Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus - Wikidata - awgldk - TriplyDB

Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus

Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus

http://www.wikidata.org/entity/Q27729878

about

Expression of a gene encoding a tRNA synthetase-like protein is enhanced in tumorigenic human myeloid leukemia cells and is cell cycle stage- and differentiation-dependent The p43 component of the mammalian multi-synthetase complex is likely to be the precursor of the endothelial monocyte-activating polypeptide II cytokine Structure of the EMAPII domain of human aminoacyl-tRNA synthetase complex reveals evolutionary dimer mimicry Post-transfer editing in vitro and in vivo by the beta subunit of phenylalanyl-tRNA synthetase Purification, crystallization and preliminary X-ray characterization of a human mitochondrial phenylalanyl-tRNA synthetase TARP: a nuclear protein expressed in prostate and breast cancer cells derived from an alternate reading frame of the T cell receptor gamma chain locus Pyrrolysyl-tRNA synthetase: an ordinary enzyme but an outstanding genetic code expansion tool The crystal structure of the ttCsaA protein: an export-related chaperone from Thermus thermophilus.Crystal structure of a hypothetical protein, TT1725, from Thermus thermophilus HB8 at 1.7 A resolution Toward understanding phosphoseryl-tRNACys formation: The crystal structure of Methanococcus maripaludis phosphoseryl-tRNA synthetase Eukaryotic cytosolic and mitochondrial phenylalanyl-tRNA synthetases catalyze the charging of tRNA with the meta-tyrosine Structural insights into the first step of RNA-dependent cysteine biosynthesis in archaea Unique protein architecture of alanyl-tRNA synthetase for aminoacylation, editing, and dimerization Idiosyncrasy and identity in the prokaryotic phe-system: Crystal structure ofE. coliphenylalanyl-tRNA synthetase complexed with phenylalanine and AMP The Role of a Novel Auxiliary Pocket in Bacterial Phenylalanyl-tRNA Synthetase Druggability The mechanistic and evolutionary aspects of the 2'- and 3'-OH paradigm in biosynthetic machinery The evolutionary history of Cys-tRNACys formation.The NMR structure of Escherichia coli ribosomal protein L25 shows homology to general stress proteins and glutaminyl-tRNA synthetases.Structural similarities in the noncatalytic domains of phenylalanyl-tRNA and biotin synthetases Double-sieving-defective aminoacyl-tRNA synthetase causes protein mistranslation and affects cellular physiology and development Functional analysis of peptide motif for RNA microhelix binding suggests new family of RNA-binding domains An RNA ligase from Deinococcus radiodurans.The Escherichia coli lipB gene encodes lipoyl (octanoyl)-acyl carrier protein:protein transferase.Fidelity escape by the unnatural amino acid β-hydroxynorvaline: an efficient substrate for Escherichia coli threonyl-tRNA synthetase with toxic effects on growth.Footprinting of tRNA(Phe) transcripts from Thermus thermophilus HB8 with the homologous phenylalanyl-tRNA synthetase reveals a novel mode of interaction.RNA binding targets aminoacyl-tRNA synthetases to translating ribosomes.Structural and mutational studies of the amino acid-editing domain from archaeal/eukaryal phenylalanyl-tRNA synthetase.Universal pathway for posttransfer editing reactions: insights from the crystal structure of TtPheRS with puromycin High Throughput Screen Identifies Natural Product Inhibitor of Phenylalanyl-tRNA Synthetase from Pseudomonas aeruginosa and Streptococcus pneumoniae.New class of bacterial phenylalanyl-tRNA synthetase inhibitors with high potency and broad-spectrum activity.Mechanism of tRNA-dependent editing in translational quality control Defining functional distance using manifold embeddings of gene ontology annotations.Structure and two-metal mechanism of a eukaryal nick-sealing RNA ligase.The homotetrameric phosphoseryl-tRNA synthetase from Methanosarcina mazei exhibits half-of-the-sites activity.Transplantation of a tyrosine editing domain into a tyrosyl-tRNA synthetase variant enhances its specificity for a tyrosine analog.The crystal structures of the α-subunit of the α(2)β (2) tetrameric Glycyl-tRNA synthetase Protein synthesis editing by a DNA aptamer.A biologically active 53 kDa fragment of overproduced alanyl-tRNA synthetase from Thermus thermophilus HB8 specifically interacts with tRNA Ala acceptor helix.Structural Aspects of Phenylalanylation and Quality Control in Three Major Forms of Phenylalanyl-tRNA Synthetase.Kinetic and structural changes in HsmtPheRS, induced by pathogenic mutations in human FARS2.

