Potassium functionally replaces the second lysine of the KMSKS signature sequence in human tyrosyl-tRNA synthetase - Test2 - elhamkhani - TriplyDB

Potassium functionally replaces the second lysine of the KMSKS signature sequence in human tyrosyl-tRNA synthetase

Potassium functionally replaces the second lysine of the KMSKS signature sequence in human tyrosyl-tRNA synthetase

http://www.wikidata.org/entity/Q28212098

about

sameAs

Glycerol-3-phosphate cytidylyltransferase. Structural changes induced by binding of CDP-glycerol and the role of lysine residues in catalysis Functional and Crystal Structure Analysis of Active Site Adaptations of a Potent Anti-Angiogenic Human tRNA Synthetase The Double-Length Tyrosyl-tRNA Synthetase from the Eukaryote Leishmania major Forms an Intrinsically Asymmetric Pseudo-Dimer Comparison of the catalytic roles played by the KMSKS motif in the human and Bacillus stearothermophilus trosyl-tRNA synthetases Reduced amino acid specificity of mammalian tyrosyl-tRNA synthetase is associated with elevated mistranslation of Tyr codons.Orthogonal use of a human tRNA synthetase active site to achieve multifunctionality Aminoacyl-tRNA synthetases: essential and still promising targets for new anti-infective agents.Computational modeling and molecular dynamics simulations of mammalian cytoplasmic tyrosyl-tRNA synthetase and its complexes with substrates.Activation of D-tyrosine by Bacillus stearothermophilus tyrosyl-tRNA synthetase: 2. Cooperative binding of ATP is limited to the initial turnover of the enzyme.Conformational landscapes for KMSKS loop in tyrosyl-tRNA synthetases.Recognize three different human telomeric G-quadruplex conformations by quinacrine.

P2860

Q27642222-49182615-7287-49B1-9A03-5CAAF4A1F782 Q27646797-1551DDC4-9638-4A54-B3C9-AFEA75C80C7A Q27667299-EBA0090E-AAB0-4434-BE94-A48F8612D1DA Q28218070-322DEBE6-8B38-42B1-8EF0-6979545CDEC8 Q33793012-C0110A83-9135-477D-9ACC-42D3693C0B6C Q34593076-63D0D034-5A06-4979-A2DD-2A6FB8FF0274 Q36802598-816B4AAE-6E6E-4684-877B-66AADE48D5FA Q39403152-46EF2B2B-2B88-4499-8ABF-24BAB8749514 Q39648089-060DC4AA-300F-4D4F-9334-1DF7D1C0E3C9 Q42653986-DBC23E4A-A43A-4A97-A433-AD310377486E Q54538195-557B0746-3574-498B-B87A-640AD18E2A4B

P2860

Potassium functionally replaces the second lysine of the KMSKS signature sequence in human tyrosyl-tRNA synthetase

http://www.wikidata.org/entity/Q28212098

description

2002 nî lūn-bûn

@nan

2002 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2002年の論文

@ja

2002年論文

@yue

2002年論文

@zh-hant

2002年論文

@zh-hk

2002年論文

@zh-mo

2002年論文

@zh-tw

2002年论文

@wuu

name

Potassium functionally replace ...... human tyrosyl-tRNA synthetase

@ast

Potassium functionally replace ...... human tyrosyl-tRNA synthetase

@en

Potassium functionally replace ...... human tyrosyl-tRNA synthetase

@nl

type

label

Potassium functionally replace ...... human tyrosyl-tRNA synthetase

@ast

Potassium functionally replace ...... human tyrosyl-tRNA synthetase

@en

Potassium functionally replace ...... human tyrosyl-tRNA synthetase

@nl

prefLabel

Potassium functionally replace ...... human tyrosyl-tRNA synthetase

@ast

Potassium functionally replace ...... human tyrosyl-tRNA synthetase

@en

Potassium functionally replace ...... human tyrosyl-tRNA synthetase

@nl

P1433

Q28212098-AFDA1D3D-5A09-444A-9C40-781DFE56C383

P1476

Q28212098-B204D703-30E1-4A6A-882D-8D6C8E462824

P2093

Q28212098-9BA045A8-704F-4304-9FA9-DFB145E9B964

Q28212098-9E5B48CF-1621-4212-A5B4-CA55D95ADFC0

P2860

Q28212098-04F1BE9A-8F32-426C-885A-72E0CF96EE48

Q28212098-11D375A6-0AD4-4BE4-AB6B-B2DF481EE63A

Q28212098-20516E7D-EDE4-4DC0-BCFA-1BF5F30B9D94

Q28212098-2D54D1D7-A09E-4EFC-8C1E-D30B4A8C8B96

Q28212098-35593890-37EA-4B56-8BEF-CB275C3D58D1

Q28212098-4A999693-7143-4E37-85D0-28733E05CA45

Q28212098-5D1EFAB5-94E2-4898-A32F-A6EDA233ADEA

Q28212098-6075EB8B-F44B-4D85-9CB7-2AA7F8B91079

Q28212098-65E8C2F1-182E-4E88-8CC0-767F7F158495

Q28212098-76287115-3E19-40F5-BF3B-A08F6F3E2EC8

P304

Q28212098-3DD4470D-6911-4C4B-BEA8-728DDD49A1D9

P31

Q28212098-4800D428-9612-4499-90C9-E34E7FA5F8E6

P356

Q28212098-00028A24-4583-45D8-B9DE-9EAE9934C63F

P407

Q28212098-D7DDFFCA-1B44-4364-85E3-066A7D24992C

P433

Q28212098-6AEE0C33-065B-4CFC-9066-AEDA01C0AD4A

P478

Q28212098-03871A9D-0C0E-4E6E-A989-3CA640CE2495

P577

Q28212098-9551524B-2842-4E61-8DB0-AFCDC2EF73BF

P698

Q28212098-863EB420-B1DE-44C6-81AC-63EB5E5310D2

P356

P1433

Journal of Biological Chemistry

P1476

Potassium functionally replace ...... human tyrosyl-tRNA synthetase

@en

P2093

Eric A First

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

Joseph Austin

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

P2860

Genetic code in evolution: switching species-specific aminoacylation with a peptide transplant.

THE ATTRACTIONS OF PROTEINS FOR SMALL MOLECULES AND IONS

Human tyrosyl-tRNA synthetase shares amino acid sequence homology with a putative cytokine

Catalysis of tyrosyl-adenylate formation by the human tyrosyl-tRNA synthetase

Reconstruction by site-directed mutagenesis of the transition state for the activation of tyrosine by the tyrosyl-tRNA synthetase: a mobile loop envelopes the transition state in an induced-fit mechanism.

Genomics-based identification of targets in pathogenic bacteria for potential therapeutic and diagnostic use.

Mechanism of mupirocin transport into sensitive and resistant bacteria

Thyroid Ribonucleic Acid-Iodopeptides. Comparison of Tyrosyl-Complex II and Tyrosyl-tRNA.

Ligand binding and enzymic catalysis coupled through subunits in tyrosyl-tRNA synthetase.

Dissection of the structure and activity of the tyrosyl-tRNA synthetase by site-directed mutagenesis.

P304

20243-8

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

P31

scholarly article

P356

10.1074/JBC.M201923200

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

P407

P433

23

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

P478

277

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

P577

2002-06-07T00:00:00Z

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

P698

11927599

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