Page last updated: 2024-08-17

aspartic acid and s-adenosylhomocysteine

aspartic acid has been researched along with s-adenosylhomocysteine in 10 studies

Research

Studies (10)

TimeframeStudies, this research(%)All Research%
pre-19901 (10.00)18.7374
1990's2 (20.00)18.2507
2000's4 (40.00)29.6817
2010's3 (30.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Barber, JR; Clarke, S1
Aswad, DW; Johnson, BA1
Djordjevic, S; Stock, AM1
Aswad, DW; Schurter, BT1
D'angelo, S; di Carlo, E; Galletti, P; Ingrosso, D; Perna, AF; Zappia, V1
Castaldo, P; Cimmino, A; De Santo, NG; di Carlo, E; Galletti, P; Ingrosso, D; Perna, AF; Zappia, V1
Clarke, S; Farrar, C1
D'Angelo, S; Daniele, L; Galletti, P; MonsurrĂ², MR; Raimo, M; Salvatore, A; Trojsi, F1
Blobel, G; Clarke, SG; Debler, EW; Feng, Y; Jain, K; Stavropoulos, P; Warmack, RA1
Jackman, JE; Krishnamohan, A1

Other Studies

10 other study(ies) available for aspartic acid and s-adenosylhomocysteine

ArticleYear
Inhibition of protein carboxyl methylation by S-adenosyl-L-homocysteine in intact erythrocytes. Physiological consequences.
    The Journal of biological chemistry, 1984, Jun-10, Volume: 259, Issue:11

    Topics: Adenosine; Aspartic Acid; Erythrocyte Membrane; Erythrocytes; Homocysteine; Humans; Membrane Proteins; Methionine; Methylation; Protein D-Aspartate-L-Isoaspartate Methyltransferase; Protein Methyltransferases; Protein Processing, Post-Translational; S-Adenosylhomocysteine; S-Adenosylmethionine

1984
Kinetic properties of bovine brain protein L-isoaspartyl methyltransferase determined using a synthetic isoaspartyl peptide substrate.
    Neurochemical research, 1993, Volume: 18, Issue:1

    Topics: Amino Acid Sequence; Animals; Aspartic Acid; Brain; Cattle; Chromatography, High Pressure Liquid; Kinetics; Methylation; Molecular Sequence Data; Peptides; Protein D-Aspartate-L-Isoaspartate Methyltransferase; Protein Methyltransferases; S-Adenosylhomocysteine; S-Adenosylmethionine; Tritium

1993
Chemotaxis receptor recognition by protein methyltransferase CheR.
    Nature structural biology, 1998, Volume: 5, Issue:6

    Topics: Amino Acid Sequence; Aspartic Acid; Bacterial Proteins; Binding Sites; Chemoreceptor Cells; Chemotaxis; Crystallography, X-Ray; Escherichia coli Proteins; Membrane Proteins; Methyltransferases; Models, Molecular; Molecular Sequence Data; Oligopeptides; Receptors, Amino Acid; Receptors, Cell Surface; S-Adenosylhomocysteine; Salmonella typhimurium

1998
Analysis of isoaspartate in peptides and proteins without the use of radioisotopes.
    Analytical biochemistry, 2000, Jul-01, Volume: 282, Issue:2

    Topics: Aspartic Acid; Chromatography, High Pressure Liquid; Delta Sleep-Inducing Peptide; Methylation; Peptides; Protein Methyltransferases; Proteins; S-Adenosylhomocysteine; S-Adenosylmethionine; Sensitivity and Specificity; Time Factors

2000
Increased methyl esterification of altered aspartyl residues in erythrocyte membrane proteins in response to oxidative stress.
    European journal of biochemistry, 2000, Volume: 267, Issue:14

    Topics: Anion Exchange Protein 1, Erythrocyte; Ankyrins; Antioxidants; Ascorbic Acid; Aspartic Acid; Blood Proteins; Cell Membrane; Cytoskeletal Proteins; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Erythrocytes; Humans; Hydrogen Peroxide; Malondialdehyde; Membrane Proteins; Methemoglobin; Methylation; Models, Biological; Neuropeptides; Oxidants; Oxidative Stress; Oxyhemoglobins; Protein D-Aspartate-L-Isoaspartate Methyltransferase; Protein Methyltransferases; S-Adenosylhomocysteine; S-Adenosylmethionine; tert-Butylhydroperoxide; Time Factors; Vitamin E

2000
Plasma proteins containing damaged L-isoaspartyl residues are increased in uremia: implications for mechanism.
    Kidney international, 2001, Volume: 59, Issue:6

    Topics: Aspartic Acid; Biomarkers; Blood Proteins; Chromatography, High Pressure Liquid; Folic Acid; Hematinics; Homocysteine; Humans; Hyperhomocysteinemia; Methylation; Protein D-Aspartate-L-Isoaspartate Methyltransferase; Protein Methyltransferases; Renal Dialysis; S-Adenosylhomocysteine; Serum Albumin; Uremia

2001
Altered levels of S-adenosylmethionine and S-adenosylhomocysteine in the brains of L-isoaspartyl (D-Aspartyl) O-methyltransferase-deficient mice.
    The Journal of biological chemistry, 2002, Aug-02, Volume: 277, Issue:31

    Topics: Adenosylhomocysteinase; Animals; Aspartic Acid; Brain; Hydrolases; Kinetics; Methionine Adenosyltransferase; Mice; Mice, Knockout; Protein D-Aspartate-L-Isoaspartate Methyltransferase; S-Adenosylhomocysteine; S-Adenosylmethionine; Time Factors

2002
Accumulation of altered aspartyl residues in erythrocyte membrane proteins from patients with sporadic amyotrophic lateral sclerosis.
    Neurochemistry international, 2013, Volume: 63, Issue:6

    Topics: Adult; Aged; Amyotrophic Lateral Sclerosis; Aspartic Acid; Erythrocyte Membrane; Female; Humans; Male; Membrane Proteins; Methionine; Methionine Adenosyltransferase; Middle Aged; Oxidation-Reduction; Oxidative Stress; Protein D-Aspartate-L-Isoaspartate Methyltransferase; Reactive Oxygen Species; S-Adenosylhomocysteine

2013
A glutamate/aspartate switch controls product specificity in a protein arginine methyltransferase.
    Proceedings of the National Academy of Sciences of the United States of America, 2016, Feb-23, Volume: 113, Issue:8

    Topics: Aspartic Acid; Crystallography, X-Ray; Glutamic Acid; Protein Multimerization; Protein Structure, Quaternary; Protein Structure, Tertiary; Protein-Arginine N-Methyltransferases; Protozoan Proteins; S-Adenosylhomocysteine; Substrate Specificity; Trypanosoma brucei brucei

2016
Mechanistic features of the atypical tRNA m1G9 SPOUT methyltransferase, Trm10.
    Nucleic acids research, 2017, Sep-06, Volume: 45, Issue:15

    Topics: Amino Acid Sequence; Aspartic Acid; Binding Sites; Biocatalysis; Catalytic Domain; Cloning, Molecular; Crystallography, X-Ray; Escherichia coli; Gene Expression; Hydrogen-Ion Concentration; Isoenzymes; Kinetics; Methylation; Models, Molecular; Protein Binding; Protein Conformation, alpha-Helical; Protein Interaction Domains and Motifs; Recombinant Proteins; RNA, Transfer; S-Adenosylhomocysteine; S-Adenosylmethionine; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Sequence Alignment; Sequence Homology, Amino Acid; Substrate Specificity; tRNA Methyltransferases

2017