A complex profile of protein elongation: translating chemical energy into molecular movement (Q41111056)

26 September 2017

title

A complex profile of protein elongation: translating chemical energy into molecular movement (English)

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26 September 2017

Abel K

1

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26 September 2017

Jurnak F

series ordinal

2

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26 September 2017

publication date

1 March 1996

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26 September 2017

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26 September 2017

volume

4

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26 September 2017

issue

3

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26 September 2017

page(s)

229-238

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publication type of scholarly work

26 September 2017

review article

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The GTPase superfamily: a conserved switch for diverse cell functions

cites work

1 reference

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7 January 2021

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

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7 January 2021

GTP-binding domain: three consensus sequence elements with distinct spacing

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7 January 2021

The GTPase superfamily: conserved structure and molecular mechanism

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https://api.crossref.org/works/10.1016%2FS0969-2126%2896%2900027-5

7 January 2021

Crystal structure of active elongation factor Tu reveals major domain rearrangements

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7 January 2021

The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation

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7 January 2021

Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog

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7 January 2021

The structure of the Escherichia coli EF-Tu.EF-Ts complex at 2.5 A resolution

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2896%2900027-5

7 January 2021

Identification of a histidine residue near the aminoacyl transfer ribonucleic acid binding site of elongation factor Tu.

1 reference

https://api.crossref.org/works/10.1016%2FS0969-2126%2896%2900027-5

7 January 2021

The site of interaction of aminoacyl-tRNA with elongation factor Tu

1 reference

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7 January 2021

A second tRNA binding site on elongation factor Tu is induced while the factor is bound to the ribosome

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7 January 2021

How many EF-Tu molecules participate in aminoacyl-tRNA binding and peptide bond formation in Escherichia coli translation?

1 reference

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7 January 2021

GTP consumption of elongation factor Tu during translation of heteropolymeric mRNAs

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7 January 2021

The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution

1 reference

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7 January 2021

Evidence that the G2661 region of 23S rRNA is located at the ribosomal binding sites of both elongation factors.

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7 January 2021

Interaction of elongation factors EF-G and EF-Tu with a conserved loop in 23S RNA.

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7 January 2021

Localization of the elongation factor G on Escherichia coli ribosome

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7 January 2021

Localization of elongation factor Tu on the ribosome

1 reference

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7 January 2021

Elongation factor Tu localized on the exterior surface of the small ribosomal subunit

1 reference

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7 January 2021

Molecular mimicry in protein synthesis?

1 reference

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7 January 2021

Equilibrium measurements of the interactions of guanine nucleotides with Escherichia coli elongation factor G and the ribosome

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7 January 2021

Crystallization and preliminary x-ray diffraction data of the EF-Tu . EF-Ts (EF-T) complex of Escherichia coli

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7 January 2021

Extension of the diffraction resolution of crystals

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7 January 2021

Purification of factor Ts: studies on the formation and stability of nucleotide complexes containing transfer factor Tu.

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7 January 2021

Studies on the polypeptide elongation factors from E. coli. 3. Molecular characteristics of EF-Tu-guanosine diphosphate, EP-Ts, and EF-Tu-Ts complex

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7 January 2021

Studies on Polypeptide-Chain-Elongation Factors from an Extreme Thermophile, Thermus thermophilus HB8. 2. Catalytic Properties

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7 January 2021

Novel data on interactions of elongation factor Ts.

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7 January 2021

RNA Replication: Function and Structure of QBeta-Replicase

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7 January 2021

How does the switch II region of G-domains work?

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7 January 2021

Toward a model for the interaction between elongation factor Tu and the ribosome

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7 January 2021

Improved methods for building protein models in electron density maps and the location of errors in these models

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Restrained refinement of the monoclinic form of yeast phenylalanine transfer RNA. Temperature factors and dynamics, coordinated waters, and base-pair propeller twist angles

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7 January 2021

10.1016/S0969-2126(96)00027-5

Identifiers

DOI

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26 September 2017

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