tRNA aminoacylation by arginyl-tRNA synthetase: induced conformations during substrates binding - Wikidata - awgldk - TriplyDB

tRNA aminoacylation by arginyl-tRNA synthetase: induced conformations during substrates binding

tRNA aminoacylation by arginyl-tRNA synthetase: induced conformations during substrates binding

http://www.wikidata.org/entity/Q27627790

about

A single residue in leucyl-tRNA synthetase affecting amino acid specificity and tRNA aminoacylation Tools for the automatic identification and classification of RNA base pairs Human tryptophanyl-tRNA synthetase is switched to a tRNA-dependent mode for tryptophan activation by mutations at V85 and I311 Predicting functional sites with an automated algorithm suitable for heterogeneous datasets MD Simulations of tRNA and Aminoacyl-tRNA Synthetases: Dynamics, Folding, Binding, and Allostery Structural and mutational studies of the recognition of the arginine tRNA-specific major identity element, A20, by arginyl-tRNA synthetase Structural origins of amino acid selection without editing by cysteinyl-tRNA synthetase Class I tyrosyl-tRNA synthetase has a class II mode of cognate tRNA recognition ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding Mechanism of molecular interactions for tRNA(Val) recognition by valyl-tRNA synthetase.Crystal Structure of Tryptophanyl-tRNA Synthetase Complexed with Adenosine-5′ Tetraphosphate: Evidence for Distributed Use of Catalytic Binding Energy in Amino Acid Activation by Class I Aminoacyl-tRNA Synthetases DNA mimicry by a high-affinity anti-NF- B RNA aptamer Modeling of tRNA-assisted mechanism of Arg activation based on a structure of Arg-tRNA synthetase, tRNA, and an ATP analog (ANP)Tertiary structure checkpoint at anticodon loop modification in tRNA functional maturation Structural dynamics of the aminoacylation and proofreading functional cycle of bacterial leucyl-tRNA synthetase Crystal structure of E. coli arginyl-tRNA synthetase and ligand binding studies revealed key residues in arginine recognition A novel crystal form of pyrrolysyl-tRNA synthetase reveals the pre- and post-aminoacyl-tRNA synthesis conformational states of the adenylate and aminoacyl moieties and an asparagine residue in the catalytic site The crystal structure of arginyl-tRNA synthetase from Homo sapiens Aminoacylation and conformational properties of yeast mitochondrial tRNA mutants with respiratory deficiency.Identification of functional similarities between proteins using directed evolution.Two distinct domains of the beta subunit of Aquifex aeolicus leucyl-tRNA synthetase are involved in tRNA binding as revealed by a three-hybrid selection.Crystal structures of apo wild-type M. jannaschii tyrosyl-tRNA synthetase (TyrRS) and an engineered TyrRS specific for O-methyl-L-tyrosine.Conformational change of Escherichia coli initiator methionyl-tRNA(fMet) upon binding to methionyl-tRNA formyl transferase.Recognizing the D-loop of transfer RNAs.Modulation of tRNAAla identity by inorganic pyrophosphatase.Hemin binds to human cytoplasmic arginyl-tRNA synthetase and inhibits its catalytic activity An archaeal tRNA-synthetase complex that enhances aminoacylation under extreme conditions.Structural basis for amino acid and tRNA recognition by class I aminoacyl-tRNA synthetases.A yeast knockout strain to discriminate between active and inactive tRNA molecules.Exit strategies for charged tRNA from GluRS The mechanism of L-canavanine cytotoxicity: arginyl tRNA synthetase as a novel target for anticancer drug discovery.MIST, a Novel Approach to Reveal Hidden Substrate Specificity in Aminoacyl-tRNA Synthetases.Predicting helical coaxial stacking in RNA multibranch loops Survival from hypoxia in C. elegans by inactivation of aminoacyl-tRNA synthetases.Evaluating and learning from RNA pseudotorsional space: quantitative validation of a reduced representation for RNA structure The Escherichia coli argU10(Ts) phenotype is caused by a reduction in the cellular level of the argU tRNA for the rare codons AGA and AGG.Experimental and computational determination of tRNA dynamics.Emergence and evolution.The Enzymatic Paradox of Yeast Arginyl-tRNA Synthetase: Exclusive Arginine Transfer Controlled by a Flexible Mechanism of tRNA Recognition.Dissecting protein-RNA recognition sites.

