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lysine-trna ligase - metabolism (225) 225
lysine-trna ligase - genetics (103) 103
biochemistry & molecular biology (98) 98
humans (84) 84
animals (79) 79
molecular sequence data (79) 79
lysine-trna ligase - chemistry (77) 77
index medicus (76) 76
kinetics (64) 64
amino acyl-trna synthetases - metabolism (63) 63
escherichia coli - enzymology (55) 55
escherichia-coli (54) 54
amino acid sequence (53) 53
transfer rna (52) 52
base sequence (44) 44
lysine - metabolism (44) 44
escherichia coli - genetics (42) 42
models, molecular (41) 41
mutation (41) 41
rna, transfer, lys - metabolism (41) 41
research (40) 40
protein binding (39) 39
ligases (33) 33
proteins (32) 32
transfer-rna-synthetase (32) 32
trna (31) 31
binding sites (30) 30
bacteria (29) 29
crystal-structure (28) 28
lysyl-trna synthetase (28) 28
aminoacyl-trna synthetases (27) 27
cell biology (27) 27
substrate specificity (27) 27
protein biosynthesis (26) 26
rna, transfer - metabolism (26) 26
rats (25) 25
enzymes (23) 23
lysine (23) 23
amino acyl-trna synthetases - genetics (22) 22
complex (22) 22
recognition (22) 22
aminoacylation (21) 21
binding (21) 21
liver - enzymology (21) 21
lysine - analogs & derivatives (21) 21
adenosine triphosphate - metabolism (20) 20
biophysics (20) 20
nucleic acid conformation (20) 20
rna, transfer, lys - genetics (20) 20
analysis (19) 19
escherichia coli (19) 19
physiological aspects (19) 19
research article (19) 19
rna, transfer, lys - chemistry (18) 18
saccharomyces cerevisiae - enzymology (18) 18
sequence alignment (18) 18
sequence homology, amino acid (18) 18
acylation (17) 17
article (17) 17
escherichia coli - metabolism (17) 17
molecular weight (17) 17
protein structure, tertiary (17) 17
rna, transfer, amino acyl - metabolism (17) 17
amino acids (16) 16
aminoacyl-trna synthetase (16) 16
cloning, molecular (16) 16
immunodeficiency-virus type-1 (16) 16
protein (16) 16
translation (16) 16
crystallography, x-ray (15) 15
transcription, genetic (15) 15
cell line (14) 14
dna (14) 14
gene expression (14) 14
lysine-trna ligase - antagonists & inhibitors (14) 14
lysine-trna ligase - isolation & purification (14) 14
mice (14) 14
microbiology (14) 14
protein conformation (14) 14
biological sciences (13) 13
expression (13) 13
genetic aspects (13) 13
hiv-1 - physiology (13) 13
lysine - chemistry (13) 13
multidisciplinary sciences (13) 13
plasmids (13) 13
recombinant proteins - metabolism (13) 13
structure-activity relationship (13) 13
anticodon (12) 12
evolution, molecular (12) 12
gag (12) 12
gene (12) 12
genes (12) 12
genetic-code (12) 12
hiv-1 - genetics (12) 12
macromolecular substances (12) 12
mitochondria (12) 12
mitochondria - metabolism (12) 12
phosphorylation (12) 12
protein structure, secondary (12) 12
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81. Full Text Engineered Monomeric Human Histidine Triad Nucleotide-binding Protein 1 Hydrolyzes Fluorogenic Acyl-adenylate and Lysyl-tRNA Synthetase-generated Lysyl-adenylate
by Tsui-Fen Chou and Ilya B. Tikh and Bruno A. C. Horta and Brahma Ghosh and Ricardo B. De Alencastro and Carston R. Wagner
Journal of Biological Chemistry, ISSN 0021-9258, 05/2007, Volume 282, Issue 20, pp. 15137 - 15147
Hint1 is a homodimeric protein and member of the ubiquitous HIT superfamily. Hint1 catalyzes the hydrolysis of purine phosphoramidates and lysyl-adenylate... 
