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1. Full Text Endothelial Cells Promote the Colorectal Cancer Stem Cell Phenotype through a Soluble Form of Jagged-1
by Lu, Jia and Ye, Xiangcang and Fan, Fan and Xia, Ling and Bhattacharya, Rajat and Bellister, Seth and Tozzi, Federico and Sceusi, Eric and Zhou, Yunfei and Tachibana, Isamu and Maru, Dipen M and Hawke, David H and Rak, Janusz and Mani, Sendurai A and Zweidler-McKay, Patrick and Ellis, Lee M
Cancer Cell, ISSN 1535-6108, 02/2013, Volume 23, Issue 2, pp. 171 - 185
We report a paracrine effect whereby endothelial cells (ECs) promote the cancer stem cell (CSC) phenotype of human colorectal cancer (CRC) cells. We showed... 
COLON-CANCER | METASTASIS | ONCOLOGY | NOTCH | NICHE | SELF-RENEWAL | RECEPTOR | GROWTH-FACTOR | TUMOR ANGIOGENESIS | DIFFERENTIATION | ANGIOCRINE FACTORS | CELL BIOLOGY | ADAM17 Protein | RNA, Small Interfering - genetics | Immunoprecipitation | Receptors, Notch - metabolism | Colorectal Neoplasms - genetics | Humans | Calcium-Binding Proteins - antagonists & inhibitors | Culture Media, Conditioned - pharmacology | Drug Resistance, Neoplasm | Immunoblotting | Peptide Fragments - pharmacology | Intercellular Signaling Peptides and Proteins - metabolism | Neoplastic Stem Cells - metabolism | Serrate-Jagged Proteins | Neoplastic Stem Cells - pathology | Antineoplastic Agents - pharmacology | Membrane Proteins - metabolism | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Tumor Cells, Cultured | Liver Neoplasms - secondary | Colorectal Neoplasms - metabolism | Jagged-1 Protein | Biomarkers - metabolism | Calcium-Binding Proteins - metabolism | ADAM Proteins - antagonists & inhibitors | Liver Neoplasms - genetics | Signal Transduction | Endothelial Cells - metabolism | Membrane Proteins - genetics | Intercellular Signaling Peptides and Proteins - genetics | Cell Communication | Xenograft Model Antitumor Assays | ADAM Proteins - metabolism | Phenotype | Animals | Membrane Proteins - antagonists & inhibitors | Mice, Nude | Liver Neoplasms - metabolism | Mice | ADAM Proteins - genetics | Colorectal Neoplasms - pathology | Endothelial Cells - pathology | Calcium-Binding Proteins - genetics | Genetic aspects | Colorectal cancer | Stem cells | Endothelium | Index Medicus
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2. Full Text ADAMs 10 and 17 Represent Differentially Regulated Components of a General Shedding Machinery for Membrane Proteins Such as Transforming Growth Factor alpha, L-Selectin, and Tumor Necrosis Factor alpha
by Le Gall, SM and Bobe, P and Reiss, K and Horiuchi, K and Niu, XD and Lundell, D and Gibb, DR and Conrad, D and Saftig, P and Blobel, CP
MOLECULAR BIOLOGY OF THE CELL, ISSN 1059-1524, 03/2009, Volume 20, Issue 6, pp. 1785 - 1794
Protein ectodomain shedding is a critical regulator of many membrane proteins, including epidermal growth factor receptor-ligands and tumor necrosis factor... 