P2860

Q24308114-B3CE774E-A820-4F1B-899C-46A3DF82FACE Q24314886-F076ACCD-B8F7-4F3C-B494-F9A77573DC7A Q24536732-4C92DA8C-8E56-4942-BD4E-8CDE6146CC54 Q24559890-A2C24876-280A-417F-89CA-078EFDFD9F6F Q24657525-BD8C32A1-7F5B-468B-B3D1-2BAF0BAE6E47 Q24673353-4EA5FFEA-D5F5-4F71-84F4-5AFFA211974F Q26850882-74ED6766-0EE4-401E-80B5-5512E9F11F38 Q27629266-7101AF4A-CA47-4155-A10B-AFF87AA0012A Q27642420-9DB0464F-8063-46C2-A845-B5A334082777 Q27643821-76939B1A-48EB-43BC-8104-8021012E46B0 Q27643962-4576990B-F0F7-446C-8B35-D77CD68D788D Q27644031-EB8004DD-C35E-4453-A423-56ED77F3A973 Q27655412-630B452F-E6FA-4B99-A246-181C4ADC54E3 Q27665929-0B387EBE-4C97-42CE-980E-45030F6CED98 Q27684359-8395144B-6737-430E-AC55-822EAC36EC49 Q28676991-641B0C74-17C4-49AA-9EA2-A8C452F2874B Q28768709-530EC008-88DE-4BB4-AE1C-85AA17DCACA1 Q30175995-565A1688-0011-457B-A3C3-DE27771E8561 Q30192985-06D791AA-5FAF-46BE-A991-D0E57519AF69 Q30607478-34AB22E6-C1B4-415F-8148-9AE2FB8E589E Q32022036-10FB6C5F-104C-4A3A-B0F6-DABAB93F38DB Q33980934-30D0E152-CCF1-4FBA-BF4A-97287F36076F Q34688122-2D8D8E9A-9560-4A08-AFD9-C5F3B3CB2967 Q34714315-367CB1A4-4525-448E-A4D1-B03CE980FB04 Q34780247-9F4A8FB6-FF89-40D9-8F42-EF6ED98920C9 Q35063447-EDF2ED38-4456-48E9-AFF1-804E9A01AFFB Q35075453-BC682D03-3092-4BD4-88E8-211B47535F46 Q35279945-3F311763-D20C-433F-8FBF-C964A8E30ECF Q35544892-A20D8F24-4201-4F18-BD9E-27392D29B50B Q35547361-F4271408-46C1-4ED5-8748-591B7CE67C50 Q35576074-1215EEC5-7393-4F76-A1FB-89F2EF39EF68 Q36090173-F9B8F87A-1409-4A7B-8AA5-532254435712 Q36300386-F344DA0F-95A8-425B-ABA4-F6FABE8F61D1 Q36808459-CE693844-899A-4690-AA3F-9CCC12E8DE0F Q36869815-3124A06E-11F9-4014-8A65-BB362A957745 Q36950783-43D4E035-3BB9-47CC-A2F4-1F4FFD0E660B Q37673897-C50D0940-916D-4E28-9AFC-C48812A64AFF Q39720569-35A66420-76FE-4B07-B6AD-917AA3135C2D Q40970864-EB05AA1D-0F41-4D1E-B39C-FC65FE698E70 Q41088644-90905C2F-E006-41FC-9680-3E5D87983F2F