TRANSCRIPTIONAL ACTIVITY | MECHANISM | HINT | SUBSTRATE | BIOCHEMISTRY & MOLECULAR BIOLOGY | GROWTH | ACTIVATED MAST-CELLS | FORCE-FIELD | SUBUNIT INTERFACE | FHIT | C-INTERACTING PROTEIN-1 | Mutagenesis, Site-Directed | Adenosine Monophosphate - metabolism | Humans | Adenosine Monophosphate - chemistry | Protein Structure, Tertiary - genetics | Binding Sites - genetics | Substrate Specificity - genetics | Nerve Tissue Proteins - genetics | Hydrolysis | Nerve Tissue Proteins - metabolism | Nerve Tissue Proteins - chemistry | Adenosine Monophosphate - analogs & derivatives | Lysine-tRNA Ligase - metabolism | Lysine-tRNA Ligase - chemistry | Catalysis | Enzyme Stability - genetics | Kinetics | Adenosine Monophosphate - chemical synthesis | Circular Dichroism | Dimerization | Amino Acid Substitution
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82. Full Text The Interaction between HIV-1 Gag and Human Lysyl-tRNA Synthetase during Viral Assembly
by Hassan Javanbakht and Rabih Halwani and Shan Cen and Jenan Saadatmand and Karin Musier-Forsyth and Heinrich Gottlinger and Lawrence Kleiman
Journal of Biological Chemistry, ISSN 0021-9258, 07/2003, Volume 278, Issue 30, pp. 27644 - 27651
Human lysyl-tRNA synthetase (LysRS) is a tRNA-binding protein that is selectively packaged into HIV-1 along with its cognate tRNA Lys isoacceptors. Evidence... 
CAPSID PROTEIN | WILD-TYPE | TERMINAL DOMAIN | PARTICLES | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | IMMUNODEFICIENCY-VIRUS TYPE-1 | PR160GAG-POL | PRIMER TRANSFER-RNAS | BINDING | Protein Structure, Tertiary | Cell Line | Humans | Glutathione Transferase - metabolism | Cytoplasm - metabolism | Plasmids - metabolism | Blotting, Western | Precipitin Tests | Gene Products, gag - metabolism | HIV-1 - physiology | Transfection | Gene Deletion | Protein Binding | Lysine-tRNA Ligase - metabolism | Models, Genetic | Proto-Oncogene Proteins c-myc - genetics | Mutation | Binding Sites | Dimerization
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83. Full Text Anticodon Recognition and Discrimination by the α-Helix Cage Domain of Class I Lysyl-tRNA Synthetase
by Levengood, Jeffrey D and Roy, Hervé and Ishitani, Ryuichiro and Söll, Dieter and Nureki, Osamu and Ibba, Michael
Biochemistry, ISSN 0006-2960, 10/2007, Volume 46, Issue 39, pp. 11033 - 11038
Aminoacyl-tRNA synthetases are normally found in one of two mutually exclusive structural classes, the only known exception being lysyl-tRNA synthetase which... 
IDENTITY | COMPLEX | EVOLUTION | BINDING | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRNA(LYS) | Amino Acyl-tRNA Synthetases - genetics | Protein Structure, Tertiary | Amino Acid Sequence | Lysine-tRNA Ligase - genetics | Anticodon - metabolism | Protein Structure, Secondary | Anticodon - genetics | Models, Molecular | Molecular Sequence Data | Substrate Specificity | Structure-Activity Relationship | Sequence Homology, Amino Acid | Glutamate-tRNA Ligase - metabolism | Models, Biological | Glutamate-tRNA Ligase - chemistry | Protein Binding | Lysine-tRNA Ligase - metabolism | Lysine-tRNA Ligase - chemistry | Amino Acyl-tRNA Synthetases - chemistry | Mutation | Amino Acyl-tRNA Synthetases - metabolism | Binding Sites | Glutamate-tRNA Ligase - genetics
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84. Full Text Entamoeba lysyl-tRNA synthetase contains a cytokine-like domain with chemokine activity towards human endothelial cells
by de Moura, Manuel Castro and Miro, Francesc and Han, Jung Min and Kim, Sunghoon and Celada, Antonio and Ribas de Pouplana, Lluís
PLoS Neglected Tropical Diseases, ISSN 1935-2727, 11/2011, Volume 5, Issue 11, p. e1398
Immunological pressure encountered by protozoan parasites drives the selection of strategies to modulate or avoid the immune responses of their hosts. Here we... 
