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Review: Translational GTPases

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/embj.201387465openalex-snapshot

GTP hydrolysis by EF‐G synchronizes tRNA movement on small and large ribosomal subunits

inferredcites →https://doi.org/10.1002/j.1460-2075.1995.tb07259.xopenalex-snapshot

Codon‐dependent conformational change of elongation factor Tu preceding GTP hydrolysis on the ribosome.

inferredcites →https://doi.org/10.1006/jmbi.1998.2387openalex-snapshot

Crystal Structure of Intact Elongation Factor EF-Tu from Escherichia coli in GDP Conformation at 2.05Å Resolution

inferredcites →https://doi.org/10.1006/jmbi.2001.5378openalex-snapshot

Classification and evolution of P-loop GTPases and related ATPases

inferredcites →https://doi.org/10.1016/0014-5793(91)80122-jopenalex-snapshot

Examination of elongation factor Tu for aluminum fluoride binding sites using fluorescence and 19F‐NMR methodologies

inferredcites →https://doi.org/10.1016/0014-5793(93)80097-eopenalex-snapshot

Divergent effects of fluoroaluminates on the peptide chain elongation factors EF‐Tu and EF‐G as members of the GTPase superfamily

inferredcites →https://doi.org/10.1016/0014-5793(95)00469-popenalex-snapshot

Relevance of histidine‐84 in the elongation factor Tu GTPase activity and in poly(Phe) synthesis: Its substitution by glutamine and alanine

inferredcites →https://doi.org/10.1016/0022-2860(74)85135-5openalex-snapshot

Advances in physical organic chemistry

inferredcites →https://doi.org/10.1016/0304-4173(78)90009-5openalex-snapshot

The role of guanosine 5′-triphosphate in polypeptide chain elongation

inferredcites →https://doi.org/10.1016/0959-440x(95)80015-8openalex-snapshot

Regulatory GTPases

inferredcites →https://doi.org/10.1016/0969-2126(93)90007-4openalex-snapshot

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

inferredcites →https://doi.org/10.1016/j.abb.2015.02.027openalex-snapshot

Modeling the mechanisms of biological GTP hydrolysis

inferredcites →https://doi.org/10.1016/j.bbapap.2008.08.003openalex-snapshot

Mechanism of the chemical step for the guanosine triphosphate (GTP) hydrolysis catalyzed by elongation factor Tu

inferredcites →https://doi.org/10.1016/j.cell.2005.04.015openalex-snapshot

Structural Basis for the Function of the Ribosomal L7/12 Stalk in Factor Binding and GTPase Activation

inferredcites →https://doi.org/10.1016/j.cell.2007.05.018openalex-snapshot

GEFs and GAPs: Critical Elements in the Control of Small G Proteins

inferredcites →https://doi.org/10.1016/j.cell.2014.11.049openalex-snapshot

Conformational Changes of Elongation Factor G on the Ribosome during tRNA Translocation

inferredcites →https://doi.org/10.1016/j.febslet.2005.07.016openalex-snapshot

Crystal structure of a mutant elongation factor G trapped with a GTP analogue

inferredcites →https://doi.org/10.1016/j.febslet.2012.06.030openalex-snapshot

The cation‐dependent G‐proteins: In a class of their own

inferredcites →https://doi.org/10.1016/j.jmb.2003.11.025openalex-snapshot

GTP-dependent Recognition of the Methionine Moiety on Initiator tRNA by Translation Factor eIF2

inferredcites →https://doi.org/10.1016/j.jmb.2004.06.007openalex-snapshot

GTP Hydrolysis Mechanism of Ras-like GTPases

inferredcites →https://doi.org/10.1016/j.jmb.2007.07.032openalex-snapshot

A Quantitative Kinetic Scheme for 70 S Translation Initiation Complex Formation

inferredcites →https://doi.org/10.1016/j.jmb.2010.04.038openalex-snapshot

Conformational Sampling of Aminoacyl-tRNA during Selection on the Bacterial Ribosome

inferredcites →https://doi.org/10.1016/j.jmb.2014.11.010openalex-snapshot

Movement of Elongation Factor G between Compact and Extended Conformations

inferredcites →https://doi.org/10.1016/j.jsb.2015.06.011openalex-snapshot

Structural outline of the detailed mechanism for elongation factor Ts-mediated guanine nucleotide exchange on elongation factor Tu

inferredcites →https://doi.org/10.1016/j.molcel.2005.12.018openalex-snapshot

A Uniform Response to Mismatches in Codon-Anticodon Complexes Ensures Ribosomal Fidelity

inferredcites →https://doi.org/10.1016/j.molcel.2007.01.014openalex-snapshot

Kinetically Competent Intermediates in the Translocation Step of Protein Synthesis

inferredcites →https://doi.org/10.1016/j.molcel.2008.04.010openalex-snapshot

The Kinetics of Ribosomal Peptidyl Transfer Revisited

inferredcites →https://doi.org/10.1016/s0021-9258(17)42947-4openalex-snapshot

Relative affinities of all Escherichia coli aminoacyl-tRNAs for elongation factor Tu-GTP.

