about
Crystal structure of Escherichia coli methionyl-tRNA synthetase highlights species-specific featuresStructure of crystalline D-Tyr-tRNA(Tyr) deacylase. A representative of a new class of tRNA-dependent hydrolasesThe large subunit of initiation factor aIF2 is a close structural homologue of elongation factors.Structure of an archaeal heterotrimeric initiation factor 2 reveals a nucleotide state between the GTP and the GDP statesA unique conformation of the anticodon stem-loop is associated with the capacity of tRNAfMet to initiate protein synthesisStructural bases for 16 S rRNA methylation catalyzed by ArmA and RmtB methyltransferasesStructure of the ternary initiation complex aIF2-GDPNP-methionylated initiator tRNAUnravelling the mechanism of non-ribosomal peptide synthesis by cyclodipeptide synthasesCdc123, a Cell Cycle Regulator Needed for eIF2 Assembly, Is an ATP-Grasp Protein with Unique FeaturesMitochondrial methionyl-tRNAfMet formyltransferase from Saccharomyces cerevisiae: gene disruption and tRNA substrate specificity.Cryo-EM study of start codon selection during archaeal translation initiationThe many routes of bacterial transfer RNAs after aminoacylation.Crystal structure of methionyl-tRNAfMet transformylase complexed with the initiator formyl-methionyl-tRNAfMet.Role of the 1-72 base pair in tRNAs for the activity of Escherichia coli peptidyl-tRNA hydrolase.Structure of a left-handed DNA G-quadruplex.Identification of a second GTP-bound magnesium ion in archaeal initiation factor 2.Roles of yeast eIF2α and eIF2β subunits in the binding of the initiator methionyl-tRNA.Capturing the mutational landscape of the beta-lactamase TEM-1.Discovery of Escherichia coli methionyl-tRNA synthetase mutants for efficient labeling of proteins with azidonorleucine in vivoEukaryotic and archaeal translation initiation factor 2: a heterotrimeric tRNA carrier.The structure of an E. coli tRNAfMet A1-U72 variant shows an unusual conformation of the A1-U72 base pair.Methionine as translation start signal: a review of the enzymes of the pathway in Escherichia coli.Crystallization and preliminary X-ray analysis of Escherichia coli peptidyl-tRNA hydrolase.Structural basis for tRNA-dependent amidotransferase function.Structural switch of the gamma subunit in an archaeal aIF2 alpha gamma heterodimer.Three-dimensional structure of methionyl-tRNA synthetase from Pyrococcus abyssi.Structural basis for partition of the cyclodipeptide synthases into two subfamilies.General structure/function properties of microbial methionyl-tRNA synthetases.Methionyl-tRNA synthetase needs an intact and mobile 332KMSKS336 motif in catalysis of methionyl adenylate formation.Interplay of Methionine tRNAs with Translation Elongation Factor Tu and Translation Initiation Factor 2 inEscherichia coliRole of aIF1 in Pyrococcus abyssi translation initiationStart Codon Recognition in Eukaryotic and Archaeal Translation Initiation: A Common Structural CoreCrystallization and preliminary X-ray analysis of Escherichia coli methionyl-tRNAMet(f) formyltransferase complexed with formyl-methionyl-tRNAMet(f)Receptor site for the 5'-phosphate of elongator tRNAs governs substrate selection by peptidyl-tRNA hydrolaseStructural basis of RNA-dependent recruitment of glutamine to the genetic codeProtection-based assays to measure aminoacyl-tRNA binding to translation initiation factorsStructure-function relationships of the intact aIF2alpha subunit from the archaeon Pyrococcus abyssitRNA binding properties of eukaryotic translation initiation factor 2 from Encephalitozoon cuniculiTranslation InitiationThe trimeric coiled-coil HSBP1 protein promotes WASH complex assembly at centrosomes
P50
Q27620716-A2FCA4EE-E948-4AC6-9DCE-173EBFD632ACQ27634982-593F9EC3-D955-48D5-B05A-3B51EBF1B5EBQ27638673-D9A65934-BB3A-4EDC-8245-B95F38B85774Q27649026-8A1B14C9-E283-4A93-902C-FF3A512252A3Q27651334-DFBF5FFF-69B7-4259-A936-12D0EDBCDFC1Q27654233-12A3581F-8E50-421D-AB44-9A9217F60BD7Q27678199-33E5969F-2B9D-4946-B4F1-5C2ECCCF92E8Q27695680-8F1D2EE5-6D6B-41FC-A610-BF53C3594BADQ27701649-173A3559-FF3A-4FEC-974E-8DA091238197Q27936520-DCC3049E-B674-4747-9FE7-B378F335FA2AQ30828138-EC12DD62-5B58-40F9-8585-321D428860C6Q33840738-206EE21B-C768-4488-98F8-E5F2A7F39058Q33890098-E2625972-4A25-42DF-BEA8-10469BFFE51DQ34998809-FD87B56B-CFC3-4C80-9B95-8A9097F43657Q35156943-D45E64E7-BFFD-4B06-B075-0807C9DC34DDQ35171556-AB0615D1-BA58-4092-8F32-078297C0DEB3Q36559289-BA3EB458-7DD7-4883-83D8-C01DFC163368Q37088726-4CB213EB-829A-409C-A1A1-A9EDD1C6B113Q37340804-D660741E-8E64-4932-B15B-D6BFA16265ADQ37629201-91F0986E-ED51-4826-9B4C-F1B0528756B6Q38988167-38B58BDE-4E0E-4553-A11A-09EE0716C19CQ40760044-23BC6536-A36B-43FC-BD2A-6728FB00BC26Q41113837-37B70855-E929-47F8-9112-201A68594955Q46745511-58DE9358-D93B-48A0-8E20-C4E179E743F0Q46890201-77098CF7-8284-4961-A1CF-185FFB90B581Q48018212-B0735FD7-DF51-4614-A81E-50A647438D35Q52673861-C0B6BC4A-4882-4F73-963C-C1EF96BE5A61Q54564880-A557878D-247B-462E-BAEC-5D4B653465B1Q54627061-0BD74B49-FA59-4DB8-B59E-B2DFC57D2FC6Q57990782-E818B325-4458-4393-8824-551354024F42Q59125509-725AA72F-2662-4796-96F1-FEB454A1C4F0Q64119701-A081DA78-5575-4FBC-9017-B0EF5E975744Q74629915-31F8E14A-81A5-44EC-A614-AEA01332A635Q77357808-A14E9BF5-5F95-4C78-A6F8-7A5FECAD733CQ79816008-B47BD1D1-D4FD-4FB2-A85B-07BBBFE15AA4Q81390816-896A7216-F3F7-4E13-9BFC-87384E1BA514Q81843281-FD292ADC-B819-4EF6-B8AC-C9DF025E46D5Q84991924-16A6BF2E-F9CC-4216-A9CE-CC74DF0223ADQ86404320-8E8988F7-A722-4602-A2B8-46EAE5585EF7Q88909342-D7BEA93E-8E06-4D22-9685-A3540D0C730C
P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Yves Mechulam
@ast
Yves Mechulam
@en
Yves Mechulam
@es
Yves Mechulam
@nl
type
label
Yves Mechulam
@ast
Yves Mechulam
@en
Yves Mechulam
@es
Yves Mechulam
@nl
prefLabel
Yves Mechulam
@ast
Yves Mechulam
@en
Yves Mechulam
@es
Yves Mechulam
@nl
P106
P31
P496
0000-0003-3586-3554