HISTOLYTICA PATHOGENESIS | MAXIMUM-LIKELIHOOD | IN-VITRO | PROTEIN | CHEMOATTRACTANT ACTIVITY | ACTIVATING POLYPEPTIDE-II | LIVER | GENE-EXPRESSION | NONCANONICAL FUNCTION | PARASITOLOGY | TROPICAL MEDICINE | TRANSLATIONAL CONTROL | Protein Structure, Tertiary | Lysine-tRNA Ligase - genetics | RNA-Binding Proteins - genetics | Cytokines - metabolism | Humans | Cells, Cultured | Molecular Sequence Data | Neoplasm Proteins - metabolism | Human Experimentation | Sequence Analysis, DNA | Endothelial Cells - parasitology | Sequence Homology, Amino Acid | Entamoeba histolytica - genetics | Entamoeba histolytica - enzymology | Lysine-tRNA Ligase - metabolism | Neoplasm Proteins - genetics | Cytokines - genetics | RNA-Binding Proteins - metabolism | Physiological aspects | Entamoeba histolytica | Immune response | Research | Aminoacyl-tRNA synthetases | Proteins | Polypeptides | Migration | Parasites | Gene expression | Experiments | Mass spectrometry | Chemokines | Apoptosis
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85. Full Text Identity Elements for Specific Aminoacylation of a tRNA by Mammalian Lysyl-tRNA Synthetase Bearing a Nonspecific tRNA-Interacting Factor
by Francin, Mathilde and Mirande, Marc
Biochemistry, ISSN 0006-2960, 08/2006, Volume 45, Issue 33, pp. 10153 - 10160
Mammalian lysyl-tRNA synthetase (LysRS) has an N-terminal polypeptide chain extension appended to a prokaryotic-like synthetase domain. This extension, termed... 
YEAST | ANTICODON-BINDING DOMAIN | ADENYLATE | CONFORMATIONAL-CHANGES | ACID | RECOGNITION | N-TERMINAL EXTENSION | EFFICIENT AMINOACYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | MINIHELICES | METHIONINE | RNA-Binding Proteins - genetics | Aminoacylation | Anticodon - metabolism | Humans | Molecular Sequence Data | RNA - genetics | Base Sequence | RNA, Transfer - genetics | Lysine-tRNA Ligase - chemistry | Catalysis | Nucleic Acid Conformation | RNA, Transfer - chemistry | Binding Sites | RNA, Transfer, Lys - metabolism | RNA - metabolism | Yeasts - metabolism | Lysine-tRNA Ligase - genetics | RNA, Transfer, Lys - chemistry | Anticodon - genetics | RNA, Transfer - metabolism | RNA-Binding Proteins - chemistry | RNA - chemistry | RNA, Transfer, Lys - genetics | Yeasts - genetics | Animals | Base Pairing | Lysine-tRNA Ligase - metabolism | Kinetics | RNA-Binding Proteins - metabolism | RNA | Analysis | Research | Nucleotide sequencing | Structure | Aminoacyl-tRNA synthetases | Acylation
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86. Full Text Glyceraldehyde 3-phosphate dehydrogenase negatively regulates human immunodeficiency virus type 1 infection
by Kishimoto, Naoki and Onitsuka, Ayano and Kido, Keishi and Takamune, Nobutoki and Shoji, Shozo and Misumi, Shogo
Retrovirology, ISSN 1742-4690, 12/2012, Volume 9, Issue 1, pp. 107 - 107
Background: Host proteins are incorporated inside human immunodeficiency virus type 1 (HIV-1) virions during assembly and can either positively or negatively... 