inferredcites →https://doi.org/10.1016/s0021-9258(19)81087-6openalex-snapshot

Hydrolysis of GTP by elongation factor Tu can be induced by monovalent cations in the absence of other effectors.

inferredcites →https://doi.org/10.1016/s0022-2836(03)00947-1openalex-snapshot

Essential Role of Histidine 84 in Elongation Factor Tu for the Chemical Step of GTP Hydrolysis on the Ribosome

inferredcites →https://doi.org/10.1016/s0022-2836(66)80248-6openalex-snapshot

Ribonucleic acid composition of bacteria as a function of growth rate

inferredcites →https://doi.org/10.1016/s0092-8674(00)00181-1openalex-snapshot

X-Ray Structures of the Universal Translation Initiation Factor IF2/eIF5B

inferredcites →https://doi.org/10.1016/s0092-8674(01)00508-6openalex-snapshot

A Posttermination Ribosomal Complex Is the Guanine Nucleotide Exchange Factor for Peptide Release Factor RF3

inferredcites →https://doi.org/10.1016/s0960-9822(00)00025-7openalex-snapshot

Eukaryotic translation initiation factor 5 (eIF5) acts as a classical GTPase-activator protein

inferredcites →https://doi.org/10.1016/s0969-2126(96)00061-5openalex-snapshot

The structure of elongation factor G in complex with GDP: conformational flexibility and nucleotide exchange

inferredcites →https://doi.org/10.1016/s0969-2126(96)00122-0openalex-snapshot

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

inferredcites →https://doi.org/10.1016/s1097-2765(00)00122-2openalex-snapshot

Structural Basis for Nucleotide Exchange and Competition with tRNA in the Yeast Elongation Factor Complex eEF1A:eEF1Bα

inferredcites →https://doi.org/10.1016/s1097-2765(03)00230-2openalex-snapshot

An Elongation Factor G-Induced Ribosome Rearrangement Precedes tRNA-mRNA Translocation

inferredcites →https://doi.org/10.1016/s1097-2765(04)00005-xopenalex-snapshot

Kinetic Determinants of High-Fidelity tRNA Discrimination on the Ribosome

inferredcites →https://doi.org/10.1017/s0033583512000157openalex-snapshot

Why nature really chose phosphate

inferredcites →https://doi.org/10.1021/bi0017024openalex-snapshot

Ras Catalyzes GTP Hydrolysis by Shifting Negative Charges from γ- to β-Phosphate As Revealed by Time-Resolved FTIR Difference Spectroscopy

inferredcites →https://doi.org/10.1021/bi00216a008openalex-snapshot

Substitution of histidine-84 and the GTPase mechanism of elongation factor Tu

inferredcites →https://doi.org/10.1021/bi00324a023openalex-snapshot

Direct determination of the association constant between elongation factor Tu.cntdot.GTP and aminoacyl-tRNA using fluorescence

inferredcites →https://doi.org/10.1021/bi00527a017openalex-snapshot

Modulation by monovalent and divalent cations of the guanosine-5'-triphosphatase activity dependent on elongation factor Tu

inferredcites →https://doi.org/10.1021/bi015712wopenalex-snapshot

Kinetic Mechanism of Elongation Factor Ts-Catalyzed Nucleotide Exchange in Elongation Factor Tu

inferredcites →https://doi.org/10.1021/bi026301yopenalex-snapshot

GTPase Activation of Elongation Factors Tu and G on the Ribosome

inferredcites →https://doi.org/10.1021/bi0509806openalex-snapshot

What Are the Roles of Substrate-Assisted Catalysis and Proximity Effects in Peptide Bond Formation by the Ribosome?

inferredcites →https://doi.org/10.1021/bi061192zopenalex-snapshot

Delayed Release of Inorganic Phosphate from Elongation Factor Tu Following GTP Hydrolysis on the Ribosome

inferredcites →https://doi.org/10.1021/bi501373gopenalex-snapshot

The Conformation of a Catalytic Loop Is Central to GTPase Activity on the Ribosome

inferredcites →https://doi.org/10.1021/bi961118oopenalex-snapshot

Linear Free Energy Relationships in the Intrinsic and GTPase Activating Protein-Stimulated Guanosine 5‘-Triphosphate Hydrolysis of p21ras

inferredcites →https://doi.org/10.1021/bi961119gopenalex-snapshot

Mechanistic Analysis of the Observed Linear Free Energy Relationships in p21ras and Related Systems

inferredcites →https://doi.org/10.1021/bi992331yopenalex-snapshot

Intact Aminoacyl-tRNA Is Required To Trigger GTP Hydrolysis by Elongation Factor Tu on the Ribosome

inferredcites →https://doi.org/10.1038/349117a0openalex-snapshot

The GTPase superfamily: conserved structure and molecular mechanism

inferredcites →https://doi.org/10.1038/35002118openalex-snapshot

The joining of ribosomal subunits in eukaryotes requires eIF5B

inferredcites →https://doi.org/10.1038/365126a0openalex-snapshot

Crystal structure of active elongation factor Tu reveals major domain rearrangements

