asparagine and guanosine diphosphate

asparagine has been researched along with guanosine diphosphate in 12 studies

Research

Studies (12)

TimeframeStudies, this research(%)All Research%
pre-19902 (16.67)18.7374
1990's3 (25.00)18.2507
2000's6 (50.00)29.6817
2010's1 (8.33)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Balaji, PV; Rao, VS1
Cooper, GM; Feig, LA1
Hwang, YW; Miller, DL1
Farrar, CT; Halkides, CJ; Larsen, RG; Redfield, AG; Singel, DJ1
Clark, BF; Knudsen, CR; Nautrup Pedersen, G; Rattenborg, T1
Dumas, JJ; Lambright, DG; Lietzke, SE; Zhu, Z1
Brito, M; Guzmán, L; Hinrichs, MV; Olate, J; Romo, X; Soto, X1
Cerione, RA; Hahn, K; Nolbant, P; Tu, SS; Wu, WJ; Yang, W1
Cooperman, BS; Kashlan, OB1
Bos, JL; Rehmann, H1
Arnold, E; Ding, J; Guan, K; Li, S; Li, Y; Xu, X; Yu, Y1
Garcia-Diaz, M; Nassar, N; Singh, K1

Other Studies

12 other study(ies) available for asparagine and guanosine diphosphate

ArticleYear
Computer modeling studies on the subsite interactions of ribonuclease T1.
    Journal of biomolecular structure & dynamics, 1992, Volume: 9, Issue:5

    Topics: Asparagine; Binding Sites; Computer Simulation; Dinucleoside Phosphates; Exoribonucleases; Guanosine Diphosphate; Guanosine Monophosphate; Tyrosine

1992
Inhibition of NIH 3T3 cell proliferation by a mutant ras protein with preferential affinity for GDP.
    Molecular and cellular biology, 1988, Volume: 8, Issue:8

    Topics: Animals; Asparagine; Cell Division; Cells, Cultured; Cloning, Molecular; Guanine Nucleotides; Guanosine Diphosphate; Guanosine Triphosphate; Kinetics; Membrane Proteins; Mice; Mice, Inbred Strains; Mutation; Protein Binding; Proto-Oncogene Proteins; Proto-Oncogene Proteins p21(ras); Serine; Transfection

1988
A mutation that alters the nucleotide specificity of elongation factor Tu, a GTP regulatory protein.
    The Journal of biological chemistry, 1987, Sep-25, Volume: 262, Issue:27

    Topics: Asparagine; Aspartic Acid; Cloning, Molecular; Escherichia coli; Genes; Genes, Bacterial; Guanine Nucleotides; Guanosine Diphosphate; Guanosine Triphosphate; Mutation; Peptide Elongation Factor Tu; Plasmids; Protein Binding

1987
Characterization of the active site of p21 ras by electron spin-echo envelope modulation spectroscopy with selective labeling: comparisons between GDP and GTP forms.
    Biochemistry, 1994, Apr-05, Volume: 33, Issue:13

    Topics: Asparagine; Aspartic Acid; Binding Sites; Electron Spin Resonance Spectroscopy; GTP Phosphohydrolases; GTP-Binding Proteins; Guanosine Diphosphate; Guanosine Triphosphate; Humans; Ligands; Phosphates; Proto-Oncogene Proteins p21(ras); Recombinant Proteins; Threonine

1994
Contribution of Arg288 of Escherichia coli elongation factor Tu to translational functionality.
    European journal of biochemistry, 1997, Oct-15, Volume: 249, Issue:2

    Topics: Amino Acid Sequence; Amino Acid Substitution; Arginine; Asparagine; Binding Sites; Conserved Sequence; Escherichia coli; GTP Phosphohydrolase-Linked Elongation Factors; Guanosine Diphosphate; Guanosine Triphosphate; Hydrogen Bonding; Kinetics; Lysine; Models, Molecular; Mutagenesis, Site-Directed; Peptide Elongation Factor Tu; Protein Conformation; Recombinant Proteins; Ribosomes; RNA, Transfer, Phe; Thermus

1997
A helical turn motif in Mss4 is a critical determinant of Rab binding and nucleotide release.
    Biochemistry, 2001, Mar-13, Volume: 40, Issue:10