ECTODOMAIN | RECEPTOR | NEUTROPHILS | TNF-ALPHA | LIGAND | CLEAVAGE | CANCER | EGFR | CONVERTING-ENZYME | METALLOPROTEASES | CELL BIOLOGY | ADAM17 Protein | Tumor Necrosis Factor-alpha - metabolism | Amyloid Precursor Protein Secretases - genetics | Calcium - metabolism | Humans | Substrate Specificity | L-Selectin - metabolism | Protease Inhibitors - pharmacology | RNA Interference | Membrane Proteins - metabolism | Transforming Growth Factor alpha - metabolism | ADAM Proteins - antagonists & inhibitors | Membrane Proteins - genetics | Cells, Cultured | ADAM Proteins - deficiency | ADAM10 Protein | Mice, Knockout | ADAM Proteins - metabolism | Amyloid Precursor Protein Secretases - metabolism | Animals | Membrane Proteins - antagonists & inhibitors | Signal Transduction - drug effects | Mice | Amyloid Precursor Protein Secretases - antagonists & inhibitors | ADAM Proteins - genetics | Index Medicus
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3. Full Text ADAMs 10 and 17 represent differentially regulated components of a general shedding machinery for membrane proteins such as transforming growth factor alpha, L-selectin, and tumor necrosis factor alpha
by Le Gall, Sylvain M and Bobé, Pierre and Reiss, Karina and Horiuchi, Keisuke and Niu, Xiao-Da and Lundell, Daniel and Gibb, David R and Conrad, Daniel and Saftig, Paul and Blobel, Carl P
Molecular biology of the cell, ISSN 1059-1524, 03/2009, Volume 20, Issue 6, pp. 1785 - 1794
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4. Full Text Receptor for Advanced Glycation End Products Is Subjected to Protein Ectodomain Shedding by Metalloproteinases
by Ling Zhang and Monika Bukulin and Elzbieta Kojro and Annette Roth and Verena V. Metz and Falk Fahrenholz and Peter P. Nawroth and Angelika Bierhaus and Rolf Postina
Journal of Biological Chemistry, ISSN 0021-9258, 12/2008, Volume 283, Issue 51, pp. 35507 - 35516
The receptor for advanced glycation end products (RAGE) is a 55-kDa type I membrane glycoprotein of the immunoglobulin superfamily. Ligand-induced... 
ALPHA-SECRETASE | RAGE RECEPTOR | MATRIX METALLOPROTEINASES | CELLS | BIOCHEMISTRY & MOLECULAR BIOLOGY | AMYLOID PRECURSOR PROTEIN | BLOOD-BRAIN-BARRIER | SPLICE VARIANTS | MULTILIGAND RECEPTOR | EXPRESSION | SOLUBLE RECEPTOR | Amyloid Precursor Protein Secretases - genetics | RNA, Small Interfering - genetics | Tetradecanoylphorbol Acetate - pharmacology | Humans | Cell Membrane - genetics | Protease Inhibitors - pharmacology | Matrix Metalloproteinase 9 - metabolism | Carcinogens - pharmacology | Protein Isoforms - metabolism | Cell Membrane - metabolism | Diabetes Complications - genetics | Membrane Proteins - metabolism | Hydroxamic Acids - pharmacology | Receptor for Advanced Glycation End Products | Ionophores - pharmacology | Cell Line | ADAM Proteins - antagonists & inhibitors | Membrane Proteins - genetics | Alternative Splicing - genetics | Diabetes Complications - metabolism | ADAM10 Protein | Protein Structure, Tertiary - genetics | Calcimycin - pharmacology | ADAM Proteins - metabolism | Amyloid Precursor Protein Secretases - metabolism | Alternative Splicing - drug effects | Membrane Proteins - antagonists & inhibitors | Alzheimer Disease - metabolism | Matrix Metalloproteinase Inhibitors | Amyloid Precursor Protein Secretases - antagonists & inhibitors | ADAM Proteins - genetics | Alzheimer Disease - genetics | Receptors, Immunologic - genetics | Receptors, Immunologic - metabolism | Protein Isoforms - genetics | Index Medicus
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5. Full Text Shedding of endogenous MHC class I-related chain molecules A and B from different human tumor entities: Heterogeneous involvement of the "a disintegrin and metalloproteases" 10 and 17
by Chitadze, Guranda and Lettau, Marcus and Bhat, Jaydeep and Wesch, Daniela and Steinle, Alexander and Fürst, Daniel and Mytilineos, Joannis and Kalthoff, Holger and Janssen, Ottmar and Oberg, Hans-Heinrich and Kabelitz, Dieter
International Journal of Cancer, ISSN 0020-7136, 10/2013, Volume 133, Issue 7, pp. 1557 - 1566
The interaction of the MHC class I-related chain molecules A and B (MICA and MICB) with the corresponding natural killer group 2, member D (NKG2D) receptor... 