inferredcites →https://doi.org/10.1038/385037a0openalex-snapshot

Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome

inferredcites →https://doi.org/10.1038/emboj.2009.26openalex-snapshot

GTPase activation of elongation factor EF‐Tu by the ribosome during decoding

inferredcites →https://doi.org/10.1038/emboj.2010.229openalex-snapshot

Optimization of speed and accuracy of decoding in translation

inferredcites →https://doi.org/10.1038/emboj.2011.58openalex-snapshot

Structural insights into cognate versus near‐cognate discrimination during decoding

inferredcites →https://doi.org/10.1038/nature14275openalex-snapshot

Structure of the E. coli ribosome–EF-Tu complex at <3 Å resolution by Cs-corrected cryo-EM

inferredcites →https://doi.org/10.1038/ncomms2373openalex-snapshot

Evolution of the protein stoichiometry in the L12 stalk of bacterial and organellar ribosomes

inferredcites →https://doi.org/10.1038/ncomms2741openalex-snapshot

Energetics of activation of GTP hydrolysis on the ribosome

inferredcites →https://doi.org/10.1038/ncomms8442openalex-snapshot

Fluctuations between multiple EF-G-induced chimeric tRNA states during translocation on the ribosome

inferredcites →https://doi.org/10.1038/nsb0195-36openalex-snapshot

Substrate-assisted catalysis as a mechanism for GTP hydrolysis of p21ras and other GTP-binding proteins

inferredcites →https://doi.org/10.1038/nsb0794-476openalex-snapshot

Why have mutagenesis studies not located the general base in ras p21

inferredcites →https://doi.org/10.1038/nsb0897-650openalex-snapshot

Crystal structure of the EF-Tu˙EF-Ts complex from Thermus thermophilus

inferredcites →https://doi.org/10.1038/nsmb.2645openalex-snapshot

Structure of EF-G–ribosome complex in a pretranslocation state

inferredcites →https://doi.org/10.1038/nsmb.2859openalex-snapshot

Structure of the mammalian 80S initiation complex with initiation factor 5B on HCV-IRES RNA

inferredcites →https://doi.org/10.1038/nsmb831openalex-snapshot

tRNA selection and kinetic proofreading in translation

inferredcites →https://doi.org/10.1038/sj.emboj.7600505openalex-snapshot

Selenocysteine tRNA‐specific elongation factor SelB is a structural chimaera of elongation and initiation factors

inferredcites →https://doi.org/10.1038/sj.emboj.7601171openalex-snapshot

Dimerisation‐dependent GTPase reaction of MnmE: how potassium acts as GTPase‐activating element

inferredcites →https://doi.org/10.1038/srep15817openalex-snapshot

Exceptionally large entropy contributions enable the high rates of GTP hydrolysis on the ribosome

inferredcites →https://doi.org/10.1073/pnas.0606099103openalex-snapshot

Role and timing of GTP binding and hydrolysis during EF-G-dependent tRNA translocation on the ribosome

inferredcites →https://doi.org/10.1073/pnas.1105714108openalex-snapshot

Converting structural information into an allosteric-energy-based picture for elongation factor Tu activation by the ribosome

inferredcites →https://doi.org/10.1073/pnas.1309360110openalex-snapshot

Initiation factor 2 crystal structure reveals a different domain organization from eukaryotic initiation factor 5B and mechanism among translational GTPases

inferredcites →https://doi.org/10.1073/pnas.1319854110openalex-snapshot

Quantitative exploration of the molecular origin of the activation of GTPase

inferredcites →https://doi.org/10.1073/pnas.1412676111openalex-snapshot

Ribosome-induced tuning of GTP hydrolysis by a translational GTPase

inferredcites →https://doi.org/10.1073/pnas.1505231112openalex-snapshot

Role of a ribosomal RNA phosphate oxygen during the EF-G–triggered GTP hydrolysis

inferredcites →https://doi.org/10.1073/pnas.1506823112openalex-snapshot

Accuracy of initial codon selection by aminoacyl-tRNAs on the mRNA-programmed bacterial ribosome

inferredcites →https://doi.org/10.1073/pnas.72.12.4780openalex-snapshot

Content of elongation factor Tu in Escherichia coli.

inferredcites →https://doi.org/10.1073/pnas.93.16.8160openalex-snapshot

Ras-catalyzed hydrolysis of GTP: a new perspective from model studies.

