myristic acid has been researched along with tyrosine in 24 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 6 (25.00) | 18.7374 |
| 1990's | 8 (33.33) | 18.2507 |
| 2000's | 7 (29.17) | 29.6817 |
| 2010's | 1 (4.17) | 24.3611 |
| 2020's | 2 (8.33) | 2.80 |
| Authors | Studies |
|---|---|
| Abraham, N; Veillette, A | 1 |
| Kanner, SB; Parsons, JT; Reynolds, AB | 1 |
| Sefton, BM | 1 |
| Hanafusa, H; Jove, R; Kornbluth, S | 1 |
| Burr, JG; Linder, ME | 1 |
| Brugge, JS; Schuh, SM | 1 |
| Glenney, JR | 1 |
| Cross, FR; Garber, EA; Hanafusa, H; Iba, H | 1 |
| Alam, MS; Banno, Y; Nakashima, S; Nozawa, Y | 1 |
| Ballmer-Hofer, K; Kaech, S; Schnierle, B; Wyss, A | 1 |
| Bagrodia, S; Shalloway, D; Taylor, SJ | 1 |
| Bouton, AH; Moyers, JS; Parsons, SJ | 1 |
| DeClue, JE; Johnson, MR; Lowy, DR; Stacey, DW; Vass, WC | 1 |
| Aiken, C; Gallay, P; Swingler, S; Trono, D | 1 |
| Engelman, JA; Galbiati, F; Kaufman, HL; Lee, H; Lisanti, MP; Lublin, DM; Volonté, D; Woodman, SE | 1 |
| Aversa, G; Bennett, MK; Chan, E; Chu, P; Fu, A; Holland, SJ; Kolbinger, F; Li, C; Liao, XC; Luo, Y; Mancebo, HS; Mendenhall, MK; Molineaux, S; Nagin, A; Pali, E; Pardo, J; Payan, DG; Shen, M; Sheng, N; Spencer, C; Woisetschlager, M; Wu, J; Wu, X; Yu, P; Yu, S; Zhou, X | 1 |
| Arudchandran, R; Dráber, P; Dráberová, L; Kovárová, M; Rivera, J; Tolar, P | 1 |
| Constantinescu, SN; Fernandez, MM; Ibarrola, N; Kratchmarova, I; Lodish, HF; Mann, M; Ohara, O; Pandey, A; Sawasdikosol, S | 1 |
| Andresen, BS; Bross, P; Corydon, TJ; Engel, PC; Frazier, DM; Gregersen, N; Hansen, J; Kenney, JM; McCandless, SE; O'Reilly, L; Olpin, SE; Winter, V | 1 |
| Cowan-Jacob, SW; Fabbro, D; Fendrich, G; Jahnke, W; Liebetanz, J; Manley, PW; Meyer, T | 1 |
| Haegebarth, A; Nunez, R; Tyner, AL | 1 |
| Balk, SP; Chen, S; Fang, Z; Wang, H; Xu, Y; Yuan, X | 1 |
| Ahn, Y; Choi, M; Kwon, H; Pak, Y | 1 |
| Kawahara, M; Kongkrongtong, T; Zhang, R | 1 |
24 other study(ies) available for myristic acid and tyrosine
| Article | Year |
|---|---|
Activation of p56lck through mutation of a regulatory carboxy-terminal tyrosine residue requires intact sites of autophosphorylation and myristylation.
Topics: Animals; Base Sequence; Cell Compartmentation; Cell Line; Cell Membrane; DNA; DNA Mutational Analysis; Enzyme Activation; Lymphocyte Specific Protein Tyrosine Kinase p56(lck); Lymphocytes; Mice; Molecular Sequence Data; Mutation; Myristic Acid; Myristic Acids; Oligonucleotides; Phosphorylation; Phosphotyrosine; Protein Processing, Post-Translational; Protein-Tyrosine Kinases; Rats; Tyrosine | 1990 |
Tyrosine phosphorylation of a 120-kilodalton pp60src substrate upon epidermal growth factor and platelet-derived growth factor receptor stimulation and in polyomavirus middle-T-antigen-transformed cells.
Topics: Animals; Antigens, Polyomavirus Transforming; Cell Line; Cell Transformation, Neoplastic; Chick Embryo; ErbB Receptors; Humans; Kinetics; Molecular Weight; Moloney murine leukemia virus; Myristic Acid; Myristic Acids; Palmitic Acid; Palmitic Acids; Phosphates; Phosphorylation; Platelet-Derived Growth Factor; Proto-Oncogene Proteins pp60(c-src); Receptors, Cell Surface; Receptors, Platelet-Derived Growth Factor; Tyrosine | 1991 |
The viral tyrosine protein kinases.