ADAM10 | ADAM17 | shedding | NKG2D ligands | MICA | MICB | ACTIVATION | CANCER | CUTTING EDGE | RECEPTOR NKG2D | NK CELLS | ONCOLOGY | ENGAGEMENT | SOLUBLE MICA | CYTOTOXICITY | T-CELLS | ADAM17 Protein | Immunologic Surveillance | Neoplasms - metabolism | T-Lymphocyte Subsets - immunology | Amyloid Precursor Protein Secretases - genetics | Prostatic Neoplasms - metabolism | Pancreatic Neoplasms - metabolism | Breast Neoplasms - immunology | Humans | Carcinoma, Pancreatic Ductal - metabolism | Male | Exosomes | Breast Neoplasms - metabolism | Prostatic Neoplasms - immunology | Histocompatibility Antigens Class I - metabolism | NK Cell Lectin-Like Receptor Subfamily K - metabolism | RNA Interference | Killer Cells, Natural - immunology | Female | Membrane Proteins - metabolism | Carcinoma, Pancreatic Ductal - immunology | Tumor Escape - immunology | ADAM Proteins - antagonists & inhibitors | Membrane Proteins - genetics | Dipeptides - pharmacology | Histocompatibility Antigens Class I - immunology | ADAM10 Protein | Matrix Metalloproteinase Inhibitors - pharmacology | ADAM Proteins - metabolism | Amyloid Precursor Protein Secretases - metabolism | Membrane Proteins - antagonists & inhibitors | Neoplasms - immunology | Pancreatic Neoplasms - immunology | Cell Line, Tumor | RNA, Small Interfering | Amyloid Precursor Protein Secretases - antagonists & inhibitors | ADAM Proteins - genetics | Tetraspanin-29 - metabolism | Cytokines - biosynthesis | T cells | Proteases | Analysis | Enzyme-linked immunosorbent assay | Tumors | Ligands | Immunology | Immune system | Index Medicus | ADAM10 protein
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6. Full Text Blocking ADAM10 synaptic trafficking generates a model of sporadic Alzheimer's disease
by Epis, Roberta and Marcello, Elena and Gardoni, Fabrizio and Vastagh, Csaba and Malinverno, Matteo and Balducci, Claudia and Colombo, Alessio and Borroni, Barbara and Vara, Hugo and Dell'Agli, Mario and Cattabeni, Flamino and Giustetto, Maurizio and Borsello, Tiziana and Forloni, Gianluigi and Padovani, Alessandro and Di Luca, Monica
Brain, ISSN 0006-8950, 11/2010, Volume 133, Issue 11, pp. 3323 - 3335
We describe here an innovative, non-transgenic animal model of Alzheimer's disease. This model mimics early stages of sporadic disease, which represents the... 
amyloid precursor protein metabolism | SAP97 | NMDA | synaptopathy | animal models | SECRETASE CLEAVAGE | AMYLOID-PRECURSOR-PROTEIN | COGNITIVE IMPAIRMENT | TRIPLE-TRANSGENIC MODEL | NMDA RECEPTOR TRAFFICKING | NEUROSCIENCES | OLIGOMERS | CLINICAL NEUROLOGY | INTRACELLULAR A-BETA | MOUSE MODEL | IN-VIVO | PLASTICITY | Alzheimer Disease - etiology | Molecular Sequence Data | Male | Protein Transport - physiology | Multiprotein Complexes - antagonists & inhibitors | Multiprotein Complexes - metabolism | Neural Inhibition - physiology | Synapses - metabolism | Time Factors | Adaptor Proteins, Signal Transducing - antagonists & inhibitors | Membrane Proteins - metabolism | Disease Models, Animal | Amino Acid Sequence | Nerve Tissue Proteins - antagonists & inhibitors | Alzheimer Disease - physiopathology | ADAM Proteins - antagonists & inhibitors | Discs Large Homolog 1 Protein | Mice, Inbred C57BL | ADAM10 Protein | Synapses - enzymology | Nerve Tissue Proteins - metabolism | ADAM Proteins - metabolism | Amyloid Precursor Protein Secretases - metabolism | Animals | Guanylate Kinases | Membrane Proteins - antagonists & inhibitors | Alzheimer Disease - metabolism | Mice | Amyloid Precursor Protein Secretases - antagonists & inhibitors | Adaptor Proteins, Signal Transducing - metabolism | Index Medicus | Abridged Index Medicus
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7. Full Text Metalloprotease-mediated tumor cell shedding of B7-H6, the ligand of the natural killer cell-activating receptor NKp30
by Schlecker, Eva and Fiegler, Nathalie and Arnold, Annette and Altevogt, Peter and Rose-John, Stefan and Moldenhauer, Gerhard and Sucker, Antje and Paschen, Annette and Von Strandmann, Elke Pogge and Textor, Sonja and Cerwenka, Adelheid
Cancer Research, ISSN 0008-5472, 07/2014, Volume 74, Issue 13, pp. 3429 - 3440
Natural killer (NK) cells are potent immune effector cells capable of mediating antitumor responses. Thus, during immunoediting, tumor cell populations evolve... 
