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animals (674) 674
humans (668) 668
biochemistry & molecular biology (541) 541
phosphorylation (535) 535
protein tyrosine phosphatase, non-receptor type 11 (424) 424
intracellular signaling peptides and proteins (419) 419
sh2 domain (402) 402
signal transduction (402) 402
sh2 domain-containing protein tyrosine phosphatases (401) 401
src homology domains (367) 367
mice (366) 366
protein tyrosine phosphatases - metabolism (362) 362
protein tyrosine phosphatase, non-receptor type 6 (347) 347
cell biology (321) 321
amino acid sequence (257) 257
molecular sequence data (255) 255
activation (249) 249
index medicus (244) 244
protein binding (229) 229
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binding (107) 107
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biophysics (105) 105
kinase (99) 99
cells, cultured (98) 98
expression (98) 98
oncology (96) 96
article (92) 92
receptor (92) 92
research (92) 92
models, molecular (87) 87
mutation (87) 87
phosphatidylinositol 3-kinase (85) 85
protein structure, tertiary (85) 85
tumor cells, cultured (84) 84
recombinant fusion proteins - metabolism (83) 83
phosphatases (82) 82
phosphotyrosine - metabolism (82) 82
growth-factor receptor (81) 81
tyrosine kinase (81) 81
kinases (80) 80
phosphatidylinositol 3-kinases - metabolism (79) 79
src homology domains - genetics (78) 78
ligands (77) 77
genetics & heredity (73) 73
protein tyrosine phosphatases - chemistry (73) 73
association (72) 72
grb2 adaptor protein (69) 69
protein tyrosine phosphatases - physiology (69) 69
sh2-containing phosphotyrosine phosphatase (69) 69
base sequence (67) 67
mutagenesis, site-directed (67) 67
proto-oncogene proteins - metabolism (67) 67
cells (66) 66
shc signaling adaptor proteins (66) 66
female (65) 65
sequence homology, amino acid (65) 65
kinetics (64) 64
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src homology 2 domain-containing, transforming protein 1 (63) 63
physiological aspects (62) 62
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cloning, molecular (61) 61
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shp-2 (57) 57
antigen receptor (55) 55
crystal-structure (55) 55
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grb2 (53) 53
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analysis (52) 52
3t3 cells (51) 51
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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
Immunologic Research, ISSN 0257-277X, 5/2006, Volume 35, Issue 1, pp. 127 - 136
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, 12/2004, Volume 173, Issue 12, pp. 7385 - 7393
Journal Article
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
International Immunopharmacology, ISSN 1567-5769, 11/2013, Volume 17, Issue 3, pp. 638 - 650
Neutrophils play a critical role in the host defense against bacterial and fungal infections, but their inappropriate activation also contributes to tissue... 
Signaling | Receptors | Inflammation | Kinases | Neutrophils | ACTIVATED PROTEIN-KINASE | COLONY-STIMULATING FACTOR | LEUKOCYTE ADHESION DEFICIENCY | IMMUNOLOGY | SRC-FAMILY KINASES | HUMAN POLYMORPHONUCLEAR LEUKOCYTES | HIGH-AFFINITY RECEPTOR | TUMOR-NECROSIS-FACTOR | TOLL-LIKE RECEPTORS | PHARMACOLOGY & PHARMACY | BETA-GAMMA-SUBUNITS | NF-KAPPA-B | Signal Transduction - immunology | Animals | Receptors, Cell Surface - immunology | Humans | Neutrophils - immunology | Selectins - immunology | Mycoses | Lectins | Fc receptors | Integrins | FcR, Fc-receptor | GPI, glycosylphosphatidylinositol anchor | CLEC, C-type lectin | OSCAR, osteoclast-associated receptor | PKB, protein kinase