inferredcites →https://doi.org/10.1074/jbc.271.2.646openalex-snapshot

Initial Binding of the Elongation Factor Tu·GTP·Aminoacyl-tRNA Complex Preceding Codon Recognition on the Ribosome

inferredcites →https://doi.org/10.1074/jbc.274.10.6074openalex-snapshot

In Vitro Study of Two Dominant Inhibitory GTPase Mutants of Escherichia coli Translation Initiation Factor IF2

inferredcites →https://doi.org/10.1074/jbc.275.2.890openalex-snapshot

Stimulation of the GTPase Activity of Translation Elongation Factor G by Ribosomal Protein L7/12

inferredcites →https://doi.org/10.1074/jbc.m110.210021openalex-snapshot

Distortion of tRNA upon Near-cognate Codon Recognition on the Ribosome

inferredcites →https://doi.org/10.1074/jbc.m707245200openalex-snapshot

Kinetics of the Interactions between Yeast Elongation Factors 1A and 1Bα, Guanine Nucleotides, and Aminoacyl-tRNA

inferredcites →https://doi.org/10.1080/08927022.2014.895000openalex-snapshot

Overview of simulation studies on the enzymatic activity and conformational dynamics of the GTPase Ras

inferredcites →https://doi.org/10.1093/emboj/17.24.7490openalex-snapshot

Complete kinetic mechanism of elongation factor Tu‐dependent binding of aminoacyl‐tRNA to the A site of the E.coli ribosome

inferredcites →https://doi.org/10.1093/emboj/18.13.3800openalex-snapshot

Induced fit in initial selection and proofreading of aminoacyl‐tRNA on the ribosome

inferredcites →https://doi.org/10.1093/emboj/19.9.2127openalex-snapshot

Late events of translation initiation in bacteria: a kinetic analysis

inferredcites →https://doi.org/10.1093/emboj/cdf326openalex-snapshot

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

inferredcites →https://doi.org/10.1093/emboj/cdg525openalex-snapshot

The roles of initiation factor 2 and guanosine triphosphate in initiation of protein synthesis

inferredcites →https://doi.org/10.1093/nar/gkt1095openalex-snapshot

Timing of GTP binding and hydrolysis by translation termination factor RF3

inferredcites →https://doi.org/10.1093/nar/gkv053openalex-snapshot

Identification of a second GTP-bound magnesium ion in archaeal initiation factor 2

inferredcites →https://doi.org/10.1093/nar/gkv856openalex-snapshot

EF-Tu dynamics during pre-translocation complex formation: EF-Tu·GDP exits the ribosome via two different pathways

inferredcites →https://doi.org/10.1093/nar/gkv869openalex-snapshot

Directional transition from initiation to elongation in bacterial translation

inferredcites →https://doi.org/10.1098/rstb.2011.0138openalex-snapshot

Evolutionary optimization of speed and accuracy of decoding on the ribosome

inferredcites →https://doi.org/10.1101/gad.1255704openalex-snapshot

Release of initiation factors from 48S complexes during ribosomal subunit joining and the link between establishment of codon-anticodon base-pairing and hydrolysis of eIF2-bound GTP

inferredcites →https://doi.org/10.1111/j.1365-2958.1994.tb00309.xopenalex-snapshot

In vivo study of engineered G‐domain mutants of Escherichia coli translation initiation factor IF2

inferredcites →https://doi.org/10.1111/j.1432-1033.1978.tb12560.xopenalex-snapshot

Modification of Elongation‐Factor‐Tu · Guanine‐Nucleotide Interaction by Kirromycin

inferredcites →https://doi.org/10.1111/j.1432-1033.1990.tb19228.xopenalex-snapshot

Fluoroaluminates do not affect the guanine‐nucleotide binding centre of the peptide chain elongation factor EF‐Tu

inferredcites →https://doi.org/10.1111/j.1432-1033.1995.0596j.xopenalex-snapshot

Site‐Directed Mutagenesis of Thermus thermophilus Elongation Factor Tu

inferredcites →https://doi.org/10.1111/j.1432-1033.1995.tb20503.xopenalex-snapshot

Site-Directed Mutagenesis of Thermus thermophilus Elongation Factor Tu. Replacement of His85, Asp81 and Arg300

inferredcites →https://doi.org/10.1126/science.1060612openalex-snapshot

Recognition of Cognate Transfer RNA by the 30 S Ribosomal Subunit

inferredcites →https://doi.org/10.1126/science.1062023openalex-snapshot

The Guanine Nucleotide-Binding Switch in Three Dimensions

inferredcites →https://doi.org/10.1126/science.1111408openalex-snapshot

An Active Role for tRNA in Decoding Beyond Codon:Anticodon Pairing

inferredcites →https://doi.org/10.1126/science.1179700openalex-snapshot

The Crystal Structure of the Ribosome Bound to EF-Tu and Aminoacyl-tRNA

inferredcites →https://doi.org/10.1126/science.1194460openalex-snapshot

The Mechanism for Activation of GTP Hydrolysis on the Ribosome

inferredcites →https://doi.org/10.1126/science.1202472openalex-snapshot

Comment on “The Mechanism for Activation of GTP Hydrolysis on the Ribosome”

inferredcites →https://doi.org/10.1126/science.1202532openalex-snapshot

Response to Comment on “The Mechanism for Activation of GTP Hydrolysis on the Ribosome”

inferredcites →https://doi.org/10.1126/science.1235490openalex-snapshot

Elongation Factor G Bound to the Ribosome in an Intermediate State of Translocation

