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Immunologic Research, ISSN 0257-277X, 4/2011, Volume 49, Issue 1, pp. 235 - 247
Aberrant signaling pathways are a hallmark of cancer. A variety of strategies for inhibiting signaling pathways have been developed, but monoclonal antibodies... 
Allergology | Antigens | Active immunotherapy | Immunology | Medicine & Public Health | Internal Medicine | Polyclonal | Vaccines | Cancer immunotherapy | Medicine/Public Health, general | TYROSINE KINASES | IMMUNOLOGY | HUMAN BREAST-CANCER | METASTATIC COLORECTAL-CANCER | GROWTH-FACTOR RECEPTOR | ENDOCYTIC DOWN-REGULATION | IN-VIVO | REGULATORY T-CELLS | ANTITUMOR IMMUNITY | RESISTANT PROSTATE-CANCER | LAPATINIB GW572016 | Humans | Antibodies, Monoclonal - therapeutic use | Clinical Trials as Topic | Protein-Tyrosine Kinases - immunology | Neoplasms - drug therapy | Antibodies, Monoclonal, Humanized | Cancer Vaccines - immunology | Signal Transduction - immunology | Neoplasms - therapy | Neoplasms - immunology | Quinazolines - therapeutic use | Immunotherapy | T-Lymphocytes - immunology | Receptor, ErbB-2 - antagonists & inhibitors | Receptor, ErbB-2 - immunology | Antibodies, Monoclonal - immunology | Trastuzumab | Protein-Tyrosine Kinases - antagonists & inhibitors | Cancer vaccines | Tyrosine | Care and treatment | Immune response | Health aspects | Phosphotransferases | Cancer | Monoclonal antibodies | ErbB protein | ErbB-2 protein | Survival | Signal transduction | Immunogenicity | Protein-tyrosine kinase receptors | Microenvironments | Mutation | Receptor mechanisms | Tumors | polyclonal | antigens | active immunotherapy | vaccines
Journal Article
Journal Article
Trends in Pharmacological Sciences, ISSN 0165-6147, 1989, Volume 10, Issue 10, pp. 411 - 414
The EGF receptor, which is homologous to the ν-erb-B oncogene product, has intrinsic tyrosine kinase activity, and mediates an increase in polyphosphoinositide... 
PHARMACOLOGY & PHARMACY | ErbB Receptors - physiology | Animals | ErbB Receptors - metabolism | Signal Transduction | Humans | Cell Membrane - metabolism | Cell Membrane - physiology | ErbB Receptors - drug effects
Journal Article
Journal of Steroid Biochemistry and Molecular Biology, ISSN 0960-0760, 1991, Volume 40, Issue 1, pp. 175 - 183
Journal Article
Science, ISSN 0036-8075, 5/1991, Volume 252, Issue 5006, pp. 668 - 674
Src homology (SH) regions 2 and 3 are noncatalytic domains that are conserved among a series of cytoplasmic signaling proteins regulated by receptor... 
Signal transduction | Receptors | Phosphorylation | Cell growth | Signaling proteins | Complementary DNA | Ligands | Amino acids | Mathematical functions | Cells | TYROSINE KINASE GENE | GROWTH-FACTOR RECEPTOR | AMINO-TERMINAL DOMAIN | PHOSPHATIDYLINOSITOL KINASE | ROUS-SARCOMA VIRUS | MULTIDISCIPLINARY SCIENCES | SRC GENE | REGULATES INTERACTIONS | PHOSPHOLIPASE-C-GAMMA | PDGF RECEPTOR | EGF RECEPTOR | Protein-Tyrosine Kinases - metabolism | Phosphotyrosine | Molecular Sequence Data | Type C Phospholipases - metabolism | Cytoplasm - metabolism | Phosphoproteins - metabolism | Tyrosine - analogs & derivatives | Protein Sorting Signals - metabolism | Receptors, Platelet-Derived Growth Factor | Protein-Tyrosine Kinases - chemistry | Binding Sites | Amino Acid Sequence | ErbB Receptors - metabolism | GTPase-Activating Proteins | Signal Transduction | ras GTPase-Activating Proteins | Receptors, Cell Surface - metabolism | Platelet-Derived Growth Factor - pharmacology | Type C Phospholipases - chemistry | Sequence Homology, Nucleic Acid | Tyrosine - metabolism | Proteins - metabolism | Protein Sorting Signals - chemistry | Epidermal Growth Factor - pharmacology | Proteins - chemistry | Protein tyrosine kinase | Cellular signal transduction | Research | Growth factor receptors | Cellular control mechanisms | Membrane proteins | Proteins | Physical growth | Biochemistry
Journal Article
Structure, ISSN 0969-2126, 1994, Volume 2, Issue 5, pp. 423 - 438
Background Src homology 2 (SH2) domains bind to phosphotyrosine residues in a sequence-specific manner, and thereby couple tyrosine phosphorylation to changes... 
crystal structure | SH2 domain | tyrosine phosphorylation | signal transduction | Syp tyrosine phosphatase | Signal transduction | Tyrosine phosphorylation | Crystal structure | PHOSPHORYLATED PEPTIDES | PROTEIN | TYROSINE PHOSPHORYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | CRYSTAL STRUCTURE | TRANSFORMING ACTIVITY | PI 3-KINASE | EXPRESSION CLONING | PDGF RECEPTOR | CELL BIOLOGY | SH2 DOMAIN | SH2-CONTAINING PHOSPHOTYROSINE PHOSPHATASE | BIOPHYSICS | SYP TYROSINE PHOSPHATASE | BINDING-SITE | FACTOR RECEPTOR-BETA | SIGNAL TRANSDUCTION | SRC HOMOLOGY-2 DOMAIN | Protein Tyrosine Phosphatase, Non-Receptor Type 11 | Oncogene Protein pp60(v-src) - metabolism | Receptors, Platelet-Derived Growth Factor - chemistry | Protein-Tyrosine Kinases - metabolism | Phosphotyrosine | Molecular Sequence Data | Crystallography, X-Ray | Protein Tyrosine Phosphatases - metabolism | Structure-Activity Relationship | Phosphoproteins - metabolism | Tyrosine - analogs & derivatives | Phosphoproteins - chemistry | Oncogene Protein pp60(v-src) - chemistry | Protein Tyrosine Phosphatases - chemistry | Peptides - metabolism | Insulin Receptor Substrate Proteins | Protein-Tyrosine Kinases - chemistry | Amino Acid Sequence | Peptide Fragments - metabolism | ErbB Receptors - metabolism | Lymphocyte Specific Protein Tyrosine Kinase p56(lck) | Peptides - chemistry | Intracellular Signaling Peptides and Proteins | Models, Molecular | Peptide Fragments - chemistry | Tyrosine - metabolism | Animals | ErbB Receptors - chemistry | Receptors, Platelet-Derived Growth Factor - metabolism | SH2 Domain-Containing Protein Tyrosine Phosphatases | Protein Binding | Protein Conformation | Mice | Protein Tyrosine Phosphatase, Non-Receptor Type 6
Journal Article
International Journal of Radiation Oncology, Biology, Physics, ISSN 0360-3016, 1994, Volume 29, Issue 4, pp. 813 - 819
Journal Article
Journal Article