P2860

Q24643316-F7688C05-5C4E-4998-B459-7E43A3832C90 Q24672574-B1DDD23D-05C1-4421-B811-103B037A5BE9 Q24678207-8A9D24C4-FAB3-484E-953C-095A16B8331C Q24810161-CFA5DDB3-60FF-4FC9-9B65-5B0B7A5238E7 Q26799988-84E3491A-894D-42E4-A37B-F485E7A7AE37 Q27636050-6A14A346-B0E5-40B4-ADD1-36455E25146B Q27639036-AC5DF8D6-DA35-44B2-9630-1287CE1589C2 Q27639341-80431385-9B64-46FE-A4BE-493F43FAAEC2 Q27640374-1FE2FFCD-2075-454C-916A-B814C2A2B4BB Q27640379-EBAB7A63-06E2-4E1E-9345-A2577A898F91 Q27644417-A8BC3A33-F516-4318-930D-7D3A50B83A9E Q27649437-8006DFF1-9FDB-4F7F-84B4-2476D275C7F9 Q27656901-E54F002D-8849-4F5A-BD47-C991AC5E0859 Q27657427-D4479500-41BA-43D4-8DFC-ED81DE60E4B0 Q27681061-5CE5316A-B3A6-4E86-AFED-511EE9255380 Q27681498-A66FE3DC-7C91-4F19-A614-C757255EB3AC Q27683661-D93112D5-537F-4A30-BFF7-EB48DA01D67C Q27690292-9855A634-C416-4B65-A51A-41BA4927D347 Q29048143-0015E288-233B-4E77-B04A-E50C6D5EB3A5 Q33194152-F085EA4F-4CE8-4BC0-84B7-E324FBF5E488 Q33203997-86779AE2-CD92-4641-87C7-C18D0A6F861A Q33214237-8DA9042B-5A4B-4605-B807-F6CDA844C981 Q33888920-46576F19-6C9D-4D44-AA7F-2D5E0EF1ED5D Q33949738-01880944-70BC-42BD-9C5C-BBBB42D958A5 Q34027482-9923BDFF-5CAB-481C-89FF-EEFA427EDFB4 Q34385919-5C0DE2FE-9592-4764-B68F-26EE66E29A38 Q34536872-8CF9DA11-B91C-4369-9139-87355B0288EE Q35133650-440FA663-E5DE-4EA4-B325-E6A974037D53 Q35222948-9A5B8E4C-CE56-41A1-AA20-E011F7630B5B Q35596415-954C9D9F-E9CE-4FDF-953A-C46D25CCD32E Q35614613-ED77B21E-09D6-4849-945D-35FAC70DFCB7 Q35661618-A8CA38A0-7D4B-46BD-B8BF-74D6B3E1120D Q35847218-5BD5F8DB-FBD7-45FD-8086-090E12E2A3B2 Q37084494-9842E004-37F0-4C9C-A6F1-23D662293BA2 Q37286979-147A66C5-2D0B-4BDD-85C8-1C662935A925 Q37516281-DDCB486F-F69D-49BF-8C3D-38553F49C979 Q37636974-929D024B-5D53-4211-B270-013EE64ABF31 Q38088164-13720699-F3DD-441A-AA7C-5EBD68844830 Q38262499-A5E2F48D-ED7D-4F7D-A560-864BEECF0E2F Q38315151-86BF4C06-DD9E-4B3F-9768-B29495BB7746

P2860

tRNA aminoacylation by arginyl-tRNA synthetase: induced conformations during substrates binding

http://www.wikidata.org/entity/Q27627790

description

2000 nî lūn-bûn

@nan

2000 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի նոյեմբերին հրատարակված գիտական հոդված