inferredcites →https://doi.org/10.1126/science.1235970openalex-snapshot

Control of Ribosomal Subunit Rotation by Elongation Factor G

inferredcites →https://doi.org/10.1126/science.1236086openalex-snapshot

Crystal Structures of EF-G–Ribosome Complexes Trapped in Intermediate States of Translocation

inferredcites →https://doi.org/10.1126/science.270.5241.1464openalex-snapshot

Crystal Structure of the Ternary Complex of Phe-tRNA Phe , EF-Tu, and a GTP Analog

inferredcites →https://doi.org/10.1126/science.277.5324.333openalex-snapshot

The Ras-RasGAP Complex: Structural Basis for GTPase Activation and Its Loss in Oncogenic Ras Mutants

inferredcites →https://doi.org/10.1126/science.8430333openalex-snapshot

Probing the Structure and Mechanism of Ras Protein with an Expanded Genetic Code

inferredcites →https://doi.org/10.1146/annurev-biochem-060409-092741openalex-snapshot

Biological Phosphoryl-Transfer Reactions: Understanding Mechanism and Catalysis

inferredcites →https://doi.org/10.1146/annurev-biochem-062708-134043openalex-snapshot

Structure-Function Relationships of the G Domain, a Canonical Switch Motif

inferredcites →https://doi.org/10.1146/annurev-biochem-113009-092313openalex-snapshot

Structural Basis of the Translational Elongation Cycle

inferredcites →https://doi.org/10.1152/physrev.00003.2012openalex-snapshot

Regulation of Small GTPases by GEFs, GAPs, and GDIs

inferredcites →https://doi.org/10.1186/s12864-015-1289-7openalex-snapshot

The evolutionary and functional diversity of classical and lesser-known cytoplasmic and organellar translational GTPases across the tree of life

inferredcites →https://doi.org/10.1261/rna.031187.111openalex-snapshot

Crystal structure of release factor RF3 trapped in the GTP state on a rotated conformation of the ribosome

inferredcites →https://doi.org/10.1261/rna.036038.112openalex-snapshot

tRNA residues evolved to promote translational accuracy

inferredcites →https://doi.org/10.1261/rna.040097.113openalex-snapshot

Mechanism of activation of elongation factor Tu by ribosome: Catalytic histidine activates GTP by protonation

inferredcites →https://doi.org/10.1261/rna.042523.113openalex-snapshot

RF3:GTP promotes rapid dissociation of the class 1 termination factor

inferredcites →https://doi.org/10.1261/rna.2228510openalex-snapshot

Missense suppressor mutations in 16S rRNA reveal the importance of helices h8 and h14 in aminoacyl-tRNA selection

inferredcites →https://doi.org/10.1371/journal.pcbi.1003909openalex-snapshot

Deducing the Kinetics of Protein Synthesis In Vivo from the Transition Rates Measured In Vitro

inferredcites →https://doi.org/10.15252/embj.201488517openalex-snapshot

A monovalent cation acts as structural and catalytic cofactor in translational GTPases

inferredcites →https://doi.org/10.3390/ijms16059866openalex-snapshot

Structural Insights into tRNA Dynamics on the Ribosome

inferredcites →https://doi.org/10.4161/trla.24315openalex-snapshot

Dual use of GTP hydrolysis by elongation factor G on the ribosome

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Asymmetric inheritance of cytoophidia could contribute to determine cell fate and plasticity

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GLOBAL AND TARGETED PROFILING OF GTP‐BINDING PROTEINS IN BIOLOGICAL SAMPLES BY MASS SPECTROMETRY

inferred← citeshttps://doi.org/10.1007/978-1-0716-1975-9_12openalex-snapshot

Fluorescence Intensity-Based eIF2B’s Guanine Nucleotide-Exchange Factor Activity Assay

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Emw1/TTC27 is a chaperone required for folding of the eukaryotic elongation factor 2

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1H, 13C, and 15N backbone and methyl group resonance assignments of ricin toxin A subunit

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inferred← citeshttps://doi.org/10.1016/b978-0-12-822563-9.00166-9openalex-snapshot

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The natural bicyclic hexapeptide RA-VII is a novel inhibitor of the eukaryotic translocase eEF2

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Bacterial GTPases as druggable targets to tackle antimicrobial resistance

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Structural insights into the Switching Off of the Interaction between the Archaeal Ribosomal Stalk and aEF1A by Nucleotide Exchange Factor aEF1B

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Compartmentalization and regulation of GTP in control of cellular phenotypes

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The promiscuous ribosomal P-stalk: a new functional portrait

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The space between notes: emerging roles for translationally silent ribosomes

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Targeted Quantitative Profiling of GTP-Binding Proteins in Cancer Cells Using Isotope-Coded GTP Probes