Glyceraldehyde 3-phosphate dehydrogenase | Human immunodeficiency virus type 1 | Lysyl-tRNA synthetase | tRNALys3 | FUNCTIONAL DIVERSITY | tRNA(Lys3) | 2-DIMENSIONAL GEL-ELECTROPHORESIS | HIV-1 VIRIONS | CYCLOPHILIN-A | FLIGHT MASS-SPECTROMETRY | VIROLOGY | TRANSFER-RNA SYNTHETASE | CELLULAR-PROTEINS | ASSOCIATION | PROTEOMICS | Cell Line | HIV-1 - physiology | Isoenzymes | Models, Biological | Humans | Virion - physiology | Lysine-tRNA Ligase - metabolism | Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism | Virus Assembly | RNA, Transfer, Lys - metabolism | Phosphates | Genetic transcription | HIV (Viruses) | Monosaccharides | Infection | Ligases | Analysis | Packaging | DNA polymerases | Oxidoreductases | Health aspects | Mass spectrometry | Molybdenum alloys | Sugars | Biotechnology industry | Transfer RNA | Immunoprecipitation | RNA-directed DNA polymerase | Gel electrophoresis | RNA-mediated interference | Antibodies | Reverse transcription | Mass spectroscopy | Defense mechanisms | Life cycle | Allosteric properties | Gag protein | Infectivity | Virions | Peripheral blood mononuclear cells | Glyceraldehyde-3-phosphate dehydrogenase | Replication | Isoelectric points
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87. Full Text The T box regulatory element controlling expression of the class i lysyl-tRNA synthetase of Bacillus cereus strain 14579 is functional and can be partially induced by reduced charging of asparaginyl-tRNAAsn
by Foy, Niall and Jester, Brian and Conant, Gavin C and Devine, Kevin M
BMC Microbiology, ISSN 1471-2180, 2010, Volume 10, Issue 1, pp. 196 - 196
Lysyl-tRNA synthetase (LysRS) is unique within the aminoacyl-tRNA synthetase family in that both class I (LysRS1) and class II (LysRS2) enzymes exist. LysRS1... 
Amino Acid Sequence | Lysine-tRNA Ligase - genetics | Bacillus cereus - metabolism | Bacterial Proteins - chemistry | Bacterial Proteins - genetics | Molecular Sequence Data | Bacillus cereus - enzymology | RNA, Transfer, Asn - metabolism | Gene Expression Regulation, Enzymologic | Sequence Alignment | Bacillus cereus - genetics | Regulatory Elements, Transcriptional | Bacillus cereus - chemistry | RNA, Transfer, Amino Acyl - metabolism | Bacterial Proteins - metabolism | Lysine-tRNA Ligase - metabolism | Lysine-tRNA Ligase - chemistry
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88. Suppression of lysyl-tRNA synthetase, KRS, causes incomplete epithelial-mesenchymal transition and ineffective cell‑extracellular matrix adhesion for migration
by Nam, Seo Hee and Kang, Minkyung and Ryu, Jihye and Kim, Hye-Jin and Kim, Doyeun and Kim, Dae Gyu and Kwon, Nam Hoon and Kim, Sunghoon and Lee, Jung Weon
International journal of oncology, 04/2016, Volume 48, Issue 4, p. 1553
The cell-adhesion properties of cancer cells can be targeted to block cancer metastasis. Although cytosolic lysyl-tRNA synthetase (KRS) functions in protein... 
Focal Adhesion Protein-Tyrosine Kinases - genetics | Extracellular Matrix - genetics | Lysine-tRNA Ligase - genetics | Neoplasms - genetics | Signal Transduction | HCT116 Cells | Humans | Epithelial-Mesenchymal Transition | Lysine-tRNA Ligase - metabolism | Neoplasms - pathology | Cell Adhesion | Cell Movement
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89. Full Text The Tandem PDZ Protein Syntenin Interacts with the Aminoacyl tRNA Synthetase Complex in a Lysyl-tRNA Synthetase-Dependent Manner
by Meerschaert, Kris and Remue, Eline and De Ganck, Ariane and Staes, An and Boucherie, Ciska and Gevaert, Kris and Vandekerckhove, Joël and Kleiman, Lawrence and Gettemans, Jan
Journal of Proteome Research, ISSN 1535-3893, 11/2008, Volume 7, Issue 11, pp. 4962 - 4973
Syntenin-1 is a tandem PDZ protein that binds a diverse array of signaling molecules that are often associated with cell adhesion and intracellular... 
