The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases - Test2 - elhamkhani - TriplyDB

The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases

The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases

http://www.wikidata.org/entity/Q27640478

about

On the evolution of structure in aminoacyl-tRNA synthetases Biosynthesis and functions of mycothiol, the unique protective thiol of Actinobacteria Comparative genomics of Archaea: how much have we learned in six years, and what's next?On the origin of life in the Zinc world. 2. Validation of the hypothesis on the photosynthesizing zinc sulfide edifices as cradles of life on Earth Structure of the prolyl-tRNA synthetase from the eukaryotic pathogenGiardia lamblia Towards a functional identification of catalytically inactive [Fe]-hydrogenase paralogs Pre-transfer editing by class II prolyl-tRNA synthetase: role of aminoacylation active site in "selective release" of noncognate amino acids.An isolated class II aminoacyl-tRNA synthetase insertion domain is functional in amino acid editing Cotranslational incorporation of a structurally diverse series of proline analogues in an Escherichia coli expression system.TALI: local alignment of protein structures using backbone torsion angles.Ligand co-crystallization of aminoacyl-tRNA synthetases from infectious disease organisms Evolution of multiple, mutually orthogonal prolyl-tRNA synthetase/tRNA pairs for unnatural amino acid mutagenesis in Escherichia coli.Cysteinyl-tRNA(Cys) formation in Methanocaldococcus jannaschii: the mechanism is still unknown.Substrate-mediated fidelity mechanism ensures accurate decoding of proline codons.Homologous trans-editing factors with broad tRNA specificity prevent mistranslation caused by serine/threonine misactivation.Structural Basis for Specific Inhibition of tRNA Synthetase by an ATP Competitive Inhibitor.Structure of a putative trans-editing enzyme for prolyl-tRNA synthetase from Aeropyrum pernix K1 at 1.7 A resolution.Reconstitution of translation from Thermus thermophilus reveals a minimal set of components sufficient for protein synthesis at high temperatures and functional conservation of modern and ancient translation components Emergence and evolution.Trans-editing of Cys-tRNAPro by Haemophilus influenzae YbaK protein.Asymmetric behavior of archaeal prolyl-tRNA synthetase.

P2860

Q24597654-F3D55450-422E-4D3A-8D56-3842B1080D3E Q24646505-4B3B3042-08F8-4D9D-8998-BE2B126750D5 Q24796655-27B68B3E-05FC-4ED3-AB1D-DD84330E47C7 Q27498817-09DD2F13-B640-47B3-B88F-37F51FAFA97C Q27671923-5B5DD0BD-3EBD-4C10-BF63-5D53A2276116 Q27701046-5C58BF24-0921-4EF6-936B-E45E0AF06057 Q27939503-24A96EA8-593B-499D-9DEF-B64B60C2D613 Q28484984-E86DA28B-BF99-46B2-91F1-6D69A23D22F5 Q30342165-EBC7CA27-3E30-4E81-A065-65BFDB5E670F Q30368126-7C870A83-C288-4D06-9EA5-36A587481CDD Q33671214-3F91E9DE-D8F9-4F31-B9B4-A1D55695D569 Q34395094-9B7BB9F3-C6C5-404C-8927-9EED27F7CD35 Q34555735-25B2DA2C-EF67-49AF-A30E-373635487412 Q35213173-BECC2A08-D0ED-41C0-A4E9-0AE85C1B5B46 Q35616247-5FCA4610-010A-40D4-A244-9A47B77FE310 Q35854829-95A4411A-A718-4C41-873B-FDE6267621D2 Q35950869-4020D4AB-1BB0-44EA-A6E4-0F27891FB32C Q36228630-C9237EB5-D00F-411D-BADD-FDC9A8DF43A6 Q38088164-B945865F-190B-4C35-AEE2-A7A195193D62 Q45025085-FA3CACFC-07F2-4143-924D-6636438C3CF9 Q46754146-3F98D50D-83F2-4CCC-9463-A577E8FBCC86