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The Biochemical Landscape of Riboswitch Ligands

inferred← citeshttps://doi.org/10.1021/acs.biochem.7b00591openalex-snapshot

The Conformational Change in Elongation Factor Tu Involves Separation of Its Domains

inferred← citeshttps://doi.org/10.1021/acs.jpcb.2c05859openalex-snapshot

Sarcin/Ricin Domain RNA Retains Its Structure Better Than A-RNA in Adaptively Biased Molecular Dynamics Simulations

inferred← citeshttps://doi.org/10.1021/acschembio.6c00228openalex-snapshot

Carbene Footprinting and Mass Spectrometry Captures Global Conformational Changes in Elongation Factor-Tu Induced by Antibiotic Binding

inferred← citeshttps://doi.org/10.1021/jacs.9b01522openalex-snapshot

Elongation Factor Tu’s Nucleotide Binding Is Governed by a Thermodynamic Landscape Unique among Bacterial Translation Factors

inferred← citeshttps://doi.org/10.1038/nature20560openalex-snapshot

The pathway to GTPase activation of elongation factor SelB on the ribosome

inferred← citeshttps://doi.org/10.1038/nature22397openalex-snapshot

Ensemble cryo-EM elucidates the mechanism of translation fidelity

inferred← citeshttps://doi.org/10.1038/s41467-018-05465-1openalex-snapshot

Visualization of translation termination intermediates trapped by the Apidaecin 137 peptide during RF3-mediated recycling of RF1

inferred← citeshttps://doi.org/10.1038/s41467-021-27160-4openalex-snapshot

Functionally distinct roles for eEF2K in the control of ribosome availability and p-body abundance

inferred← citeshttps://doi.org/10.1038/s41467-025-61398-6openalex-snapshot

Arrest Peptide Profiling resolves co-translational folding pathways and chaperone interactions in vivo

inferred← citeshttps://doi.org/10.1038/s41580-025-00914-4openalex-snapshot

Regulation of RNA-binding proteins by small biomolecules

inferred← citeshttps://doi.org/10.1073/pnas.1610917113openalex-snapshot

Two proofreading steps amplify the accuracy of genetic code translation

inferred← citeshttps://doi.org/10.1073/pnas.1920013117openalex-snapshot

The alarmones (p)ppGpp directly regulate translation initiation during entry into quiescence

inferred← citeshttps://doi.org/10.1073/pnas.2415807122openalex-snapshot

Structure of a Gcn2 dimer in complex with the large 60S ribosomal subunit

inferred← citeshttps://doi.org/10.1074/jbc.m116.761809openalex-snapshot

Structural and biochemical analysis of Escherichia coli ObgE, a central regulator of bacterial persistence

inferred← citeshttps://doi.org/10.1074/jbc.rev120.012742openalex-snapshot

Translational regulation of environmental adaptation in bacteria

inferred← citeshttps://doi.org/10.1080/15476286.2019.1670598openalex-snapshot

Developmental changes of rRNA ribose methylations in the mouse

inferred← citeshttps://doi.org/10.1080/21541264.2021.1927652openalex-snapshot

Evolution of the genetic code

inferred← citeshttps://doi.org/10.1091/mbc.e20-07-0457openalex-snapshot

MRX8, the conserved mitochondrial YihA GTPase family member, is required for de novo Cox1 synthesis at suboptimal temperatures in Saccharomyces cerevisiae

inferred← citeshttps://doi.org/10.1093/abbs/gmy164openalex-snapshot

Biophysical characterization and ligand-binding properties of the elongation factor Tu from

inferred← citeshttps://doi.org/10.1093/bbb/zbae201openalex-snapshot

Prokaryotic ATP-binding cassette type F proteins in overcoming ribosomal stalling: mechanisms, evolution, and perspective for applications in bio-manufacturing

inferred← citeshttps://doi.org/10.1093/femsre/fuad044openalex-snapshot

Giving a signal: how protein phosphorylation helps Bacillus navigate through different life stages

inferred← citeshttps://doi.org/10.1093/nar/gkab260openalex-snapshot

Estimation of peptide elongation times from ribosome profiling spectra

inferred← citeshttps://doi.org/10.1093/nar/gkac1162openalex-snapshot

Salmonella antibacterial Rhs polymorphic toxin inhibits translation through ADP-ribosylation of EF-Tu P-loop

inferred← citeshttps://doi.org/10.1093/nar/gkae556openalex-snapshot

Resolution of ribosomal stalling by EF-P and ABCF ATPases YfmR and YkpA/YbiT

inferred← citeshttps://doi.org/10.1093/nar/gkag352openalex-snapshot

How interdiction of inositol pyrophosphate catabolism perturbs the fission yeast response to phosphate starvation

inferred← citeshttps://doi.org/10.1093/nar/gky346openalex-snapshot

Cryo-EM shows stages of initial codon selection on the ribosome by aa-tRNA in ternary complex with GTP and the GTPase-deficient EF-TuH84A

inferred← citeshttps://doi.org/10.1093/nar/gkz296openalex-snapshot

Two classes of EF1-family translational GTPases encoded by giant viruses

inferred← citeshttps://doi.org/10.1093/nar/gkz600openalex-snapshot

A role for the Saccharomyces cerevisiae ABCF protein New1 in translation termination/recycling

