X
Search Filters
Format Format
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
protein tyrosine phosphatase, non-receptor type 11 (410) 410
animals (403) 403
sh2 domain-containing protein tyrosine phosphatases (399) 399
intracellular signaling peptides and proteins (390) 390
humans (386) 386
protein tyrosine phosphatases - metabolism (344) 344
protein tyrosine phosphatase, non-receptor type 6 (337) 337
phosphorylation (336) 336
biochemistry & molecular biology (293) 293
mice (249) 249
src homology domains (242) 242
signal transduction (231) 231
sh2 domain (172) 172
activation (166) 166
protein tyrosine phosphatases - genetics (165) 165
cell line (150) 150
molecular sequence data (148) 148
cell biology (145) 145
amino acid sequence (142) 142
protein binding (121) 121
signal-transduction (116) 116
tyrosine - metabolism (115) 115
immunology (111) 111
index medicus (105) 105
sh2 domains (103) 103
protein-tyrosine-phosphatase (99) 99
transfection (95) 95
protein-tyrosine kinases - metabolism (91) 91
binding sites (88) 88
enzyme activation (82) 82
phosphoproteins - metabolism (79) 79
cells, cultured (75) 75
expression (72) 72
proteins (72) 72
proteins - metabolism (72) 72
adaptor proteins, signal transducing (71) 71
kinase (71) 71
protein tyrosine phosphatases - chemistry (71) 71
rats (70) 70
phosphatases (69) 69
research (66) 66
tyrosine (66) 66
protein tyrosine phosphatases - physiology (65) 65
sh2-containing phosphotyrosine phosphatase (63) 63
protein (62) 62
signal transduction - physiology (61) 61
tumor cells, cultured (61) 61
mutation (60) 60
phosphatidylinositol 3-kinases - metabolism (60) 60
src homology domains - genetics (59) 59
phosphotyrosine phosphatase (57) 57
oncology (54) 54
kinases (52) 52
receptor (52) 52
recombinant fusion proteins - metabolism (52) 52
multidisciplinary sciences (51) 51
shp-2 (51) 51
association (50) 50
growth-factor receptor (49) 49
tyrosine phosphorylation (49) 49
biophysics (48) 48
male (48) 48
mutagenesis, site-directed (48) 48
protein structure, tertiary (47) 47
base sequence (45) 45
genetics & heredity (44) 44
proto-oncogene proteins - metabolism (44) 44
sh-ptp2 (44) 44
src homology domains - immunology (44) 44
binding (43) 43
phosphotyrosine - metabolism (43) 43
female (42) 42
protein phosphatase 2 (42) 42
research article (42) 42
signal transduction - immunology (42) 42
negative regulation (41) 41
phosphatidylinositol 3-kinase (41) 41
cells (40) 40
kinetics (40) 40
recombinant proteins - metabolism (40) 40
cloning, molecular (39) 39
grb2 adaptor protein (39) 39
phosphatidylinositol-3,4,5-trisphosphate 5-phosphatases (39) 39
physiological aspects (39) 39
mice, inbred c57bl (37) 37
src homology-2 domains (37) 37
src homology domains - physiology (36) 36
ligands (35) 35
shp-1 (35) 35
blotting, western (34) 34
moth-eaten (34) 34
moth-eaten mice (34) 34
phosphoric monoester hydrolases - metabolism (34) 34
protein phosphatase 1 (34) 34
sequence homology, amino acid (34) 34
signal transduction - genetics (34) 34
receptors (33) 33
carrier proteins - metabolism (31) 31
dna-binding proteins - metabolism (31) 31
hematology (31) 31
more...
Language Language
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


Journal Article
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 8/1999, Volume 96, Issue 17, pp. 9677 - 9682
Leptin exerts its weight-reducing effects by binding to its receptor and activating signal transduction in hypothalamic neurons and other cell types. To... 
Proteins | Signal transduction | Receptors | Phosphorylation | Phosphatases | Ungulates | Antibodies | Lead | Hypothalamus | Cells | DIABETIC MICE | DB/DB MICE | SHP-2 | CLONING | OBESE GENE | MULTIDISCIPLINARY SCIENCES | ADHESION MOLECULE-1 PECAM-1 | PROLIFERATION | IDENTIFICATION | EXPRESSION | PHOSPHOTYROSINE PHOSPHATASE | Hormone receptors | Cellular signal transduction | Research | Leptin
Journal Article
Academic Journal of Second Military Medical University, ISSN 0258-879X, 2017, Volume 38, Issue 9, pp. 1128 - 1133
Journal Article
Journal Article
The Journal of Immunology, ISSN 0022-1767, 03/2001, Volume 166, Issue 5, pp. 3098 - 3106
Platelet endothelial cell adhesion molecule-1 (PECAM-1/CD31) is a newly assigned member of the Tg immunoreceptor tyrosine-based inhibitory motif superfamily,... 