P2860

The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases

http://www.wikidata.org/entity/Q27640478

description

2003 nî lūn-bûn

@nan

2003 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2003年の論文

@ja

2003年論文

@yue

2003年論文

@zh-hant

2003年論文

@zh-hk

2003年論文

@zh-mo

2003年論文

@zh-tw

2003年论文

@wuu

name

The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases

@ast

The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases

@en

The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases

@nl

type

label

The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases

@ast

The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases

@en

The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases

@nl

prefLabel

The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases

@ast

The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases

@en

The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases

@nl

P1433

Q27640478-E7A1646D-6EB6-4F6E-A73D-5A54CF95C2D2

P1476

Q27640478-2BCB810E-1C66-426D-81DF-627B5D6928E2

P2093

Q27640478-01D4389C-6677-4296-BA1E-EED1357E8B30

Q27640478-26770809-6300-4EB0-BB42-D1B0DE4410B5

Q27640478-84847236-B233-4BCD-ACB8-AABC309F5B23

Q27640478-BE892090-8EB7-4FD0-A13D-6505C207E64B

Q27640478-C4D73027-DE7F-482D-A2BE-BBFE17662C73

P2860

Q27640478-016642DB-63A8-486F-BE1A-7669332195AF

Q27640478-034E9291-115A-4958-A0B1-7B2C549DD966

Q27640478-04A1593A-D22B-4B35-8808-1316162795BA

Q27640478-0BAF59C1-7048-458F-B904-8EEA31E42B3B

Q27640478-0F773BFA-8346-4CB2-A7FB-45039BDB32A4

Q27640478-1CC2A1A7-783B-4F48-BF05-76D4AEC0CEE7

Q27640478-2EF1F5A1-1AF0-4A3E-8002-B7AC57DF895C

Q27640478-302868A1-A99F-4FE9-B2D3-EB3902F2FCDA

Q27640478-3CB035DE-72B9-4A3B-840D-F61CA176C200

Q27640478-458F8B22-F03B-4A91-AC99-36809839614F

P304

Q27640478-51F958EA-60F8-4C7A-B3C3-5CA2C915970F

P31

Q27640478-59B51F5C-6F1C-4B9B-8957-462390805921

P356

Q27640478-044658DE-B95F-4F59-A219-875AF2F2D0D5

P407

Q27640478-F99843C4-5A67-4012-8045-DAAF741B3486

P433

Q27640478-8FC1D363-5D22-4D37-8BB5-8EFE896C9EE4

P478

Q27640478-9FB2A7CC-BFA9-498D-9D4F-C8017006CD2C

P50

Q27640478-FB905180-8D8E-44BB-AB7A-3ADD91FD0380

P577

Q27640478-176A687E-C326-4242-848F-D89462884E15

P5875

Q27640478-025062C7-CB6E-49C6-8624-22C69EA7CEFD

P698

Q27640478-3B43C717-B500-47E9-A9D7-182CA7400DEA

P932

Q27640478-150F03EB-F3DF-4E5C-ACA4-A8899A18D9E0

P356

PNAS.0437911100

P1433

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

P1476

The structural basis of cysteine aminoacylation of tRNAPro by prolyl-tRNA synthetases

@en

P2093

Constantinos Stathopoulos

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

Jimin Wang

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

Satwik Kamtekar

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

Thomas A Steitz

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

W Dexter Kennedy

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

P2860

Complete Genome Sequence of the Methanogenic Archaeon, Methanococcus jannaschii

The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens.

Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics

Improved methods for building protein models in electron density maps and the location of errors in these models

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

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

Processing of X-ray diffraction data collected in oscillation mode

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

The 2 Å crystal structure of leucyl-tRNA synthetase and its complex with a leucyl-adenylate analogue

Structural basis for double-sieve discrimination of L-valine from L-isoleucine and L-threonine by the complex of tRNA(Val) and valyl-tRNA synthetase

P304

1673-8

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

P31

scholarly article

P356

10.1073/PNAS.0437911100

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

P407

P433

4

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

P478

100

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

P50

P577

2003-02-18T00:00:00Z

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

P5875

10907370

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

P698

12578991

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

P932

149891

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