lysine has been researched along with 8-azidoadenosine 5'-triphosphate in 10 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 1 (10.00) | 18.7374 |
| 1990's | 4 (40.00) | 18.2507 |
| 2000's | 5 (50.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Julin, DA; Korangy, F | 1 |
| Fearnley, IM; Hollemans, M; Runswick, MJ; Walker, JE | 1 |
| Carson, MR; Travis, SM; Welsh, MJ | 1 |
| Kim, IY; Stadtman, TC; Veres, Z | 1 |
| Alexandrov, K; Carrera, AC; Roberts, TM | 1 |
| Almquist, KC; Cole, SP; Cui, HR; Deeley, RG; Gao, M; Grant, CE; Loe, DW | 1 |
| Aleksandrov, A; Aleksandrov, L; Chang , X; Mengos, A; Riordan, JR | 1 |
| Cresswell, P; Gupta, SS; Hewitt, EW; Karttunen, JT; Lehner, PJ | 1 |
| Bagley, CJ; D'Andrea, RJ; Darrow, AL; Derian, CK; Moretti, PA; Pitson, SM; Qi, J; Vadas, MA; Wattenberg, BW; Zareie, R; Zebol, JR | 1 |
| Basso, C; Gadsby, DC; Nairn, AC; Vergani, P | 1 |
10 other study(ies) available for lysine and 8-azidoadenosine 5'-triphosphate
| Article | Year |
|---|---|
Alteration by site-directed mutagenesis of the conserved lysine residue in the ATP-binding consensus sequence of the RecD subunit of the Escherichia coli RecBCD enzyme.
Topics: Adenosine Triphosphate; Affinity Labels; Amino Acid Sequence; Azides; Base Sequence; Binding Sites; Escherichia coli; Escherichia coli Proteins; Exodeoxyribonuclease V; Exodeoxyribonucleases; Genes, Bacterial; Kinetics; Lysine; Macromolecular Substances; Molecular Sequence Data; Mutagenesis, Site-Directed; Oligodeoxyribonucleotides; Plasmids; Recombinant Proteins; Restriction Mapping | 1992 |
The sites of labeling of the beta-subunit of bovine mitochondrial F1-ATPase with 8-azido-ATP.
Topics: Adenosine Triphosphate; Amino Acid Sequence; Animals; Azides; Binding Sites; Cattle; Isoleucine; Lysine; Macromolecular Substances; Mitochondria, Heart; Proton-Translocating ATPases; Trypsin; Tyrosine | 1983 |
The two nucleotide-binding domains of cystic fibrosis transmembrane conductance regulator (CFTR) have distinct functions in controlling channel activity.
Topics: 3T3 Cells; Adenosine Triphosphate; Adenylyl Imidodiphosphate; Amino Acid Sequence; Animals; Azides; Binding Sites; Chloride Channels; Conserved Sequence; Cyclic AMP-Dependent Protein Kinases; Cystic Fibrosis Transmembrane Conductance Regulator; Genetic Variation; HeLa Cells; Humans; Ion Channel Gating; Lysine; Membrane Potentials; Membrane Proteins; Mice; Molecular Sequence Data; Mutagenesis, Site-Directed; Patch-Clamp Techniques; Phosphorylation; Point Mutation; Recombinant Proteins; Transfection | 1995 |
Biochemical analysis of Escherichia coli selenophosphate synthetase mutants. Lysine 20 is essential for catalytic activity and cysteine 17/19 for 8-azido-ATP derivatization.
Topics: Adenosine Triphosphate; Affinity Labels; Amino Acid Sequence; Azides; Bacterial Proteins; Base Sequence; Catalysis; Cysteine; Drosophila Proteins; Escherichia coli; Lysine; Metals; Molecular Sequence Data; Mutagenesis, Site-Directed; Phosphotransferases; Substrate Specificity | 1993 |
The conserved lysine of the catalytic domain of protein kinases is actively involved in the phosphotransfer reaction and not required for anchoring ATP.
Topics: Adenosine Triphosphate; Amino Acid Sequence; Azides; Binding Sites; Lymphocyte Specific Protein Tyrosine Kinase p56(lck); Lysine; Molecular Probes; Molecular Sequence Data; Mutagenesis, Site-Directed; Phosphates; Phosphorylation; Protein-Tyrosine Kinases | 1993 |
Comparison of the functional characteristics of the nucleotide binding domains of multidrug resistance protein 1.
Topics: Adenosine Triphosphate; Animals; ATP Binding Cassette Transporter, Subfamily B, Member 1; Azides; Baculoviridae; Cell Line; Immunoblotting; Insecta; Leukotriene C4; Lysine; Mutagenesis, Site-Directed; Nucleotides; Plasmids; Protein Binding; Protein Structure, Tertiary; Time Factors; Vanadates | 2000 |
Differential interactions of nucleotides at the two nucleotide binding domains of the cystic fibrosis transmembrane conductance regulator.
Topics: Adenosine Triphosphate; Adenylyl Imidodiphosphate; Amino Acid Substitution; Animals; Azides; Binding Sites; Cell Line; Cystic Fibrosis Transmembrane Conductance Regulator; Humans; Ion Channel Gating; Kinetics; Lysine; Models, Molecular; Mutagenesis, Site-Directed; Photoaffinity Labels; Protein Structure, Secondary; Recombinant Proteins; Transfection; Trypsin; Vanadates | 2001 |
Distinct functions and cooperative interaction of the subunits of the transporter associated with antigen processing (TAP).
Topics: Adenosine Triphosphate; Amino Acid Substitution; Animals; ATP Binding Cassette Transporter, Subfamily B, Member 2; ATP Binding Cassette Transporter, Subfamily B, Member 3; ATP-Binding Cassette Transporters; Azides; Binding Sites; Cell Line; HeLa Cells; Humans; Lysine; Major Histocompatibility Complex; Mutagenesis, Site-Directed; Peptide Fragments; Photoaffinity Labels; Protein Subunits; Recombinant Proteins; Transfection | 2001 |
The nucleotide-binding site of human sphingosine kinase 1.
Topics: Adenosine; Adenosine Triphosphate; Affinity Labels; Alanine; Amino Acid Motifs; Amino Acid Sequence; Animals; Azides; Baculoviridae; Binding Sites; Blotting, Western; Calmodulin; Catalysis; Catalytic Domain; Cell Line; DNA, Complementary; Gene Deletion; Humans; Insecta; Kinetics; Lysine; Mass Spectrometry; Molecular Sequence Data; Mutagenesis, Site-Directed; Mutation; Nucleotides; Phosphotransferases (Alcohol Group Acceptor); Photoaffinity Labels; Protein Binding; Protein Folding; Protein Structure, Tertiary; Recombinant Proteins; Sequence Homology, Amino Acid; Substrate Specificity; Transfection | 2002 |
Prolonged nonhydrolytic interaction of nucleotide with CFTR's NH2-terminal nucleotide binding domain and its role in channel gating.
Topics: Adenosine Diphosphate; Adenosine Triphosphate; Alanine; Animals; Azides; Cell Line; Chloride Channels; Cystic Fibrosis Transmembrane Conductance Regulator; Humans; Ion Channel Gating; Kinetics; Lysine; Mutation; Oocytes; Osmolar Concentration; Peptide Fragments; Phosphorylation; Protein Isoforms; Protein Structure, Tertiary; Temperature; Time Factors; Vanadates; Xenopus laevis | 2003 |