Topics: Abelson murine leukemia virus; Animals; Avian Sarcoma Viruses; Cell Compartmentation; Cell Transformation, Viral; ErbB Receptors; Myristic Acid; Myristic Acids; Oncogene Protein pp60(v-src); Oncogene Proteins, Viral; Phosphatidylinositols; Phosphorylation; Phosphotyrosine; Protein-Tyrosine Kinases; Receptors, Cell Surface; Retroviridae; Retroviridae Proteins; Substrate Specificity; Tyrosine | 1986 |
Characterization of avian and viral p60src proteins expressed in yeast.
Topics: Animals; Avian Sarcoma Viruses; Cell Line; Chick Embryo; Chickens; Fibroblasts; Fungal Proteins; Myristic Acid; Myristic Acids; Oncogene Protein pp60(v-src); Phosphorylation; Phosphotyrosine; Protein Processing, Post-Translational; Protein-Tyrosine Kinases; Proto-Oncogene Proteins; Proto-Oncogene Proteins pp60(c-src); Recombinant Fusion Proteins; Recombinant Proteins; Retroviridae Proteins; Saccharomyces cerevisiae; Tyrosine | 1987 |
Nonmyristoylated p60v-src fails to phosphorylate proteins of 115-120 kDa in chicken embryo fibroblasts.
Topics: Animals; Avian Sarcoma Viruses; Cell Transformation, Viral; Cells, Cultured; Chick Embryo; Immunosorbent Techniques; Membrane Proteins; Molecular Weight; Myristic Acid; Myristic Acids; Oncogene Protein pp60(v-src); Phosphoproteins; Phosphotyrosine; Protein Processing, Post-Translational; Protein-Tyrosine Kinases; Retroviridae Proteins; Structure-Activity Relationship; Subcellular Fractions; Tyrosine | 1988 |
Investigation of factors that influence phosphorylation of pp60c-src on tyrosine 527.
Topics: Antigen-Antibody Complex; Electrophoresis, Polyacrylamide Gel; Mutation; Myristic Acid; Myristic Acids; Peptide Mapping; Phosphorylation; Plasmids; Protein Kinases; Proto-Oncogene Proteins; Proto-Oncogene Proteins pp60(c-src); RNA, Messenger; Tyrosine | 1988 |
Tyrosine phosphorylation of a 22-kDa protein is correlated with transformation by Rous sarcoma virus.
Topics: Animals; Antibodies, Monoclonal; Avian Sarcoma Viruses; Cell Transformation, Neoplastic; Chick Embryo; Fibroblasts; Molecular Weight; Mutation; Myristic Acid; Myristic Acids; Phosphoproteins; Phosphorylation; Phosphotyrosine; Protein-Tyrosine Kinases; Proto-Oncogene Proteins; Proto-Oncogene Proteins pp60(c-src); Tyrosine | 1989 |
Low level of cellular protein phosphorylation by nontransforming overproduced p60c-src.
Topics: Animals; Antigen-Antibody Complex; Avian Sarcoma Viruses; Cell Compartmentation; Cell Membrane; Cell Transformation, Viral; Chick Embryo; Macromolecular Substances; Molecular Weight; Mutation; Myristic Acid; Myristic Acids; Peptide Fragments; Phosphoproteins; Phosphorylation; Protein Kinases; Protein Processing, Post-Translational; Protein-Tyrosine Kinases; Proto-Oncogene Proteins pp60(c-src); Tyrosine | 1985 |
Defective phospholipase D activation in Ki-ras-transformed NIH3T3 cells: evidence for downstream effector of PLC-gamma 1 in PDGF-mediated signal transduction.
Topics: 1-Butanol; 3T3 Cells; Animals; Blotting, Western; Butanols; Cell Line, Transformed; Enzyme Activation; Enzyme Induction; Genes, ras; Glycerophospholipids; Inositol Phosphates; Kinetics; Mice; Myristic Acid; Myristic Acids; Phosphatidic Acids; Phosphatidylinositol Diacylglycerol-Lyase; Phosphoinositide Phospholipase C; Phospholipase D; Phosphoric Diester Hydrolases; Phosphotyrosine; Platelet-Derived Growth Factor; Signal Transduction; Tyrosine | 1995 |
Myristylation and amino-terminal phosphorylation are required for activation of pp60c-src during mitosis.
Topics: 3T3 Cells; Animals; Enzyme Activation; Mice; Mitosis; Myristic Acid; Myristic Acids; Phosphorylation; Protein Kinase C; Proto-Oncogene Proteins pp60(c-src); Tyrosine | 1993 |
Myristylation is required for Tyr-527 dephosphorylation and activation of pp60c-src in mitosis.
