant

name

Identification of a soluble protein that stimulates peptide bond synthesis.

@en

Identification of a soluble protein that stimulates peptide bond synthesis.

@nl

type

label

Identification of a soluble protein that stimulates peptide bond synthesis.

@en

Identification of a soluble protein that stimulates peptide bond synthesis.

@nl

prefLabel

Identification of a soluble protein that stimulates peptide bond synthesis.

@en

Identification of a soluble protein that stimulates peptide bond synthesis.

@nl

P1433

Q37458526-D8696AE9-86BA-4210-8D1A-81BE7EFE756A

P1476

Q37458526-44A48DB5-7D81-4DE1-98F2-6D810F41EC0B

P2093

Q37458526-18D01474-7467-41E3-BB50-32B446078A15

Q37458526-A02C286A-2627-4079-9CA6-81DC85F94909

P2860

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Q37458526-16A8BBF9-B45F-4F72-B830-60E3E7D78DA1

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P31

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P356

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P407

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P433

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P478

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P577

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P5875

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P698

Q37458526-A850A9DA-FFB8-4447-8705-FA4C608D8A8E

P932

Q37458526-2004F908-5BE7-450E-8D25-464FA07A120B

P356

PNAS.72.11.4257

P1433

Proceedings of the National Academy of Sciences of the United States of America

P1476

Identification of a soluble protein that stimulates peptide bond synthesis.

@en

P2093

Ganoza MC

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

Glick BR

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

P2860

Peptidyl-puromycin synthesis on polyribosomes from Escherichia coli

Inhibition of polypeptide chain initiation in Escherichia coli by elongation factor G.

RNA CODEWORDS AND PROTEIN SYNTHESIS. THE EFFECT OF TRINUCLEOTIDES UPON THE BINDING OF SRNA TO RIBOSOMES.

The peptidyl transferase activity of ribosomes.

Isolation of a factor that stimulates cleavage of ribosomal bound N-acetyl or N-formyl methionyl tRNA-Met.

Ribosome-catalyzed ester formation.

Initiation of protein synthesis II. A convenient assay for the ribosome-dependent synthesis of N-formyl-C14-methionylpuromycin.

The reactions of the sulfhydryl groups on the elongation factors Tu and Ts.

Studies on the formation of transfer ribonucleic acid-ribosome complexes. VI. Oligopeptide synthesis and translocation on ribosomes in the presence and absence of soluble transfer factors.

Occurrence of initiation factor 2 in the postribosomal fraction and identification of an initiation inhibitor as elongation factor G.

P304

4257-4260

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P31

scholarly article

P356

10.1073/PNAS.72.11.4257

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P407

P433

11

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P478

72

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P577

1975-11-01T00:00:00Z

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P5875

22048695

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P698

1105576

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P932

388699

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