Properties of a genetically engineered G domain of elongation factor Tu. - Wikidata - wikimedia - TriplyDB

Properties of a genetically engineered G domain of elongation factor Tu.

Properties of a genetically engineered G domain of elongation factor Tu.

http://www.wikidata.org/entity/Q34622043

about

Catalytic activity of an isolated domain of Na,K-ATPase expressed in Escherichia coli.Elongation factor Tu: a molecular switch in protein biosynthesis.Initiation of protein synthesis in bacteria.Tracing the Archaeal Origins of Eukaryotic Membrane-Trafficking System Building Blocks.Interaction of mammalian mitochondrial elongation factor EF-Tu with guanine nucleotides GTPase domains of ras p21 oncogene protein and elongation factor Tu: analysis of three-dimensional structures, sequence families, and functional sites Histidine-118 of elongation factor Tu: its role in aminoacyl-tRNA binding and regulation of the GTPase activity.Structure-function relationships in the GTP binding domain of EF-Tu: mutation of Val20, the residue homologous to position 12 in p21 Elfamycins: inhibitors of elongation factor-Tu.A single amino acid substitution in elongation factor Tu disrupts interaction between the ternary complex and the ribosome.Interaction of the isolated domain II/III of Thermus thermophilus elongation factor Tu with the nucleotide exchange factor EF-Ts.New antibiotic that acts specifically on the GTP-bound form of elongation factor Tu.Cell 'guidling'Thermostability of multidomain proteins: elongation factors EF-Tu from Escherichia coli and Bacillus stearothermophilus and their chimeric forms.The importance of P-loop and domain movements in EF-Tu for guanine nucleotide exchange.

P2860

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P2860

Properties of a genetically engineered G domain of elongation factor Tu.

http://www.wikidata.org/entity/Q34622043

description

1987 nî lūn-bûn

@nan

1987 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

1987 թվականի մայիսին հրատարակված գիտական հոդված

@hy

1987年の論文

@ja

1987年論文

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1987年論文

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1987年論文

@zh-hk

1987年論文

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1987年論文

@zh-tw

1987年论文

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name

Properties of a genetically engineered G domain of elongation factor Tu.

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Properties of a genetically engineered G domain of elongation factor Tu.

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Properties of a genetically engineered G domain of elongation factor Tu.

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type

label

Properties of a genetically engineered G domain of elongation factor Tu.

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Properties of a genetically engineered G domain of elongation factor Tu.

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Properties of a genetically engineered G domain of elongation factor Tu.

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prefLabel

Properties of a genetically engineered G domain of elongation factor Tu.

@ast

Properties of a genetically engineered G domain of elongation factor Tu.

@en

Properties of a genetically engineered G domain of elongation factor Tu.

@nl

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PNAS.84.10.3141

P1433

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

P1476

Properties of a genetically engineered G domain of elongation factor Tu.

@en

P2093

Clark BF

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Cortese R

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Dente L

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Jensen M

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Mortensen KK

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Parmeggiani A

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Swart GW

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P2860

Structure of the GDP domain of EF-Tu and location of the amino acids homologous to ras oncogene proteins

Structural details of the binding of guanosine diphosphate to elongation factor Tu from E. coli as studied by X-ray crystallography

A product of yeast RAS2 gene is a guanine nucleotide binding protein.

Guanine nucleotide-binding activity as an assay for src protein of rat-derived murine sarcoma viruses

Kirromycin, an inhibitor of protein biosynthesis that acts on elongation factor Tu

G proteins and dual control of adenylate cyclase.

Bacteriophage Q replicase contains the protein biosynthesis elongation factors EF Tu and EF Ts.

Mutant ras-encoded proteins with altered nucleotide binding exert dominant biological effects.

Simple method for identification of plasmid-coded proteins.

pEMBL: a new family of single stranded plasmids

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3141-3145

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scholarly article

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10.1073/PNAS.84.10.3141

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10

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84

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1987-05-01T00:00:00Z

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3554231

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304824

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