B | DAG, diacyl-glycerol | Tyk2, tyrosine protein kinase 2 | VCAM-1, vascular cell adhesion molecule 1 | ICAM-1, intercellular adhesion molecule 1 | FADD, Fas-associated protein with death domain | IκB, inhibitor of NF-κB | GM-CSF, granulocyte | MyD88, myeloid differentiation protein 88 | TNF, tumor necrosis factor | LTβ, lymphotoxin β | TRADD, TNFR1-associated death domain protein | Abl, Abelson leukemia proto-oncogene | SLP-76, SH2 domain-containing leukocyte protein of 76 kDa | CALDAG-GEFI, calcium and DAG-regulated guanine nucleotide exchange factor I | IL, interleukin | Src, Rous sarcoma virus proto-oncogene | IRF, IFN regulatory factor | RIG, retinoic acid-inducible gene | PLC, phospholipase C | TCR, T-cell receptor | IKK, IκB kinase | ITAM, immunoreceptor tyrosine-based activation motif | CARD, caspase activation and recruitment domain | IP3, inositol-tris-phosphate | CHO, Chinese hamster ovary cells | MKK, MAP kinase kinase | fMLP, formly-Met-Leu-Phe | TRAF, TNF receptor-associated factor | MIP, macrophage inflammatory protein | Rac, Ras-related C3 botulinum toxin substrate | monocyte colony-stimulating factor | PIP3, phosphatidylinositol-3-phosphate | VLA-4, very late antigen 4 (α4β1 integrin) | PAF, platelet activating factor | STAT, signal transducer and activator of transcription | TAK, TGFβ-activated kinase 1 | Mac-1, macrophage antigen 1 (αMβ2 integrin) | FcRγ, Fc-receptor γ-chain | Asc, apoptosis-associated speck-like protein containing a CARD | cIAP, cellular inhibitor of apoptosis | BCR, B-cell receptor | Fgr, Gardner–Rasheed feline sarcoma proto-oncogene | VASP, vasodilator-stimulated phosphoprotein | Hck, hematopoietic cell kinase | TGFβ, transforming growth factor β | Rap, Ras-related protein | SHP-1, SH2 domain-containing protein tyrosine phosphatase 1 | Syk, spleen tyrosine kinase | GPCR, G protein-coupled receptor | G-CSF, granulocyte colony-stimulating factor | TREM, triggering receptor expressed on myeloid cells | DISC, death-inducing signaling complex | MDL-1, myeloid DAP12-associating lectin 1 | C3G, Crk SH3 domain-binding guanine nucleotide exchange factor (RapGEF1) | NF-κB, nuclear factor κB | ERM, ezrin-radixin-moesin | Epac1, exchange protein activated by cyclic AMP 1 | LTB4, leukotriene B4 | Mcl, macrophage C-type lectin | SAP130, Sin3A-associated protein of 130 kDa | SH2, Src-homology 2 domain | MAP kinase, mitogen-activated protein kinase | PSGL-1, P-selectin glycoprotein ligand | PI3K, phoshoinositide-3-kinase | ADAP, adhesion and degranulation promoting adapter protein (Fyb, SLAP-130) | NLRP3, NOD-like receptor family, pyrin domain containing 3 | MDA5, melanoma differentiation-associated protein 5 | TLR, Toll-like receptor | GRK, GPCR kinase | LAD, leukocyte adhesion deficiency | MAPKAP-kinase, MAP kinase-associated protein kinase | ZAP-70, ζ-chain-associated protein of 70 kDa | TRAIL, TNF-related apoptosis-inducing ligand | JNK, c-Jun N-terminal kinase | LFA-1, lymphocyte function-associated receptor 1 (αLβ2 integrin) | ROS, reactive oxygen species | RIP3, receptor-interacting serine-threonine protein kinase 3 | DAP12, DNAX activating protein 12 | IFN, interferon | PIR, paired immunoglobulin-like receptor | PKC, protein kinase C | PAK, p21-activated kinase | ESL-1, E-selectin ligand 1 | GAP, GTPase activating protein | ERK, extracellular signal-regulated kinase | SOCS, suppressor of cytokine signaling | JAK, Janus kinase | RANK, receptor activator of NF-κB | IRAK, IL-1 receptor-associated kinase | NOD, nucleotide-binding oligomerization domain containing protein | CEACAM3, carcinoembryonic antigen-related cell adhesion molecule 3 (CD66b)
Journal Article