B-CELLS | CD31 | PATHWAYS | COMPLEX | CD22-DEFICIENT MICE | PHOSPHORYLATION | ANTIGEN-RECEPTOR | TRANSDUCTION | IMMUNOLOGY | MOLECULE-1 PECAM-1/CD31 | CD22 | Recombinant Fusion Proteins - immunology | Protein Tyrosine Phosphatase, Non-Receptor Type 11 | Platelet Endothelial Cell Adhesion Molecule-1 - genetics | Recombinant Fusion Proteins - pharmacology | Humans | src Homology Domains - genetics | Consensus Sequence - immunology | Signal Transduction - immunology | Lymphocyte Activation - genetics | Protein Tyrosine Phosphatases - genetics | Receptors, IgG - genetics | Protein Tyrosine Phosphatases - deficiency | Platelet Endothelial Cell Adhesion Molecule-1 - physiology | B-Lymphocytes - metabolism | Cell Line | Tyrosine - physiology | B-Lymphocytes - enzymology | Intracellular Signaling Peptides and Proteins | Protein Structure, Tertiary - genetics | Signal Transduction - genetics | Down-Regulation - genetics | Animals | B-Lymphocytes - immunology | Cytoplasm - immunology | Amino Acid Motifs - immunology | Down-Regulation - immunology | Chickens | SH2 Domain-Containing Protein Tyrosine Phosphatases | Mice | src Homology Domains - immunology | Consensus Sequence - genetics | Amino Acid Motifs - genetics | Protein Tyrosine Phosphatase, Non-Receptor Type 6 | Protein Tyrosine Phosphatases - physiology | Tyrosine - genetics
Journal Article
The Journal of Immunology, ISSN 0022-1767, 12/2003, Volume 171, Issue 11, pp. 6072 - 6079
Curcumin has been strongly implicated as an anti-inflammatory agent, but the precise mechanisms of its action are largely unknown. In this study, we show that... 
SH2 DOMAIN | MEMBRANE RAFTS | CELLS | JAK/STAT PATHWAY | SHP-2 | PROTEIN | PHOSPHORYLATION | GENE-EXPRESSION | IMMUNOLOGY | NITRIC-OXIDE MECHANISM | NF-KAPPA-B | Prostaglandin-Endoperoxide Synthases - biosynthesis | Microglia - metabolism | Protein Tyrosine Phosphatase, Non-Receptor Type 11 | Protein-Tyrosine Kinases - metabolism | Regulatory Sequences, Nucleic Acid | Brain - enzymology | Protein Tyrosine Phosphatases - metabolism | Interferon-gamma - metabolism | Nitric Oxide Synthase Type II | Trans-Activators - physiology | Brain - metabolism | Protein-Tyrosine Kinases - physiology | Inflammation - metabolism | Microglia - pathology | Phosphorylation - drug effects | Protein Phosphatase 2 | DNA-Binding Proteins - physiology | DNA-Binding Proteins - antagonists & inhibitors | Curcumin - pharmacology | Microglia - enzymology | Rats | src Homology Domains - physiology | Rats, Sprague-Dawley | Janus Kinase 1 | Brain - drug effects | Signal Transduction - drug effects | SH2 Domain-Containing Protein Tyrosine Phosphatases | Brain - pathology | STAT1 Transcription Factor | Inflammation - prevention & control | Protein-Tyrosine Kinases - antagonists & inhibitors | Cyclooxygenase 2 | Nitric Oxide Synthase - antagonists & inhibitors | Anti-Inflammatory Agents, Non-Steroidal - pharmacology | DNA-Binding Proteins - metabolism | Janus Kinase 2 | Interferon-gamma - antagonists & inhibitors | Nitric Oxide Synthase - biosynthesis | Proto-Oncogene Proteins | Microglia - drug effects | Cells, Cultured | Intracellular Signaling Peptides and Proteins | Down-Regulation - drug effects | Gene Expression Regulation - drug effects | Up-Regulation - drug effects | Animals | Inflammation - genetics | Signal Transduction - physiology | Trans-Activators - metabolism | STAT3 Transcription Factor | Trans-Activators - antagonists & inhibitors | Isoenzymes - biosynthesis | Interferon-gamma - pharmacology | Isoenzymes - antagonists & inhibitors
Journal Article
Science, ISSN 0036-8075, 1/2002, Volume 295, Issue 5555, pp. 683 - 686
Helicobacter pylori CagA protein is associated with severe gastritis and gastric carcinoma. CagA is injected from the attached Helicobacter pylori into host... 