inferred← citeshttps://doi.org/10.1098/rstb.2016.0182openalex-snapshot

Ribosome dynamics during decoding

inferred← citeshttps://doi.org/10.1101/2023.09.01.555749openalex-snapshot

AP profiling resolves co-translational folding pathway and chaperone interactions in vivo

inferred← citeshttps://doi.org/10.1101/2024.01.25.577322openalex-snapshot

Resolution of ribosomal stalling by ABCF ATPases YfmR and YkpA/YbiT

inferred← citeshttps://doi.org/10.1101/2025.02.05.636767openalex-snapshot

The Translation Termination Factor eRF3 Interacts Sequentially with eRF1 and ABCE1 on the Ribosome

inferred← citeshttps://doi.org/10.1101/2025.06.05.657321openalex-snapshot

SURFS and AlphaFold Reveal Ribosome Footprint Shift Caused by EF-Tu D81 Mutation

inferred← citeshttps://doi.org/10.1101/2025.10.13.682107openalex-snapshot

Oxidative stress sensing by the translation elongation machinery promotes production of detoxifying selenoproteins

inferred← citeshttps://doi.org/10.1101/331249openalex-snapshot

Nucleus- and plastid-targeted annexin 5 promotes reproductive development in Arabidopsis and is essential for pollen and embryo formation

inferred← citeshttps://doi.org/10.1101/638064openalex-snapshot

A role for the Saccharomyces cerevisiae ABCF protein New1 during translation termination

inferred← citeshttps://doi.org/10.1101/872341openalex-snapshot

A conserved translation factor is required for optimal synthesis of a membrane protein family in mycobacteria

inferred← citeshttps://doi.org/10.1101/cshperspect.a032656openalex-snapshot

Translation Termination and Ribosome Recycling in Eukaryotes

inferred← citeshttps://doi.org/10.1101/gad.314724.118openalex-snapshot

Functions of unconventional mammalian translational GTPases GTPBP1 and GTPBP2

inferred← citeshttps://doi.org/10.1111/boc.70005openalex-snapshot

Actin Binding to the BAR Domain and Arf GAP Activity of ASAP1 Coordinately Control Actin Stress Fibers and Focal Adhesions

inferred← citeshttps://doi.org/10.1111/febs.14067openalex-snapshot

Ribosomal protein L7/L12 is required for GTP ase translation factors EF ‐G, RF 3, and IF 2 to bind in their GTP state to 70S ribosomes

inferred← citeshttps://doi.org/10.1111/gtc.12942openalex-snapshot

The structure–function analysis of Obg‐like GTPase proteins along the evolutionary tree from bacteria to humans

inferred← citeshttps://doi.org/10.1126/science.ads8728openalex-snapshot

GCN1 couples GCN2 to ribosomal state to initiate amino acid response pathway signaling

inferred← citeshttps://doi.org/10.1128/mcb.00060-17openalex-snapshot

Multiplication of Ribosomal P-Stalk Proteins Contributes to the Fidelity of Translation

inferred← citeshttps://doi.org/10.1128/mcb.00653-16openalex-snapshot

Taking a Step Back from Back-Translocation: an Integrative View of LepA/EF4's Cellular Function

inferred← citeshttps://doi.org/10.1128/msphere.00713-25openalex-snapshot

An apicoplast-localized GTPase is essential for Toxoplasma gondii survival

inferred← citeshttps://doi.org/10.1134/s0006297920110103openalex-snapshot

Peculiarities in Activation of Hydrolytic Activity of Elongation Factors

inferred← citeshttps://doi.org/10.1146/annurev-biophys-101922-072452openalex-snapshot

Decoding and Recoding of mRNA Sequences by the Ribosome

inferred← citeshttps://doi.org/10.1155/2019/9264217openalex-snapshot

Immunogenic Evaluation of Ribosomal P-Protein Antigen P0, P1, and P2 and Pentameric Protein Complex P0-(P1-P2)2ofPlasmodium falciparumin a Mouse Model

inferred← citeshttps://doi.org/10.1186/s12870-018-1405-3openalex-snapshot

Nucleus- and plastid-targeted annexin 5 promotes reproductive development in Arabidopsis and is essential for pollen and embryo formation

inferred← citeshttps://doi.org/10.1186/s13062-018-0217-6openalex-snapshot

Modeling protein folding in vivo

inferred← citeshttps://doi.org/10.1261/rna.080559.125openalex-snapshot

Depurination of sarcin/ricin loop 25S rRNA is signaled through the small ribosomal subunit during translation

inferred← citeshttps://doi.org/10.12688/f1000research.28175.1openalex-snapshot

Energy-dependent protein folding: modeling how a protein folding machine may work

inferred← citeshttps://doi.org/10.1515/hsz-2016-0314openalex-snapshot

Common mechanisms of catalysis in small and heterotrimeric GTPases and their respective GAPs

inferred← citeshttps://doi.org/10.1515/hsz-2019-0313openalex-snapshot

Converting GTP hydrolysis into motion: versatile translational elongation factor G