Syntenin | Signal transduction | tRNA synthetase | Functional proteomics | PDZ | Syntenins - genetics | Syntenins - metabolism | Cell Line | Point Mutation | Humans | Glutathione Transferase - metabolism | Lysine-tRNA Ligase - metabolism | Kidney - cytology | Proteomics - methods | Recombinant Fusion Proteins - metabolism
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90. Full Text Ability of wild-type and mutant lysyl-tRNA synthetase to facilitate tRNA(Lys) incorporation into human immunodeficiency virus type 1
by Cen, S and Javanbakht, H and Niu, MJ and Kleiman, L
JOURNAL OF VIROLOGY, ISSN 0022-538X, 02/2004, Volume 78, Issue 3, pp. 1595 - 1601
The major human tRNA(Lys) isoacceptors, tRNA(1,2)(Lys) and tRNA(3)(Lys), are selectively packaged into human immunodeficiency virus type 1 (HIV-1) during... 
DOMAIN | VIROLOGY | PARTICLES | REVERSE TRANSCRIPTION | VIRAL INFECTIVITY | TRNA(LYS) | PR160GAG-POL | ANTICODON | AMINOACYLATION | PRIMER TRANSFER-RNAS | BINDING | Cytoplasm - enzymology | HIV-1 - metabolism | Lysine-tRNA Ligase - genetics | Humans | Cercopithecus aethiops | HIV-1 - genetics | Virion - metabolism | Virus Assembly | Animals | Transfection | Plasmids | HIV-1 - enzymology | Lysine-tRNA Ligase - metabolism | Mutation | COS Cells | RNA, Transfer, Lys - metabolism
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91. Full Text Nonorthologous Replacement of Lysyl-tRNA Synthetase Prevents Addition of Lysine Analogues to the Genetic Code
by Brian C. Jester and Jeffrey D. Levengood and Hervé Roy and Michael Ibba and Kevin M. Devine
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 11/2003, Volume 100, Issue 24, pp. 14351 - 14356
Insertion of lysine during protein synthesis depends on the enzyme lysyl-tRNA synthetase (LysRS), which exists in two unrelated forms, LysRS1 and LysRS2.... 
Genetic code | Enzymes | Biological Sciences | Cell growth | RNA | Plasmids | Genes | Amino acids | Bacteria | Chromosomes | Transfer RNA | ORIGINS | ACID | RECOGNITION | BACILLUS-SUBTILIS | THIALYSINE UTILIZATION | BIOSYNTHESIS | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI K-12 | GROWTH | CLASS-I | THIOSINE-RESISTANT MUTANTS | Cysteine - analogs & derivatives | Genes, Bacterial | Lysine - analogs & derivatives | Lysine-tRNA Ligase - genetics | Genetic Code | Species Specificity | Isoenzymes - genetics | Genomics | Enzyme Inhibitors - pharmacology | Bacillus subtilis - enzymology | Bacillus subtilis - genetics | Borrelia burgdorferi - enzymology | Lysine-tRNA Ligase - antagonists & inhibitors | Borrelia burgdorferi - genetics | Isoenzymes - metabolism | Cysteine - pharmacology | Lysine-tRNA Ligase - metabolism | Lysine - metabolism | Drug Resistance, Bacterial - genetics | RNA, Transfer, Lys - metabolism | Isoenzymes - antagonists & inhibitors | Bacillus subtilis - drug effects | Borrelia burgdorferi - drug effects | Evolution, Molecular | Research | S-(2-Aminoethyl)-L-cysteine
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92. Full Text The Adaptor hypothesis revisited
by Ibba, Michael and Becker, Hubert D and Stathopoulos, Constantinos and Tumbula, Debra L and Söll, Dieter
Trends in Biochemical Sciences, ISSN 0968-0004, 2000, Volume 25, Issue 7, pp. 311 - 316
As originally postulated in Crick's Adaptor hypothesis, the faithful synthesis of proteins from messenger RNA is dependent on the presence of perfectly... 