Topics: Animals; CDC2 Protein Kinase; Chickens; Enzyme Activation; Mitosis; Mutation; Myristic Acid; Myristic Acids; Protein Processing, Post-Translational; Protein Tyrosine Phosphatases; Protein-Tyrosine Kinases; Proto-Oncogene Proteins pp60(c-src); Tyrosine; Vanadates | 1993 |
The sites of phosphorylation by protein kinase C and an intact SH2 domain are required for the enhanced response to beta-adrenergic agonists in cells overexpressing c-src.
Topics: 3',5'-Cyclic-AMP Phosphodiesterases; Adenylyl Cyclases; Animals; Cell Line; Cholera Toxin; Cyclic AMP; DNA Mutational Analysis; GTP-Binding Proteins; In Vitro Techniques; Mice; Myristic Acid; Myristic Acids; Peptide Mapping; Phosphorylation; Phosphotyrosine; Protein Kinase C; Protein Processing, Post-Translational; Proto-Oncogene Proteins pp60(c-src); Receptors, Adrenergic, beta; Signal Transduction; Structure-Activity Relationship; Transfection; Tyrosine | 1993 |
Functional role of GTPase-activating protein in cell transformation by pp60v-src.
Topics: 3T3 Cells; Adenosine Triphosphate; Animals; Cell Transformation, Neoplastic; Gene Expression; Genes, ras; Genes, src; GTPase-Activating Proteins; Humans; Isoenzymes; Kinetics; Macromolecular Substances; Mice; Myristic Acid; Myristic Acids; Oncogene Protein pp60(v-src); Phosphatidylinositol 3-Kinases; Phosphoproteins; Phosphorylation; Phosphotransferases (Alcohol Group Acceptor); Phosphotyrosine; Protein Biosynthesis; Proteins; ras GTPase-Activating Proteins; Signal Transduction; Transfection; Type C Phospholipases; Tyrosine | 1993 |
HIV-1 infection of nondividing cells: C-terminal tyrosine phosphorylation of the viral matrix protein is a key regulator.
Topics: Amino Acid Sequence; Base Sequence; Cell Differentiation; Cell Division; Cell Line; Cell Nucleus; Cells, Cultured; gag Gene Products, Human Immunodeficiency Virus; Gene Products, gag; HIV Antigens; HIV-1; Humans; Macrophages; Molecular Sequence Data; Myristic Acid; Myristic Acids; Phosphorylation; Protein-Tyrosine Kinases; T-Lymphocytes; Tyrosine; Viral Proteins; Virus Replication | 1995 |
Palmitoylation of caveolin-1 at a single site (Cys-156) controls its coupling to the c-Src tyrosine kinase: targeting of dually acylated molecules (GPI-linked, transmembrane, or cytoplasmic) to caveolae effectively uncouples c-Src and caveolin-1 (TYR-14).
Topics: Animals; Caveolin 1; Caveolins; CD36 Antigens; Cell Membrane; COS Cells; CSK Tyrosine-Protein Kinase; Cytoplasm; Glycosylphosphatidylinositols; Heterotrimeric GTP-Binding Proteins; Myristic Acid; Palmitic Acid; Phosphorylation; Protein-Tyrosine Kinases; src Homology Domains; src-Family Kinases; Tyrosine | 2001 |
Functional cloning of Src-like adapter protein-2 (SLAP-2), a novel inhibitor of antigen receptor signaling.
Topics: Adaptor Proteins, Signal Transducing; Amino Acid Sequence; Antigens, CD; Antigens, Differentiation, T-Lymphocyte; B-Lymphocytes; Base Sequence; Calcium; Cell Line; Cloning, Molecular; DNA-Binding Proteins; DNA, Complementary; Humans; Jurkat Cells; Lectins, C-Type; Molecular Sequence Data; Myristic Acid; NFATC Transcription Factors; Nuclear Proteins; Phosphorylation; Promoter Regions, Genetic; Proto-Oncogene Proteins pp60(c-src); Receptor Protein-Tyrosine Kinases; Receptors, Antigen, B-Cell; Receptors, Antigen, T-Cell; Sequence Homology, Amino Acid; Signal Transduction; src Homology Domains; Tetracycline; Trans-Activators; Transcription Factors; Transcriptional Activation; Tyrosine | 2001 |
Structure-function analysis of Lyn kinase association with lipid rafts and initiation of early signaling events after Fcepsilon receptor I aggregation.