P2860

Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus

http://www.wikidata.org/entity/Q27729878

description

1995 nî lūn-bûn

@nan

1995 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

1995 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

1995年の論文

@ja

1995年論文

@yue

1995年論文

@zh-hant

1995年論文

@zh-hk

1995年論文

@zh-mo

1995年論文

@zh-tw

1995年论文

@wuu

name

Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus

@ast

Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus

@en

Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus

@nl

type

label

Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus

@ast

Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus

@en

Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus

@nl

prefLabel

Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus

@ast

Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus

@en

Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus

@nl

P1433

Q27729878-3DC34C88-2FFF-4F6D-A10A-F2E36FECD150

P1476

Q27729878-337A1BD2-5AA3-47BC-84A9-8729A0C62B3F

P2093

Q27729878-28FCFEAB-7C3A-40B2-8D78-B5FF79708B8C

Q27729878-444D8DB3-5F13-4FBB-947E-5E7730790C90

Q27729878-A0323DCB-E51E-471D-9D9C-DC0540066FA1

Q27729878-B08113C1-9280-4B05-956C-5E9370B86AAB

Q27729878-D090728E-733A-4346-9290-5079622CF1A4

P2860

Q27729878-2171DAFA-318A-491B-97EC-67E6B7D33EB1

Q27729878-28254E92-BA18-4A1E-80FF-7B1FE32377DB

Q27729878-2A96A308-9C28-4CAB-B2E1-158D46F3604C

Q27729878-643ED9DF-9E8E-4D9E-8E9D-3C0AEC2062FE

Q27729878-6F12E111-5EED-40C5-94D6-B564E6E12286

Q27729878-D5C8EE71-F145-4CD5-B1FA-51B419A20F40

Q27729878-DDB440F5-1730-4A04-9F7F-B9EE69A5619F

Q27729878-E2A66733-A60C-4456-AE4F-00B2C3449224

Q27729878-F038FC2D-1C28-489B-AE52-9B518EEBADB2

Q27729878-F6E52C7E-7EF0-451D-B759-33816F4A11E8

P304

Q27729878-F0614C6D-4F08-4CBA-B710-3ABF6A5FD15A

P31

Q27729878-01E1A744-AAF9-4B37-B2C9-05FC13552F68

P356

Q27729878-6F72B544-F065-46CE-8C06-F8E889EA51D1

P433

Q27729878-5E9867E3-FF59-4326-AFEF-D2962903B2D1

P478

Q27729878-9F0E3F0E-7B82-4CD7-BF63-54812A3E7726

P577

Q27729878-ED184BA8-3B13-4C29-8B70-AD5F65984AA0

P5875

Q27729878-A8FD951F-2915-48E9-B002-CA7093976312

P698

Q27729878-D017D0CC-51AA-4A74-B53A-68D5FBE5404D

P356

P1433

Nature structural biology

P1476

Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus

@en

P2093

L Mosyak

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

L Reshetnikova

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

M Delarue

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

M G Safro

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

Y Goldgur

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

P2860

PROCHECK: a program to check the stereochemical quality of protein structures

Crystal structure of the RNA-binding domain of the U1 small nuclear ribonucleoprotein A

Crystal structure at 1.92 A resolution of the RNA-binding domain of the U1A spliceosomal protein complexed with an RNA hairpin

Free R value: a novel statistical quantity for assessing the accuracy of crystal structures

Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs

Resolution of phase ambiguity in macromolecular crystallography

A graphics model building and refinement system for macromolecules

A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 A.

Sequence, structure and evolutionary relationships between class 2 aminoacyl-tRNA synthetases: an update.

Phenylalanyl-tRNA synthetase from E. coli MRE-600: analysis of the active site distribution on the enzyme subunits by affinity labelling.

P304

537-47

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

P31

scholarly article

P356

10.1038/NSB0795-537

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

P433

7

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

P478

2

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

P577

1995-07-01T00:00:00Z

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

P5875

15535279

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

P698

7664121

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