Adaptor | Aminoacyl-tRNA | Evolution | Translation | tRNA | Protein synthesis | GENETIC-CODE | COMPLETE GENOME SEQUENCE | EVOLUTION | AMINO-ACIDS | BIOSYNTHESIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | TRANSAMIDATION | TRANSLATION | AMINOACYLATION | TRANSFER-RNA SYNTHETASES | AMIDOTRANSFERASE | Amino Acyl-tRNA Synthetases - genetics | Archaeal Proteins - metabolism | Protein Biosynthesis | Lysine-tRNA Ligase - classification | RNA, Transfer, Amino Acid-Specific - genetics | RNA, Transfer, Amino Acid-Specific - metabolism | Substrate Specificity | Phylogeny | RNA, Transfer, Amino Acid-Specific - biosynthesis | Archaeal Proteins - genetics | Lysine-tRNA Ligase - metabolism | Models, Genetic | Amino Acyl-tRNA Synthetases - metabolism | Amino Acyl-tRNA Synthetases - classification | Evolution, Molecular | Physiological aspects | Protein biosynthesis | Messenger RNA | Research | Aminoacyl-tRNA synthetases | Gene expression | aminoacyl-tRNA
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93. Full Text Class I and class II lysyl‐tRNA synthetase mutants and the genetic encoding of pyrrolysine in Methanosarcina spp
by Mahapatra, Anirban and Srinivasan, Gayathri and Richter, Kerstin B and Meyer, Andrew and Lienard, Tanja and Zhang, Jun Kai and Zhao, Gang and Kang, Patrick T and Chan, Michael and Gottschalk, Gerhard and Metcalf, William W and Krzycki, Joseph A
Molecular Microbiology, ISSN 0950-382X, 06/2007, Volume 64, Issue 5, pp. 1306 - 1318
Summary Methanosarcina spp. begin methanogenesis from methylamines with methyltransferases made via the translation of UAG as pyrrolysine. In vitro evidence... 
ACETIVORANS | AMINO-ACID | CODE | COMPLETE GENOME SEQUENCE | M METHYL TRANSFER | ARCHAEA | RECOGNITION | METHYLTRANSFERASES | BIOCHEMISTRY & MOLECULAR BIOLOGY | BARKERI | MICROBIOLOGY | CORRINOID PROTEIN | Lysine - analogs & derivatives | Lysine-tRNA Ligase - genetics | Methanosarcina - enzymology | Lysine - genetics | Methanosarcina - genetics | Lysine-tRNA Ligase - classification | Lysine-tRNA Ligase - metabolism | Lysine - metabolism | Mutation | Chemoautotrophic Growth | Gene mutations | Genetic research
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94. Full Text Inhibition of Cellular HIV-1 Protease Activity by Lysyl-tRNA Synthetase
by Fei Guo and Juliana Gabor and Shan Cen and Kimberly Hu and Andrew J. Mouland and Lawrence Kleiman
Journal of Biological Chemistry, ISSN 0021-9258, 07/2005, Volume 280, Issue 28, pp. 26018 - 26023
During early assembly of human immunodeficiency virus type 1 (HIV-1), an assembly complex is formed, the components of which include genomic RNA, Gag, GagPol,... 
Protein Structure, Tertiary | Cell Line | Green Fluorescent Proteins - metabolism | Humans | Cytoplasm - metabolism | RNA, Messenger - metabolism | Plasmids - metabolism | Blotting, Western | Gene Products, gag - metabolism | HIV Protease Inhibitors - pharmacology | HIV Reverse Transcriptase - metabolism | Transfection | Virus Replication | Lysine-tRNA Ligase - metabolism | Lysine-tRNA Ligase - chemistry | Energy Transfer | Fusion Proteins, gag-pol - metabolism | HIV Protease - metabolism | Lysine - chemistry | RNA, Small Interfering - metabolism
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95. Full Text Mechanisms of Resistance to an Amino Acid Antibiotic That Targets Translation
by Ataide, Sandro F and Wilson, Sharnise N and Dang, Sandy and Rogers, Theresa E and Roy, Bappaditya and Banerjee, Rajat and Henkin, Tina M and Ibba, Michael
ACS Chemical Biology, ISSN 1554-8929, 12/2007, Volume 2, Issue 12, pp. 819 - 827
Structural and functional diversity among the aminoacyl-tRNA synthetases prevent infiltration of the genetic code by noncognate amino acids. To explore whether... 