NKG2D LIGANDS | BREAST-CANCER | NK CELLS | ONCOLOGY | DOWN-REGULATION | CHAIN-RELATED MOLECULE | MYELOID CELLS | ANTITUMOR-ACTIVITY | MALIGNANT DISEASES | UP-REGULATION | CUTTING EDGE | ADAM17 Protein | Melanoma - blood | Amyloid Precursor Protein Secretases - genetics | Tumor Escape | Phenylalanine - analogs & derivatives | Phenylalanine - pharmacology | Humans | B7 Antigens - blood | ADAM Proteins - biosynthesis | Protease Inhibitors - pharmacology | RNA, Messenger - biosynthesis | Lymphocyte Activation - immunology | MCF-7 Cells | RNA Interference | B7 Antigens - genetics | B7 Antigens - secretion | Killer Cells, Natural - immunology | Natural Cytotoxicity Triggering Receptor 3 - immunology | Hydroxamic Acids - pharmacology | ADAM Proteins - antagonists & inhibitors | Membrane Proteins - genetics | Dipeptides - pharmacology | HCT116 Cells | ADAM10 Protein | Thiophenes - pharmacology | Melanoma - pathology | Up-Regulation - drug effects | Membrane Proteins - biosynthesis | Membrane Proteins - antagonists & inhibitors | Cell Line, Tumor | RNA, Small Interfering | Amyloid Precursor Protein Secretases - antagonists & inhibitors | HeLa Cells | ADAM Proteins - genetics | Amyloid Precursor Protein Secretases - biosynthesis | Index Medicus
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8. Full Text Holo-APP and G-protein-mediated signaling are required for sAPPα-induced activation of the Akt survival pathway
by Milosch, N and Tanriöver, G and Kundu, A and Rami, A and François, J.-C and Baumkötter, F and Weyer, S.W and Samanta, A and Jäschke, A and Brod, F and Buchholz, C.J and Kins, S and Behl, C and Müller, U.C and Kögel, D
Cell Death and Disease, ISSN 2041-4889, 2014, Volume 5, Issue 8, pp. e1391 - e1391
Accumulating evidence indicates that loss of physiologic amyloid precursor protein (APP) function leads to reduced neuronal plasticity, diminished synaptic... 
TAU PHOSPHORYLATION | SECRETED FORMS | BRAIN-INJURY | ALZHEIMERS-DISEASE | FAMILY-MEMBERS | STRESS-INDUCED APOPTOSIS | COUPLED RECEPTORS | HIPPOCAMPAL-NEURONS | INTRACELLULAR DOMAIN AICD | AMYLOID-PRECURSOR PROTEIN | CELL BIOLOGY | Humans | Phosphatidylinositol 3-Kinases - metabolism | Recombinant Proteins - biosynthesis | Phosphatidylinositol 3-Kinases - antagonists & inhibitors | Amyloid beta-Protein Precursor - metabolism | Membrane Proteins - metabolism | Proto-Oncogene Proteins c-akt - metabolism | Hydroxamic Acids - pharmacology | Amyloid beta-Protein Precursor - deficiency | Cell Line | Cell Survival - drug effects | ADAM Proteins - antagonists & inhibitors | Dipeptides - pharmacology | Mice, Inbred C57BL | ADAM10 Protein | Hippocampus - pathology | Recombinant Proteins - genetics | Recombinant Proteins - pharmacology | Amino Acid Motifs | Mice, Knockout | Hippocampus - metabolism | ADAM Proteins - metabolism | Amyloid Precursor Protein Secretases - metabolism | Amyloid beta-Protein Precursor - genetics | Animals | Membrane Proteins - antagonists & inhibitors | Signal Transduction - drug effects | Mice | Amyloid Precursor Protein Secretases - antagonists & inhibitors | In Vitro Techniques | Pertussis Toxin - toxicity | Index Medicus | Original
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9. Full Text ADAM10: A new player in breast cancer progression?