inferred← citeshttps://doi.org/10.1515/hsz-2023-0142openalex-snapshot

The many faces of ribosome translocation along the mRNA: reading frame maintenance, ribosome frameshifting and translational bypassing

inferred← citeshttps://doi.org/10.1515/hsz-2025-0227openalex-snapshot

Mechanistic insights into Ras-catalyzed GTP hydrolysis: conformational dynamics, catalytic mechanisms, and emerging therapeutic strategies

inferred← citeshttps://doi.org/10.22533/at.ed.0622119109openalex-snapshot

GESTÃO HOSPITALAR EM TEMPOS DE PANDEMIA: UM RELATO DE EXPERIÊNCIA

inferred← citeshttps://doi.org/10.25710/5hm5-3v14openalex-snapshot

Intermolecular interactions that lead to the activation and inhibition of ribosome-dependent GTPases

inferred← citeshttps://doi.org/10.3389/fmolb.2023.1175889openalex-snapshot

Novel rRNA transcriptional activity of NhaR revealed by its growth recovery for the bipA-deleted Escherichia coli at low temperature

inferred← citeshttps://doi.org/10.3389/fvets.2021.795906openalex-snapshot

Identification and Characterization of P0 Protein as a Vaccine Candidate Against Babesia divergens, Blood Parasite of Veterinary and Zoonotic Importance

inferred← citeshttps://doi.org/10.3390/antiox9090818openalex-snapshot

Mitochondrial Oxidative and Nitrosative Stress and Alzheimer Disease

inferred← citeshttps://doi.org/10.3390/biology10111171openalex-snapshot

Molecular Effects of Elongation Factor Ts and Trigger Factor on the Unfolding and Aggregation of Elongation Factor Tu Induced by the Prokaryotic Molecular Chaperone Hsp33

inferred← citeshttps://doi.org/10.3390/biology11081246openalex-snapshot

Mutational Analyses of the Cysteine-Rich Domain of Yvh1, a Protein Required for Translational Competency in Yeast

inferred← citeshttps://doi.org/10.3390/cells8111313openalex-snapshot

The Impact of the Stringent Response on TRAFAC GTPases and Prokaryotic Ribosome Assembly

inferred← citeshttps://doi.org/10.3390/ijms20010040openalex-snapshot

Ribosome Structure, Function, and Early Evolution

inferred← citeshttps://doi.org/10.3390/molecules29092058openalex-snapshot

The Structural and Molecular Mechanisms of Mycobacterium tuberculosis Translational Elongation Factor Proteins

inferred← citeshttps://doi.org/10.3390/toxins11050241openalex-snapshot

How Ricin Damages the Ribosome

inferred← citeshttps://doi.org/10.3390/toxins16040192openalex-snapshot

Antifungal Activity of Ribosome-Inactivating Proteins

inferred← citeshttps://doi.org/10.3390/vaccines12101116openalex-snapshot

Toxicity and Efficacy Evaluation of Soluble Recombinant Ricin Vaccine

inferred← citeshttps://doi.org/10.34133/csbj.0167openalex-snapshot

D81 Mutants Reveal Hidden EF-Tu Diversity while Natural Sequences Preserve Aspartate

inferred← citeshttps://doi.org/10.53846/goediss-10187openalex-snapshot

Characterisation of human ribosome assembly factors

inferred← citeshttps://doi.org/10.53846/goediss-8128openalex-snapshot

Recoding of bacteriophage T4 gene 60 mRNA by programmed translational bypassing

inferred← citeshttps://doi.org/10.53846/goediss-9493openalex-snapshot

Ribosome dynamics during spontaneous frameshifting

inferred← citeshttps://doi.org/10.53846/goediss-9786openalex-snapshot

Cotranslational folding of HemK C-terminal domain

inferred← citeshttps://doi.org/10.53846/goediss-9933openalex-snapshot

Release of a Natural mRNA During Recycling of the Prokaryotic Ribosome

inferred← citeshttps://doi.org/10.56083/rcv4n5-155openalex-snapshot

A TRIVIALIDADE E O MAU USO DOS ANTIBIÓTICOS: DESENVOLVIMENTO DE SUPERBACTÉRIAS E OUTRAS REPERCUSSÕES

inferred← citeshttps://doi.org/10.5772/intechopen.73955openalex-snapshot

Osteogenesis and Bone Regeneration

inferred← citeshttps://doi.org/10.5772/intechopen.82451openalex-snapshot

Traditional Chinese Medicine Therapy for Targeting Osteoblastogenesis

inferred← citeshttps://doi.org/10.70675/187084d3z20b9z4c17zb93cz65a84ecab4f7openalex-snapshot

How do the metabolites, GTP and (p)ppGpp, simultaneously control the occurrence of translational errors and resource allocation in bacteria?

inferred← citeshttps://doi.org/10.7554/elife.50807openalex-snapshot

The NTP generating activity of pyruvate kinase II is critical for apicoplast maintenance in Plasmodium falciparum

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