PROTEIN | TRANSFER-RNA SYNTHETASE | BACILLUS-SUBTILIS | ACTIVE-SITE | LYSINE BIOSYNTHESIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | GENES | CLASS-I | BINDING | EXPRESSION | Cysteine - analogs & derivatives | Lysine-tRNA Ligase - genetics | Escherichia coli - enzymology | Microbial Viability - drug effects | Escherichia coli - drug effects | Enzyme Inhibitors - pharmacology | Cysteine - chemistry | Escherichia coli - cytology | Lysine-tRNA Ligase - antagonists & inhibitors | Escherichia coli - genetics | Anti-Bacterial Agents - chemistry | Enzyme Inhibitors - chemistry | Cysteine - pharmacology | Lysine-tRNA Ligase - metabolism | Protein Biosynthesis - drug effects | Anti-Bacterial Agents - pharmacology | Drug Resistance, Bacterial - drug effects | Binding Sites
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96. Full Text Active Site of Lysyl-tRNA Synthetase:  Structural Studies of the Adenylation Reaction
by Desogus, Gianluigi and Todone, Flavia and Brick, Peter and Onesti, Silvia
Biochemistry, ISSN 0006-2960, 07/2000, Volume 39, Issue 29, pp. 8418 - 8425
Aminoacyl-tRNA synthetases play a key role in protein biosynthesis by catalyzing the specific aminoacylation of tRNA. The energy required for the formation of... 
ACTIVATION | AMINOACYLATION REACTION | CONFORMATIONAL-CHANGES | RECOGNITION | STRANDED-DNA-BINDING | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | CLASS-I | THERMUS-THERMOPHILUS | TRANSFER-RNA-SYNTHETASE | Amino Acyl-tRNA Synthetases - genetics | Recombinant Proteins - metabolism | Amino Acid Sequence | Lysine-tRNA Ligase - genetics | Catalytic Domain | Escherichia coli - enzymology | Models, Molecular | Molecular Sequence Data | Recombinant Proteins - chemistry | Crystallography, X-Ray | Recombinant Proteins - genetics | Static Electricity | Adenosine Triphosphate - analogs & derivatives | Sequence Homology, Amino Acid | Escherichia coli - genetics | Adenosine Triphosphate - metabolism | Ligands | Lysine-tRNA Ligase - metabolism | Protein Conformation | Lysine - metabolism | Lysine-tRNA Ligase - chemistry | Ligases | Escherichia coli | Physiological aspects | Biosynthesis | Research | Cytochemistry | Adenylic acid | Adenosine triphosphate | Binding sites (Biochemistry)
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97. Full Text Effect of altering the tRNA(3)(Lys) concentration in human immunodeficiency virus type 1 upon its annealing to viral RNA, GagPol incorporation, and viral infectivity
by Gabor, J and Cen, S and Javanbakht, H and Niu, MJ and Kleiman, L
JOURNAL OF VIROLOGY, ISSN 0022-538X, 09/2002, Volume 76, Issue 18, pp. 9096 - 9102
Human immunodeficiency virus type 1 (HIV-1) uses tRNA(3)(Lys) a primer for reverse transcription and, during viral assembly, this tRNA is selectively packaged... 