by Mullooly, Maeve and McGowan, Patricia M and Kennedy, Susan A and Madden, Stephen F and Crown, John and O'Donovan, Norma and Duffy, Michael J
British Journal of Cancer, ISSN 0007-0920, 09/2015, Volume 113, Issue 6, pp. 945 - 951
Background: The ADAM proteases are best known for their role in shedding the extracellular domain of transmembrane proteins. Among the transmembrane proteins... 
targeted therapy | TRANSLOCATION | ACTIVATION | ADAM10 | breast cancer | E-CADHERIN | ADAM-10 | CLEAVAGE | EGFR | invasion | inhibitor | ONCOLOGY | DISINTEGRIN | migration | CELL-CELL ADHESION | EXPRESSION | Cell Count | Humans | Middle Aged | Neoplasm Proteins - antagonists & inhibitors | Neoplasm Proteins - metabolism | RNA, Messenger - metabolism | Gene Knockdown Techniques | RNA Interference | Triple Negative Breast Neoplasms - pathology | Female | Membrane Proteins - metabolism | Hydroxamic Acids - pharmacology | ADAM Proteins - antagonists & inhibitors | Neoplasm Invasiveness | Dipeptides - pharmacology | ADAM10 Protein | Disease Progression | Cell Movement - drug effects | Disease-Free Survival | ADAM Proteins - metabolism | Amyloid Precursor Protein Secretases - metabolism | Membrane Proteins - antagonists & inhibitors | Triple Negative Breast Neoplasms - metabolism | Cell Line, Tumor | Amyloid Precursor Protein Secretases - antagonists & inhibitors | Index Medicus | Molecular Diagnostics
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10. Full Text The ADAM10 Prodomain Is a Specific Inhibitor of ADAM10 Proteolytic Activity and Inhibits Cellular Shedding Events
by Marcia L. Moss and Martha Bomar and Qian Liu and Harvey Sage and Peter Dempsey and Patricia M. Lenhart and Patricia A. Gillispie and Alexander Stoeck and Dirk Wildeboer and Jörg W. Bartsch and Ralf Palmisano and Pei Zhou
Journal of Biological Chemistry, ISSN 0021-9258, 12/2007, Volume 282, Issue 49, pp. 35712 - 35721
ADAM10 is a disintegrin metalloproteinase that processes amyloid precursor protein and ErbB ligands and is involved in the shedding of many type I and type II... 
CALCIUM INFLUX | CYSTEINE SWITCH | DOMAIN | MATRIX-METALLOPROTEINASES | ALPHA-CONVERTING ENZYME | BIOCHEMISTRY & MOLECULAR BIOLOGY | RECEPTOR | CLEAVAGE | DISINTEGRIN METALLOPROTEASE | FAMILY | PROTEASES | ADAM17 Protein | ADAM Proteins - therapeutic use | Humans | Cercopithecus aethiops | Membrane Proteins - therapeutic use | Antigens, CD - metabolism | Intercellular Signaling Peptides and Proteins - metabolism | Receptor, Epidermal Growth Factor - metabolism | Amyloid beta-Protein Precursor - metabolism | Disintegrins - therapeutic use | Enzyme Precursors - antagonists & inhibitors | Membrane Proteins - metabolism | ADAM Proteins - antagonists & inhibitors | Disintegrins - metabolism | ADAM10 Protein | Neoplasms - enzymology | Neoplasms - drug therapy | Amyloid Precursor Protein Secretases - therapeutic use | ADAM Proteins - metabolism | Amyloid Precursor Protein Secretases - metabolism | Enzyme Precursors - metabolism | Animals | Betacellulin | Membrane Proteins - antagonists & inhibitors | Enzyme Precursors - therapeutic use | Mice | Amyloid Precursor Protein Secretases - antagonists & inhibitors | Disintegrins - antagonists & inhibitors | COS Cells | Protein Structure, Tertiary - physiology | Index Medicus
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11. Full Text Macrocyclic θ-defensins suppress tumor necrosis factor-α (TNF-α) shedding by inhibition of TNF-α-converting enzyme
by Schaal, Justin B and Maretzky, Thorsten and Tran, Dat Q and Tran, Patti A and Tongaonkar, Prasad and Blobel, Carl P and Ouellette, André J and Selsted, Michael E
Journal of Biological Chemistry, ISSN 0021-9258, 2018, Volume 293, Issue 8, pp. 2725 - 2734
Theta-defensins (theta-defensins) are macrocyclic peptides expressed exclusively in granulocytes and selected epithelia of Old World monkeys. They contribute... 