Topics: Animals; Antigens; Calcium; Cell Membrane; Cholesterol; Detergents; DNA; DNA Fragmentation; Enzyme Activation; Green Fluorescent Proteins; Immunoblotting; Lipid Metabolism; Luminescent Proteins; Membrane Microdomains; Mice; Microscopy, Confocal; Myristic Acid; Octoxynol; Palmitic Acid; Phosphorylation; Phosphotyrosine; Precipitin Tests; Protein Binding; Protein Conformation; Protein Structure, Tertiary; Rats; Receptors, IgE; Recombinant Proteins; Signal Transduction; Sphingolipids; src-Family Kinases; Structure-Activity Relationship; Time Factors; Transfection; Tyrosine | 2001 |
A novel Src homology 2 domain-containing molecule, Src-like adapter protein-2 (SLAP-2), which negatively regulates T cell receptor signaling.
Topics: Adaptor Proteins, Signal Transducing; Amino Acid Sequence; Cloning, Molecular; DNA, Complementary; Humans; Jurkat Cells; Molecular Sequence Data; Myristic Acid; Phosphorylation; Proto-Oncogene Proteins pp60(c-src); Receptors, Antigen, T-Cell; Reverse Transcriptase Polymerase Chain Reaction; RNA, Messenger; Signal Transduction; src Homology Domains; Tyrosine | 2002 |
The Y42H mutation in medium-chain acyl-CoA dehydrogenase, which is prevalent in babies identified by MS/MS-based newborn screening, is temperature sensitive.
Topics: Acyl-CoA Dehydrogenase; Amino Acid Substitution; Animals; Circular Dichroism; Enzyme Stability; Escherichia coli; Fibroblasts; Glutamic Acid; Histidine; Humans; Infant, Newborn; Lymphocytes; Lysine; Mitochondria, Liver; Models, Molecular; Mutagenesis, Site-Directed; Myristic Acid; Neonatal Screening; Oxidation-Reduction; Rats; Recombinant Proteins; Structure-Activity Relationship; Tyrosine | 2004 |
The crystal structure of a c-Src complex in an active conformation suggests possible steps in c-Src activation.
Topics: Amino Acid Sequence; Benzamides; Binding Sites; Conserved Sequence; Crystallography, X-Ray; Enzyme Activation; Humans; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Imatinib Mesylate; Inhibitory Concentration 50; Leucine; Models, Chemical; Molecular Conformation; Molecular Sequence Data; Molecular Structure; Myristic Acid; Nuclear Magnetic Resonance, Biomolecular; Phosphorylation; Piperazines; Protein Binding; Proto-Oncogene Proteins c-abl; Pyrimidines; Sequence Homology, Amino Acid; src Homology Domains; src-Family Kinases; Tyrosine | 2005 |
The intracellular tyrosine kinase Brk sensitizes non-transformed cells to inducers of apoptosis.
Topics: Animals; Apoptosis; Cell Differentiation; Cell Line; Cell Proliferation; Cell Transformation, Neoplastic; Cells, Cultured; Cytoplasm; DNA Damage; Fibroblasts; Flow Cytometry; Immunoblotting; Microscopy, Fluorescence; Mutation; Myristic Acid; Neoplasm Proteins; Protein Binding; Protein Structure, Tertiary; Protein-Tyrosine Kinases; Rats; Retroviridae; src Homology Domains; Time Factors; Tyrosine; Ultraviolet Rays | 2005 |
Doxycycline regulated induction of AKT in murine prostate drives proliferation independently of p27 cyclin dependent kinase inhibitor downregulation.
Topics: Animals; Apoptosis; Cell Line; Cell Proliferation; Cyclin-Dependent Kinase Inhibitor p27; Down-Regulation; Doxycycline; Enzyme Induction; Humans; Male; Mice; Myristic Acid; Operon; Phosphorylation; Prostate; Proto-Oncogene Proteins c-akt; Transgenes; Tyrosine | 2012 |
N-myristoylation regulates insulin-induced phosphorylation and ubiquitination of Caveolin-2 for insulin signaling.
Topics: Animals; Caveolin 2; Cell Line; Humans; Insulin; Lipoylation; Membrane Microdomains; Myristic Acid; Phosphorylation; Rats; Receptor, Insulin; Signal Transduction; Tyrosine; Ubiquitination | 2020 |
Rational design of heterodimeric receptors capable of activating target signaling molecules.
Topics: Amino Acid Motifs; Animals; Cell Line; Cell Membrane; Cell Proliferation; Humans; Myristic Acid; Phenotype; Protein Multimerization; Proto-Oncogene Proteins c-kit; Signal Transduction; Tyrosine | 2021 |