    Topics: Alanine; Amino Acid Sequence; Amino Acid Substitution; Animals; Asparagine; Aspartic Acid; Conserved Sequence; Evolution, Molecular; Guanine Nucleotide Exchange Factors; Guanosine Diphosphate; Helix-Turn-Helix Motifs; Kinetics; Mice; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Protein Binding; Protein Structure, Tertiary; Proteins; rab GTP-Binding Proteins; Rats; Sequence Homology, Amino Acid; Serine

2001
S111N mutation in the helical domain of human Gs(alpha) reduces its GDP/GTP exchange rate.
    Journal of cellular biochemistry, 2002, Volume: 85, Issue:3

    Topics: Adenylyl Cyclases; Aluminum Compounds; Amino Acid Substitution; Asparagine; Fluorides; GTP-Binding Protein alpha Subunits, Gs; GTP-Binding Proteins; Guanosine 5'-O-(3-Thiotriphosphate); Guanosine Diphosphate; Guanosine Triphosphate; Humans; Models, Molecular; Point Mutation; Protein Conformation; Protein Structure, Secondary; Protein Structure, Tertiary; Receptors, Cell Surface; Serine; Trypsin

2002
Antiapoptotic Cdc42 mutants are potent activators of cellular transformation.
    Biochemistry, 2002, Oct-15, Volume: 41, Issue:41

    Topics: 3T3 Cells; Amino Acid Substitution; Animals; Apoptosis; Asparagine; Aspartic Acid; cdc42 GTP-Binding Protein; Cell Division; Cell Transformation, Neoplastic; COS Cells; Guanosine Diphosphate; Guanosine Triphosphate; Humans; Mice; Mutagenesis, Site-Directed; Polymerase Chain Reaction; Protein Binding; Trans-Activators; Transfection

2002
Comprehensive model for allosteric regulation of mammalian ribonucleotide reductase: refinements and consequences.
    Biochemistry, 2003, Feb-18, Volume: 42, Issue:6

    Topics: Adenosine Triphosphate; Allosteric Regulation; Animals; Asparagine; Aspartic Acid; Cytidine Diphosphate; Deoxyadenine Nucleotides; Dimerization; Enzyme Activation; Guanosine Diphosphate; Kinetics; Light; Magnesium; Mice; Models, Chemical; Mutagenesis, Site-Directed; Protein Subunits; Recombinant Proteins; Ribonucleoside Diphosphate Reductase; Ribonucleotide Reductases; Scattering, Radiation; Substrate Specificity; Thymine Nucleotides; Tumor Cells, Cultured

2003
Signal transduction: thumbs up for inactivation.
    Nature, 2004, May-13, Volume: 429, Issue:6988

    Topics: Asparagine; Binding Sites; Catalytic Domain; GTPase-Activating Proteins; Guanosine Diphosphate; Guanosine Triphosphate; Hydrolysis; rap1 GTP-Binding Proteins; Signal Transduction

2004
Structural basis for the unique biological function of small GTPase RHEB.
    The Journal of biological chemistry, 2005, Apr-29, Volume: 280, Issue:17

    Topics: Amino Acid Sequence; Arginine; Asparagine; Binding Sites; Catalytic Domain; Cell Proliferation; Crystallography, X-Ray; Databases, Protein; GTP Phosphohydrolases; Guanosine Diphosphate; Guanosine Triphosphate; Humans; Hydrolysis; Magnesium; Models, Molecular; Molecular Sequence Data; Monomeric GTP-Binding Proteins; Neuropeptides; Protein Conformation; Protein Kinases; Protein Structure, Secondary; Protein Structure, Tertiary; Ras Homolog Enriched in Brain Protein; ras Proteins; Repressor Proteins; Sequence Homology, Amino Acid; TOR Serine-Threonine Kinases; Tuberous Sclerosis; Tuberous Sclerosis Complex 1 Protein; Tuberous Sclerosis Complex 2 Protein; Tumor Suppressor Proteins; X-Ray Diffraction

2005
Structure of the dominant negative S17N mutant of Ras.
    Biochemistry, 2010, Mar-09, Volume: 49, Issue:9

    Topics: Amino Acid Substitution; Asparagine; Crystallography, X-Ray; Guanosine Diphosphate; Guanosine Triphosphate; Humans; Magnesium; Models, Molecular; Protein Binding; ras Proteins; Serine; Signal Transduction; Structure-Activity Relationship

2010