@hy

2000年の論文

@ja

2000年論文

@yue

2000年論文

@zh-hant

2000年論文

@zh-hk

2000年論文

@zh-mo

2000年論文

@zh-tw

2000年论文

@wuu

name

tRNA aminoacylation by arginyl ...... ions during substrates binding

@ast

tRNA aminoacylation by arginyl ...... ions during substrates binding

@en

tRNA aminoacylation by arginyl ...... ions during substrates binding

@nl

type

label

tRNA aminoacylation by arginyl ...... ions during substrates binding

@ast

tRNA aminoacylation by arginyl ...... ions during substrates binding

@en

tRNA aminoacylation by arginyl ...... ions during substrates binding

@nl

prefLabel

tRNA aminoacylation by arginyl ...... ions during substrates binding

@ast

tRNA aminoacylation by arginyl ...... ions during substrates binding

@en

tRNA aminoacylation by arginyl ...... ions during substrates binding

@nl

P1433

Q27627790-25AC989F-0871-4F71-A657-88ECAAE6AF9A

P1476

Q27627790-30F2640E-60B9-4438-B9AF-E9B04FA45682

P2093

Q27627790-2E5FD428-22CD-41DA-9576-1689E60CA6EE

Q27627790-ED1BCD82-8333-417D-BFB7-0142B839AD33

P2860

Q27627790-063101EA-0310-4887-BBB9-AD3A8F6F8B9C

Q27627790-09451D67-C97B-4763-AAAE-B55A626D88F0

Q27627790-13707726-762D-448B-A14C-5A72EF4E7C6B

Q27627790-1E8C07E0-5E19-4495-9D98-622099FFB95F

Q27627790-2C970FB3-603C-4E18-8C3A-64FEE6BA9BC2

Q27627790-2CB2E6C3-2A76-4BD7-9E69-D8D1B35E54B0

Q27627790-2E22E9C6-3482-42FF-A03E-59DE2714848B

Q27627790-32908E58-953D-41B1-BDD9-299CB4FA9164

Q27627790-3D1A7787-50B7-489E-871A-4F855F0EC78A

Q27627790-3E1E5A9D-3541-4145-98B9-B5E684BFC37B

P304

Q27627790-29CDA112-0747-403E-8B6A-9A6C1FBDF4B3

P31

Q27627790-65AC9D15-E81E-4331-B6D1-B025DE7366B4

P356

Q27627790-2CE4BB33-AFFB-4250-964A-815C207F7DE7

P407

Q27627790-A9A4B57B-7F24-4E73-8819-DDFA055670DB

P433

Q27627790-84C8ED52-DA07-4FE1-BA8C-68F564A187AD

P478

Q27627790-725A7CD5-9BEA-4E0F-9A96-84060D8394E7

P50

Q27627790-25DD9EFB-BB26-46D1-B1E6-D20AEA7D5552

P577

Q27627790-62DD55EE-6BA3-4648-B576-E10031A92D31

P5875

Q27627790-7A42B870-1402-4985-93DF-28F7E2ED3E6F

P698

Q27627790-66DBEC1F-4211-4D26-9A01-70A44C9420A4

P932

Q27627790-484941DA-B37E-4457-A04A-2519CFC6795E

P356

P1433

The EMBO Journal

P1476

tRNA aminoacylation by arginyl ...... ions during substrates binding

@en

P2093

B Delagoutte

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

D Moras

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

P2860

The crystal structure of ribosomal protein S4 reveals a two-domain molecule with an extensive RNA-binding surface: one domain shows structural homology to the ETS DNA-binding motif

L-arginine recognition by yeast arginyl-tRNA synthetase.

Aminoacyl-tRNA synthetases, the genetic code, and the evolutionary process

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

The structure of threonyl-tRNA synthetase-tRNA(Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site

Insights into editing from an ile-tRNA synthetase structure with tRNAile and mupirocin

Synthesis of aspartyl-tRNA(Asp) in Escherichia coli--a snapshot of the second step.

Crystal structure of Escherichia coli methionyl-tRNA synthetase highlights species-specific features

Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP at 2.8 A resolution

Synthesis and recognition of aspartyl-adenylate by Thermus thermophilus aspartyl-tRNA synthetase

P304

5599-5610

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

P31

scholarly article

P356

10.1093/EMBOJ/19.21.5599

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

P407

P433

21

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

P478

19

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

P50

P577

2000-11-01T00:00:00Z

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

P5875

12266935

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

P698

11060012

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

P932

305789

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