Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis - Wikidata - awgldk - TriplyDB

Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis

Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis

http://www.wikidata.org/entity/Q27653327

about

Elongation in translation as a dynamic interaction among the ribosome, tRNA, and elongation factors EF-G and EF-Tu Simultaneous characterization of cellular RNA structure and function with in-cell SHAPE-Seq The p7 protein of hepatitis C virus forms structurally plastic, minimalist ion channels The Crystal Structure of the Ribosome Bound to EF-Tu and Aminoacyl-tRNA Regulation of the Protein-Conducting Channel by a Bound Ribosome Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome at 5.5-A resolution The Mechanism for Activation of GTP Hydrolysis on the Ribosome Molecular dynamics of EF-G during translocation Structural insights into cognate versus near-cognate discrimination during decoding.Structure of the no-go mRNA decay complex Dom34-Hbs1 bound to a stalled 80S ribosome Structure and Dynamics of the Mammalian Ribosomal Pretranslocation Complex Structural basis of highly conserved ribosome recycling in eukaryotes and archaea EttA regulates translation by binding the ribosomal E site and restricting ribosome-tRNA dynamics Structure of the Acinetobacter baumannii Dithiol Oxidase DsbA Bound to Elongation Factor EF-Tu Reveals a Novel Protein Interaction Site Regulation of the Mammalian Elongation Cycle by Subunit Rolling: A Eukaryotic-Specific Ribosome Rearrangement Structure of EF-G-ribosome complex in a pretranslocation state Structure of the mammalian 80S initiation complex with initiation factor 5B on HCV-IRES RNA HflX is a ribosome-splitting factor rescuing stalled ribosomes under stress conditions Saccharomyces cerevisiae Ski7 Is a GTP-Binding Protein Adopting the Characteristic Conformation of Active Translational GTPases.The selenocysteine-specific elongation factor contains a novel and multi-functional domain Evolutionary optimization of speed and accuracy of decoding on the ribosome EM-fold: De novo folding of alpha-helical proteins guided by intermediate-resolution electron microscopy density maps.EM-fold: de novo atomic-detail protein structure determination from medium-resolution density maps.The role of L1 stalk-tRNA interaction in the ribosome elongation cycle Examinations of tRNA Range of Motion Using Simulations of Cryo-EM Microscopy and X-Ray Data.Trajectories of the ribosome as a Brownian nanomachine.Tracking fluctuation hotspots on the yeast ribosome through the elongation cycle CryoEM Structure Refinement by Integrating NMR Chemical Shifts with Molecular Dynamics Simulations.Discovery through the computational microscope.Properties of Escherichia coli EF-Tu mutants designed for fluorescence resonance energy transfer from tRNA molecules.The ribosome's energy landscape: Recent insights from computation Unified data resource for cryo-EM.Accommodation of aminoacyl-tRNA into the ribosome involves reversible excursions along multiple pathways.Stereochemical errors and their implications for molecular dynamics simulations.Intensity-based skeletonization of CryoEM gray-scale images using a true segmentation-free algorithm.Computational Methodologies for Real-Space Structural Refinement of Large Macromolecular Complexes.Cleavage of the sarcin-ricin loop of 23S rRNA differentially affects EF-G and EF-Tu binding Conformational sampling of aminoacyl-tRNA during selection on the bacterial ribosome.Consensus among flexible fitting approaches improves the interpretation of cryo-EM data.Single-particle reconstruction of biological macromolecules in electron microscopy--30 years.

P2860

Q24633187-5B646AB2-7671-4B83-B6F5-8A0836E4E3B1 Q27324428-42EBB2D2-63C6-4083-9D29-0A4A0852605C Q27329756-66E2B9E3-1ACE-4BED-8562-34E7D3CFF6F4 Q27657801-58121F2F-B01A-401F-A582-F2026748EFBA Q27658163-FD26296A-C751-4930-AF5B-5F2F48D65655 Q27665394-6118A0E7-E261-4615-B9FE-148FB3751850 Q27665613-7143A2B1-FAA0-4E7B-8989-F6B641220161 Q27667125-A587F13A-0C31-42E9-9FB7-C0A63168D03E Q27667183-CA105455-4D23-47AE-B845-9085ECCB2383 Q27668080-97657F22-F5AB-467A-8EF9-45BF413AD81F Q27675157-CEDF4CB2-04EE-4FF0-9FFF-CA2C3C989C7E Q27677430-107B5DFA-6FB8-405E-8C88-068A995868BA Q27681174-BBCEE2BC-CA58-4E77-8EFF-59D2333FCE62 Q27683945-9121D043-2929-4CE0-BF5A-B720BFFAC549 Q27684558-DE791240-A68E-475C-BD7F-5D7CFDA9A5A0 Q27685333-A370F8AF-5E52-4EF4-B909-6487DE3908A4 Q27694629-94DED21E-73A7-4D46-BCBD-1875F8883438 Q27702284-4A28793C-EAEA-4850-85EA-C30FB235120C Q27937196-A9CF6290-6975-4D6E-86D9-70C596E17E39 Q28591877-7B6F5D36-D225-425A-80D0-4DA7D4638156 Q28741198-F4B004CC-1E6E-46F2-8DB0-37DA32894267 Q30378954-42A16C9F-4DBD-4787-ABFB-2418D319FCEC Q30414109-7CA111E7-9D06-4A40-A3C8-CB6B9BF28B64 Q30497195-D5D32016-68EE-4BBB-98D5-58FF5546BEA8 Q30501206-C2AB6CEA-8005-46D2-A031-80D9495F836A Q30608405-29664D74-1530-43C8-9919-A4889FF5009A Q30847758-1860E009-3CAB-4516-BD0E-9476566E5DDE Q30854732-9AB21F29-56C7-4D7A-8F5C-CBB78956C38F Q33511109-F8C73712-16F5-464C-B501-ADF91601D583 Q33630645-EA09C977-7FE7-4810-8F64-B616F0AA5B20 Q33639675-B5F0C62C-9F49-442A-8590-C4B68BD2BFBD Q33708386-21DDDEF3-E7A9-4BC8-992F-07FE081619D3 Q33867466-2E84EAF6-0F80-4795-9D58-7B22501A06E8 Q33909428-02E084BB-74AC-4017-838C-842B86C04DAE Q33925302-E26400A9-F5E4-422C-B43E-72C2112C0822 Q33926329-11FE8B3B-7378-40B1-A077-670B311FD5FD Q33959452-4FBEC5B8-F92A-4D81-9D03-67B9AEFA0AFD Q34049310-D556D950-B8BD-4495-8A41-51F3067AC730 Q34054556-FF8208F9-518C-4D4E-93C9-FE6B91D4B3DA Q34089240-FA7DE113-FBE9-4EC8-A4AB-2D33DC12EB04