ADAM17 | EPITHELIAL-CELLS | ANTIMICROBIAL ACTIVITIES | SIGNALING PATHWAY | BIOCHEMISTRY & MOLECULAR BIOLOGY | INDUCED ARTHRITIS | TACE | THERAPEUTIC TARGETS | NF-KAPPA-B | CYCLIC-PEPTIDES | EGFR | Tumor Necrosis Factor-alpha - metabolism | Amyloid Precursor Protein Secretases - genetics | Intestinal Mucosa - metabolism | ADAM10 Protein - genetics | Humans | Colon - drug effects | ADAM10 Protein - metabolism | Cercopithecus aethiops | Anti-Inflammatory Agents, Non-Steroidal - chemistry | Colon - immunology | Monocytes - metabolism | Macaca mulatta | Monocytes - immunology | Defensins - chemistry | Intestinal Mucosa - drug effects | ADAM17 Protein - metabolism | Anti-Inflammatory Agents, Non-Steroidal - pharmacology | Leukocytes - immunology | Proteolysis - drug effects | ADAM10 Protein - antagonists & inhibitors | ADAM17 Protein - antagonists & inhibitors | Intestinal Mucosa - immunology | Protein Isoforms - chemistry | Defensins - pharmacology | Membrane Proteins - metabolism | Toll-Like Receptors - metabolism | Escherichia coli - physiology | Recombinant Proteins - metabolism | Cell Line | Lipopolysaccharides - toxicity | Membrane Proteins - genetics | Solubility | Escherichia coli - immunology | Recombinant Proteins - chemistry | Colon - metabolism | Toll-Like Receptors - agonists | Monocytes - drug effects | Protein Isoforms - pharmacology | ADAM17 Protein - genetics | Amyloid Precursor Protein Secretases - metabolism | Animals | Tumor Necrosis Factor-alpha - chemistry | Membrane Proteins - antagonists & inhibitors | Leukocytes - drug effects | Protein Conformation | Amyloid Precursor Protein Secretases - antagonists & inhibitors | Leukocytes - metabolism | Tumor Necrosis Factor-alpha - antagonists & inhibitors | Index Medicus | cytokine | tumor necrosis factor (TNF) | proteolytic enzyme | theta defensin | shedding | ADAM | Immunology | enzyme inhibitor | inflammation | defensin | sheddase inhibitors
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12. Full Text Constitutive α- and β-secretase cleavages of the amyloid precursor protein are partially coupled in neurons, but not in frequently used cell lines
by Colombo, Alessio and Wang, Huanhuan and Kuhn, Peer-Hendrik and Page, Richard and Kremmer, Elisabeth and Dempsey, Peter J and Crawford, Howard C and Lichtenthaler, Stefan F
Neurobiology of Disease, ISSN 0969-9961, 2012, Volume 49, Issue 1, pp. 137 - 147
Abstract Proteolytic cleavage of the amyloid precursor protein (APP) by the two proteases α- and β-secretases controls the generation of the amyloid β peptide... 
Neurology | Beta-secretase | Alpha-secretase | Alzheimer's disease | Amyloid precursor protein | APP | ACTIVATION | ALZHEIMERS-DISEASE | ADAM10 | METALLOPROTEINASES | NEUROSCIENCES | RETINOIC ACID | DEGRADATION | INHIBITORS | UP-REGULATION | DERIVATIVES | Amyloid Precursor Protein Secretases - genetics | Humans | Aspartic Acid Endopeptidases - genetics | Gene Knockdown Techniques | Protease Inhibitors - pharmacology | Amyloid beta-Protein Precursor - metabolism | HEK293 Cells | Membrane Proteins - metabolism | Cerebral Cortex - drug effects | Neurons - drug effects | Cerebral Cortex - enzymology | ADAM Proteins - antagonists & inhibitors | Aspartic Acid Endopeptidases - antagonists & inhibitors | Membrane Proteins - genetics | Cells, Cultured | ADAM10 Protein | Mice, Knockout | ADAM Proteins - metabolism | Amyloid Precursor Protein Secretases - metabolism | Animals | Membrane Proteins - antagonists & inhibitors | Aspartic Acid Endopeptidases - metabolism | Neurons - enzymology | Cell Line, Tumor | Amyloid Precursor Protein Secretases - antagonists & inhibitors | ADAM Proteins - genetics | Index Medicus | Alzheimer’s disease
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13. Full Text ADAM10 Regulates Endothelial Permeability and T-Cell Transmigration by Proteolysis of Vascular Endothelial Cadherin
by Schulz, Beate and Pruessmeyer, Jessica and Maretzky, Thorsten and Ludwig, Andreas and Blobel, Carl P and Saftig, Paul and Reiss, Karina
Circulation Research, ISSN 0009-7330, 05/2008, Volume 102, Issue 10, pp. 1192 - 1201
Vascular endothelial (VE)-cadherin is the major adhesion molecule of endothelial adherens junctions. It plays an essential role in controlling endothelial... 