PRIMER TRANSFER-RNA | WILD-TYPE | MUTANT | VIROLOGY | INITIATION | REVERSE TRANSCRIPTION | BINDING-SITE COMPLEMENTARY | MURINE LEUKEMIA-VIRUS | DNA-SYNTHESIS | GENOMIC RNA | NUCLEOTIDE-SEQUENCE | HIV-1 - metabolism | Lysine-tRNA Ligase - genetics | HIV-1 - pathogenicity | Humans | HIV-1 - genetics | Virus Assembly | RNA, Transfer, Lys - genetics | Animals | Transfection | Plasmids | Lysine-tRNA Ligase - metabolism | RNA, Viral - metabolism | HeLa Cells | Fusion Proteins, gag-pol - metabolism | COS Cells | RNA, Transfer, Lys - metabolism
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98. Full Text Discrimination of Cognate and Noncognate Substrates at the Active Site of Class II Lysyl-tRNA Synthetase
by Ataide, Sandro F and Ibba, Michael
Biochemistry, ISSN 0006-2960, 09/2004, Volume 43, Issue 37, pp. 11836 - 11841
Within the two unrelated aminoacyl-tRNA synthetase classes, lysyl-tRNA synthetase (LysRS) is the only example known to exist in both classes. To probe the role... 
AMINOACYLATION REACTION | RECOGNITION | BINDING | BIOCHEMISTRY & MOLECULAR BIOLOGY | Lysine-tRNA Ligase - genetics | Models, Molecular | Substrate Specificity | Escherichia coli Proteins - metabolism | Point Mutation | Adenosine Triphosphate - metabolism | Escherichia coli Proteins - genetics | Protein Binding | Lysine-tRNA Ligase - metabolism | Lysine - metabolism | Lysine-tRNA Ligase - chemistry | Escherichia coli Proteins - chemistry | Lysine - chemistry | Binding Sites | Research | Structure | Lysine | Transfer RNA | Binding sites (Biochemistry)
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99. Full Text Viral Hijacking of Mitochondrial Lysyl-tRNA Synthetase
by Monika Kaminska and Vyacheslav Shalak and Mathilde Francin and Marc Mirande
Journal of Virology, ISSN 0022-538X, 01/2007, Volume 81, Issue 1, pp. 68 - 73
Article Usage Stats Services JVI Citing Articles Google Scholar PubMed Related Content Social Bookmarking CiteULike Delicious Digg Facebook Google+ Mendeley... 
WILD-TYPE | MUTANT | CELLS | COMPLEX | VIROLOGY | LEUCYL-TRANSFER RNA | REVERSE TRANSCRIPTION | ESCHERICHIA-COLI | IMMUNODEFICIENCY-VIRUS TYPE-1 | TRNA(LYS) INCORPORATION | HIV-1 GAG | Reverse Transcription - physiology | Amino Acid Sequence | Alternative Splicing | Humans | Antibodies | Molecular Sequence Data | Antibodies, Monoclonal | Virion - metabolism | Virus Assembly | Sequence Alignment | HIV-1 - physiology | Mitochondrial Proteins - metabolism | Lysine-tRNA Ligase - metabolism | HeLa Cells | Genome and Regulation of Viral Gene Expression
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100. Full Text Functional Dissection of the Eukaryotic-specific tRNA-interacting Factor of Lysyl-tRNA Synthetase
by Mathilde Francin and Marc Mirande
Journal of Biological Chemistry, ISSN 0021-9258, 01/2003, Volume 278, Issue 3, pp. 1472 - 1479
In the cytoplasm of higher eukaryotic cells, aminoacyl-tRNA synthetases (aaRSs) have polypeptide chain extensions appended to conventional prokaryotic-like... 
CONFORMATIONAL-CHANGES | N-TERMINAL EXTENSION | CRYSTAL-STRUCTURE | REVERSE TRANSCRIPTION | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | IMMUNODEFICIENCY-VIRUS TYPE-1 | BINDING DOMAIN | SECONDARY STRUCTURE | SACCHAROMYCES-CEREVISIAE | TRANSFER-RNA-SYNTHETASE | Sequence Homology, Amino Acid | Amino Acid Sequence | Lysine-tRNA Ligase - genetics | Point Mutation | Cricetinae | Animals | Molecular Sequence Data | Lysine-tRNA Ligase - metabolism | Lysine-tRNA Ligase - chemistry | RNA - metabolism
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