P2860

Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis

http://www.wikidata.org/entity/Q27653327

description

2009 nî lūn-bûn

@nan

2009 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis

@ast

Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis

@en

Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis

@nl

type

label

Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis

@ast

Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis

@en

Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis

@nl

prefLabel

Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis

@ast

Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis

@en

Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis

@nl

P1433

Q27653327-4F6B61B4-08B2-4F0C-84F8-C500395F3F15

P1476

Q27653327-355E571E-D2BA-42D7-8220-3918917BDE48

P2093

Q27653327-3C3BE28A-23B7-4640-8848-F83DCB5CDF1F

Q27653327-56844C62-8323-4965-A507-1F19A23DE04F

Q27653327-8E8D2871-A8AE-448C-943F-FE07ECCBF7C3

Q27653327-BC052DBC-EB8F-4051-AA9C-23F0397B8FA8

Q27653327-CE461C8E-4E67-489B-A7FB-FBB04A007161

Q27653327-D2270C90-38CF-491F-8F3E-785E834D1977

P2860

Q27653327-1222E010-FC52-4EEF-B825-075044BA8439

Q27653327-17C32361-D341-4D63-87B3-2B0CDD33D2D1

Q27653327-1C8E9278-36AD-4F74-94D2-78E37FD90979

Q27653327-282DF4BD-A67E-4B3D-83F8-9F7265473C24

Q27653327-2CA98D00-50BB-4F4C-813B-B7558D142300

Q27653327-3EDE3686-2F78-4CAC-8145-FDDAAB6B4816

Q27653327-4E08CDB0-B586-4C82-9BEF-60574F54BA64

Q27653327-564080ED-95CB-49BB-8876-DCAB03A936D5

Q27653327-622E3CF4-BE03-45E9-9CBA-11513A3F0F0C

Q27653327-6D8DDD53-FA45-4C99-BF65-F3527F2D4DD7

P304

Q27653327-D05F11AA-2171-4108-B6B2-4ABE89F59AC6

P31

Q27653327-5A02AD87-FD21-4BBE-A200-8EA883C7C8F7

P3181

Q27653327-B46DE203-423B-4635-BE82-8596990550E6

P356

Q27653327-72F80171-50BB-4250-BBDD-B8ACE7970E2F

P407

Q27653327-2E0C0A03-41C1-4E23-80FF-F1DDDD7E2D3B

P433

Q27653327-4342DD68-8A3F-4029-B2CD-4796D57EA6BB

P478

Q27653327-2661CA62-8ABD-43A8-8D63-8FAE959814F7

P50

Q27653327-5C07BBBF-0EE3-4C8A-AC8E-BEA0AFD577C1

Q27653327-7D1C45DD-3E71-4506-A2C8-38E6CE077267

Q27653327-A65FDDDF-2D54-4BA6-B2B1-E57E1CA1B313

Q27653327-AF04C441-6A0D-4DA7-98D4-A44950C55D76

Q27653327-EF78C049-DA34-43DD-A66C-8DB06B2BDD7F

P577

Q27653327-5260DD08-9919-4B46-95A1-148831CFC0BB

P5875

Q27653327-86D91EE1-D43B-48CB-A3A8-699C50954A1B

P698

Q27653327-19B2C923-340B-4DF7-89E7-D75243265B08

P932

Q27653327-C8D02649-276D-4649-A126-CC6FA4DD636C

P3181

P356

PNAS.0811370106

P1433

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

P1476

Ribosome-induced changes in elongation factor Tu conformation control GTP hydrolysis

@en

P2093

Jamie LeBarron

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

Jayati Sengupta

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

Leonardo G Trabuco

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

Robert A Grassucci

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

Tanvir R Shaikh

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

William T Baxter

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

P2860

Conformational change of elongation factor Tu (EF-Tu) induced by antibiotic binding. Crystal structure of the complex between EF-Tu.GDP and aurodox

Cryo-EM reveals an active role for aminoacyl-tRNA in the accommodation process

Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex

Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy

Visualization of the eEF2–80S Ribosome Transition-State Complex by Cryo-Electron Microscopy

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

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

Helix unwinding in the effector region of elongation factor EF-Tu-GDP

An alpha to beta conformational switch in EF-Tu

Structure of the GDP-Pi complex of Gly203-->Ala gialpha1: a mimic of the ternary product complex of galpha-catalyzed GTP hydrolysis

P304

1063-8

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

P31

scholarly article

P3181

4623603

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

P356

10.1073/PNAS.0811370106

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

P407

P433

4

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

P478

106

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

P50

Elizabeth Villa

Måns Ehrenberg

P577

2009-01-27T00:00:00Z

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

P5875

23719831

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

P698

19122150

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

P932

2613361

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