MIGRATION | endothelium | CARDIAC & CARDIOVASCULAR SYSTEMS | THROMBIN | BETA-CATENIN | CLEAVAGE | endothelial permeability | DISINTEGRIN-LIKE METALLOPROTEINASES | LEUKOCYTE TRANSMIGRATION | VE-cadherin | JUNCTIONS | PERIPHERAL VASCULAR DISEASE | metalloprotease | GROWTH-FACTOR | HEMATOLOGY | N-CADHERIN | Amyloid Precursor Protein Secretases - genetics | Capillary Permeability - physiology | Cadherins - metabolism | Calcium - metabolism | Humans | Capillary Permeability - drug effects | Adherens Junctions - immunology | Hemostatics - pharmacology | Adherens Junctions - metabolism | Antigens, CD - metabolism | Cell Movement - immunology | Thrombin - pharmacology | Protein Kinase C - metabolism | Membrane Proteins - metabolism | Umbilical Veins - cytology | ADAM Proteins - antagonists & inhibitors | Endothelial Cells - metabolism | Membrane Proteins - genetics | Cells, Cultured | Enzyme Inhibitors - pharmacology | ADAM10 Protein | Endothelial Cells - immunology | ADAM Proteins - metabolism | Amyloid Precursor Protein Secretases - metabolism | Membrane Proteins - antagonists & inhibitors | T-Lymphocytes - cytology | Leukocyte Rolling - physiology | T-Lymphocytes - immunology | RNA, Small Interfering | Amyloid Precursor Protein Secretases - antagonists & inhibitors | ADAM Proteins - genetics | Index Medicus
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14. Full Text NK cell CD16 surface expression and function is regulated by a disintegrin and metalloprotease-17 (ADAM17)
by Romee, Rizwan and Foley, Bree and Lenvik, Todd and Wang, Yue and Zhang, Bin and Ankarlo, Dave and Luo, Xianghua and Cooley, Sarah and Verneris, Mike and Walcheck, Bruce and Miller, Jeffrey
Blood, ISSN 0006-4971, 05/2013, Volume 121, Issue 18, pp. 3599 - 3608
The Fc receptor CD16 is present on essentially all CD56(dim) peripheral blood natural killer (NK) cells. Upon recognition of antibody-coated cells it delivers... 
MHC CLASS-I | ACTIVATION | FC-GAMMA-RIII | IFN-GAMMA | NEUTROPHILS | LYMPHOMA | INHIBITORY RECEPTORS | CYTOKINE | TNF-ALPHA | NATURAL CYTOTOXICITY | HEMATOLOGY | ADAM17 Protein | ADAM Proteins - antagonists & inhibitors | Receptors, IgG - physiology | ADAM Proteins - physiology | Humans | Cells, Cultured | Enzyme Inhibitors - pharmacology | Protein Transport - drug effects | GPI-Linked Proteins - metabolism | Receptors, IgG - metabolism | L-Selectin - metabolism | ADAM Proteins - metabolism | Protein Processing, Post-Translational - drug effects | Lymphocyte Activation - drug effects | K562 Cells | GPI-Linked Proteins - physiology | Benzimidazoles - pharmacology | Cell Membrane - metabolism | Killer Cells, Natural - drug effects | Killer Cells, Natural - metabolism | Cell Membrane - drug effects | Index Medicus | Abridged Index Medicus | Immunobiology
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