Compounds > asparagine

asparagine and cytochrome c-t

asparagine has been researched along with cytochrome c-t in 6 studies

Research

Studies (6)

Timeframe	Studies, this research(%)	All Research%
pre-1990	1 (16.67)	18.7374
1990's	1 (16.67)	18.2507
2000's	4 (66.67)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Das, G; Hickey, DR; McLendon, D; McLendon, G; Sherman, F	1
Alcazar-Roman, L; Doyle, DF; Parikh, S; Pielak, GJ; Waldner, JC	1
Bowler, BE; Kristinsson, R	1
Baddam, S; Bowler, BE	1
Bowman, MJ; Cournoyer, JJ; Lin, C; O'Connor, PB	1
Gurel, E; Mandaci, S; Ozturk, M; Watmough, NJ	1

Other Studies

6 other study(ies) available for asparagine and cytochrome c-t

Article	Year
Dramatic thermostabilization of yeast iso-1-cytochrome c by an asparagine----isoleucine replacement at position 57. Proceedings of the National Academy of Sciences of the United States of America, 1989, Volume: 86, Issue:2 Topics: Amino Acid Sequence; Asparagine; Base Sequence; Cytochrome c Group; Cytochromes c; DNA, Fungal; Hot Temperature; Isoleucine; Molecular Sequence Data; Mutation; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins	1989
Changing the transition state for protein (Un) folding. Biochemistry, 1996, Jun-11, Volume: 35, Issue:23 Topics: Asparagine; Calorimetry; Circular Dichroism; Cytochrome c Group; Cytochromes c; Genetic Variation; Guanidine; Guanidines; Isoleucine; Kinetics; Oxidation-Reduction; Protein Conformation; Protein Denaturation; Protein Folding; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Sensitivity and Specificity; Thermodynamics	1996
Communication of stabilizing energy between substructures of a protein. Biochemistry, 2005, Feb-22, Volume: 44, Issue:7 Topics: Amino Acid Substitution; Asparagine; Cytochromes c; Enzyme Stability; Genetic Variation; Guanidine; Hydrogen-Ion Concentration; Isoenzymes; Leucine; Models, Molecular; Mutagenesis, Site-Directed; Protein Conformation; Protein Denaturation; Protein Folding; Saccharomyces cerevisiae Proteins; Temperature; Thermodynamics	2005
Mutation of asparagine 52 to glycine promotes the alkaline form of iso-1-cytochrome c and causes loss of cooperativity in acid unfolding. Biochemistry, 2006, Apr-11, Volume: 45, Issue:14 Topics: Amino Acid Sequence; Asparagine; Chromatography, High Pressure Liquid; Cytochromes c; Glycine; Hydrogen-Ion Concentration; Isoenzymes; Mutagenesis, Site-Directed; Protein Denaturation; Protein Folding; Saccharomyces cerevisiae Proteins; Thermodynamics	2006
Quantitating the relative abundance of isoaspartyl residues in deamidated proteins by electron capture dissociation. Journal of the American Society for Mass Spectrometry, 2007, Volume: 18, Issue:1 Topics: Amino Acid Sequence; Asparagine; Cytochromes c; Deamination; Isoaspartic Acid; Molecular Sequence Data; Peptides; Protein Isoforms; Spectroscopy, Fourier Transform Infrared	2007
Site-directed mutagenesis of five conserved residues of subunit i of the cytochrome cbb3 oxidase in Rhodobacter capsulatus. Journal of biochemistry and molecular biology, 2007, Sep-30, Volume: 40, Issue:5 Topics: Amino Acid Sequence; Amino Acids; Asparagine; Bacterial Proteins; Catalysis; Cytochromes c; Electron Transport Complex IV; Electrophoresis, Polyacrylamide Gel; Heme; Molecular Sequence Data; Mutagenesis, Site-Directed; Protein Subunits; Rhodobacter capsulatus; Sequence Homology, Amino Acid; Serine; Structure-Activity Relationship; Threonine	2007