COS cells | Phenotypes | Phosphorylation | Phosphatases | Transfection | Hepatocytes | Epithelial cells | B lymphocytes | Antibodies | Reports | Cell membranes | SH2-CONTAINING PHOSPHOTYROSINE PHOSPHATASE | TRANSLOCATION | FOCAL ADHESION | MULTIDISCIPLINARY SCIENCES | INVOLVEMENT | IV SECRETION | GASTRIC EPITHELIAL-CELLS | SH2 DOMAINS | SH-PTP2 | ANTIGEN | Protein Tyrosine Phosphatase, Non-Receptor Type 11 | Humans | Virulence | Helicobacter pylori - genetics | Helicobacter pylori - pathogenicity | Protein Tyrosine Phosphatases - metabolism | Recombinant Fusion Proteins - metabolism | Phosphotyrosine - metabolism | Protein Tyrosine Phosphatases - antagonists & inhibitors | Protein Tyrosine Phosphatases - chemistry | Protein Tyrosine Phosphatases - genetics | Cell Membrane - metabolism | Dipeptides - pharmacology | Bacterial Proteins - genetics | Enzyme Inhibitors - pharmacology | Gastric Mucosa - enzymology | Intracellular Signaling Peptides and Proteins | Cell Size | Antigens, Bacterial | Gastric Mucosa - cytology | src Homology Domains | Cell Membrane - enzymology | Phenotype | Animals | SH2 Domain-Containing Protein Tyrosine Phosphatases | Bacterial Proteins - metabolism | Mutation | COS Cells | Protein Tyrosine Phosphatase, Non-Receptor Type 6 | Amino Acid Substitution | Helicobacter pylori | Carcinogens | Research | Proteins | Molecular biology | Cells
Journal Article
Journal Article
Cancer Research, ISSN 0008-5472, 08/2006, Volume 66, Issue 15, pp. 7473 - 7481
Glioblastoma multiforme is the most common and lethal form of primary brain cancer. Diagnosis of this advanced glioma has a poor prognosis due to the... 
MAMMALIAN TARGET | ONCOLOGY | TUMOR SUPPRESSION | PHOSPHATASE SHP-2 | GROWTH-FACTORS | JUVENILE MYELOMONOCYTIC LEUKEMIA | C-ROS | PTPN11 MUTATIONS | CELL-LINES | NOONAN-SYNDROME | BRAIN-TUMORS | Protein Kinases - metabolism | Glioblastoma - enzymology | Protein Tyrosine Phosphatase, Non-Receptor Type 11 | Tumor Suppressor Protein p14ARF - deficiency | Protein-Tyrosine Kinases - metabolism | Brain Neoplasms - pathology | Protein Tyrosine Phosphatases - metabolism | Intracellular Signaling Peptides and Proteins - metabolism | Phosphatidylinositol 3-Kinases - metabolism | Proto-Oncogene Proteins - biosynthesis | Recombinant Fusion Proteins - metabolism | Brain Neoplasms - metabolism | Astrocytoma - pathology | Protein-Tyrosine Kinases - genetics | Astrocytoma - enzymology | Glioblastoma - metabolism | Protein Phosphatase 2 | Proto-Oncogene Proteins c-akt - metabolism | Protein-Tyrosine Kinases - biosynthesis | Astrocytoma - metabolism | Proto-Oncogene Proteins - metabolism | Recombinant Fusion Proteins - biosynthesis | Brain Neoplasms - enzymology | Cyclin-Dependent Kinase Inhibitor p16 - deficiency | Signal Transduction | Cyclin-Dependent Kinase Inhibitor p16 - genetics | Proto-Oncogene Proteins - genetics | src Homology Domains | Animals | Glioblastoma - pathology | SH2 Domain-Containing Protein Tyrosine Phosphatases | Recombinant Fusion Proteins - genetics | Mice | TOR Serine-Threonine Kinases | Enzyme Activation | Tumor Suppressor Protein p14ARF - genetics
Journal Article
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 11/2001, Volume 98, Issue 24, pp. 13866 - 13871
PD-1 is an immunoreceptor that belongs to the immunoglobulin (Ig) superfamily and contains two tyrosine residues in the cytoplasmic region. Studies on... 
Proteins | Molecules | Biological Sciences | Phosphorylation | Receptors | Phosphatases | B lymphocytes | Cell lines | Ligands | Chimeras | Growth retardation | P62(DOK) | ACTIVATION | PROTEIN | MULTIDISCIPLINARY SCIENCES | ANTIGEN-RECEPTOR | MICE | SHP-1 | EXPRESSION | MEMBER | FAMILY | LYMPHOCYTES | Protein Tyrosine Phosphatase, Non-Receptor Type 11 | Calcium - metabolism | Humans | Protein Tyrosine Phosphatases - metabolism | Receptors, Antigen, B-Cell - metabolism | Antigens, CD - genetics | Receptors, IgG - metabolism | Antigens, CD - metabolism | Phosphotyrosine - metabolism | Receptors, IgG - genetics | Cell Division | Antigens, Surface - metabolism | Tumor Cells, Cultured | Protein Phosphatase 2 | Signal Transduction | Receptors, KIR | Antigens, Surface - genetics | Intracellular Signaling Peptides and Proteins | src Homology Domains | Tyrosine - metabolism | Animals | Apoptosis Regulatory Proteins | SH2 Domain-Containing Protein Tyrosine Phosphatases | Programmed Cell Death 1 Receptor | Mice | Receptors, Immunologic - genetics | Mitogen-Activated Protein Kinase 3 | Protein Tyrosine Phosphatase, Non-Receptor Type 6 | Receptors, Immunologic - metabolism | Mitogen-Activated Protein Kinase 1 - metabolism | Mitogen-Activated Protein Kinases - metabolism | Physiological aspects | Protein tyrosine kinase | Immunoglobulins | Cellular signal transduction | B cells | phosphotyrosine | thyrosine phosphatase | Fc receptors | SH2 domain | PD-1 protein
Journal Article