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Biochemistry, ISSN 0006-2960, 01/2008, Volume 47, Issue 2, pp. 537 - 547
Human ADAM12 (a disintegrin and metalloproteinase) is a multidomain zinc metalloproteinase expressed at high levels during development and in human tumors.... 
HUMAN STROMELYSIN-1 | 12 MELTRIN ALPHA | MATRIX-METALLOPROTEINASES | ALPHA-CONVERTING ENZYME | MITOCHONDRIAL PROCESSING PEPTIDASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | EPIDERMAL-GROWTH-FACTOR | METALLOPROTEINASE INHIBITORS | TISSUE INHIBITOR | CRYSTAL-STRUCTURES | VON-WILLEBRAND-FACTOR | Sequence Deletion | Sodium Chloride - pharmacology | Humans | Molecular Sequence Data | Mutant Proteins - isolation & purification | Protein Isoforms - isolation & purification | Recombinant Proteins - isolation & purification | ADAM12 Protein | Sequence Analysis, Protein | Protein Isoforms - metabolism | Protein Isoforms - chemistry | Membrane Proteins - metabolism | Catalysis | Mutant Proteins - antagonists & inhibitors | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amino Acid Sequence | Membrane Proteins - isolation & purification | ADAM Proteins - antagonists & inhibitors | Calcium - pharmacology | Guinea Pigs | ADAM Proteins - chemistry | Electrophoresis, Polyacrylamide Gel | Recombinant Proteins - chemistry | Mutant Proteins - metabolism | ADAM Proteins - isolation & purification | Tissue Inhibitor of Metalloproteinases - metabolism | ADAM Proteins - metabolism | Animals | Substrate Specificity - drug effects | Membrane Proteins - antagonists & inhibitors | Membrane Proteins - chemistry | Mutant Proteins - chemistry | Kinetics | Transferrin - metabolism | Protein Isoforms - antagonists & inhibitors | Hydrogen-Ion Concentration | Metals - pharmacology | Physiological aspects | Transferrin | Research | Chemical properties | Metalloproteins | Index Medicus
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 02/2016, Volume 291, Issue 7, pp. 3197 - 3208
The metalloproteinase ADAMTS-5 (A disintegrin and metalloproteinase with thrombospondin motifs) degrades aggrecan, a proteoglycan essential for cartilage... 
SYNOVIAL-FLUID | BIOCHEMISTRY & MOLECULAR BIOLOGY | cartilage | FUNCTIONAL DIFFERENCES | oligomer | ADAMTS | AGGRECAN INTERGLOBULAR DOMAIN | cartilage biology | VON-WILLEBRAND-FACTOR | PROTEOLYTIC ACTIVITIES | aggrecan | ADAMTS5 | NONCATALYTIC DOMAINS | OSTEOARTHRITIC CARTILAGE | oligomerization | PROCOLLAGEN N-PROTEINASE | ARTICULAR-CARTILAGE | IN-VIVO | metalloprotease | Recombinant Fusion Proteins - isolation & purification | Molecular Weight | Humans | Knee Joint - enzymology | Recombinant Fusion Proteins - metabolism | Arthritis, Experimental - pathology | Knee Joint - pathology | Knee Joint - immunology | Mice, Mutant Strains | Proteolysis | Gene Deletion | HEK293 Cells | Protein Interaction Domains and Motifs | Dimerization | Peptide Fragments - genetics | ADAMTS5 Protein | Catalytic Domain | Peptide Fragments - metabolism | Cross-Linking Reagents - chemistry | ADAM Proteins - chemistry | Peptide Fragments - isolation & purification | Mice, Inbred C57BL | Arthritis, Experimental - immunology | ADAM Proteins - isolation & purification | Aggrecans - isolation & purification | Aggrecans - metabolism | Recombinant Fusion Proteins - chemistry | Mutant Proteins | ADAM Proteins - metabolism | Peptide Fragments - chemistry | Animals | Arthritis, Experimental - enzymology | Enzyme Activation | ADAM Proteins - genetics | Crosses, Genetic | Index Medicus | Molecular Bases of Disease
Journal Article
Toxicon, ISSN 0041-0101, 08/2016, Volume 118, pp. 1 - 12
Journal Article
Journal Article
Nature, ISSN 0028-0836, 02/1997, Volume 385, Issue 6618, pp. 733 - 736
Journal Article
Biochemical and Biophysical Research Communications, ISSN 0006-291X, 11/2000, Volume 278, Issue 3, pp. 511 - 515
Journal Article
Journal Article
Biological Chemistry, ISSN 1431-6730, 03/2006, Volume 387, Issue 3, pp. 337 - 346
ADAM proteases are type I transmembrane proteins with extracellular metalloprotease domains. As for most ADAM family members, ADAM8 (CD156a, MS2) is involved... 
Peptide cleavage | Candidate substrates | ADAM protease | Fluorescence assay | Ectodomain shedding | SELECTIN GLYCOPROTEIN LIGAND-1 | ectodomain shedding | BIOCHEMISTRY & MOLECULAR BIOLOGY | SECRETASE CLEAVAGE | ALPHA-CONVERTING-ENZYME | CELL-ADHESION | AMYLOID PRECURSOR PROTEIN | FAMILY | TUMOR-NECROSIS-FACTOR | IN-VITRO | candidate substrates | fluorescence assay | CATALYTIC-ACTIVITY | peptide cleavage | ALZHEIMERS | Metalloproteases - isolation & purification | Kidney - embryology | Humans | Molecular Sequence Data | Metalloproteases - metabolism | Inflammation - metabolism | Amyloid Precursor Protein Secretases | Amyloid beta-Protein Precursor - metabolism | Platelet Aggregation Inhibitors - pharmacology | Membrane Proteins - metabolism | Disintegrins - chemistry | Metalloproteases - chemistry | Amino Acid Sequence | Membrane Proteins - isolation & purification | Disintegrins - metabolism | ADAM Proteins - chemistry | Cells, Cultured | Gene Expression Regulation | ADAM10 Protein | Kidney - cytology | ADAM Proteins - isolation & purification | Disintegrins - isolation & purification | Neurodegenerative Diseases - metabolism | ADAM Proteins - metabolism | Peptide Fragments - chemistry | Membrane Proteins - chemistry | Escherichia coli - genetics | Peptides | Proteases | Escherichia coli | Amyloid beta-protein | Fluorescence | Amino acids | Inflammation | Myelin proteins | Tumors | Index Medicus
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 08/1999, Volume 274, Issue 33, pp. 23443 - 23450
Journal Article
Journal Article
Journal Article
International Journal of Biological Sciences, ISSN 1449-2288, 10/2008, Volume 4, Issue 6, pp. 387 - 396
The transmembrane protein ADAM22 is expressed at high levels in the brain. From its molecular structure, ADAM22 is thought to be an adhesion molecule or a... 
LGI1 | ADAM22 | GeLC-MS | LGI4 | ADAM23 | SYSTEM | BIOCHEMISTRY & MOLECULAR BIOLOGY | FAMILY | PEPTIDES | ADAM11-DEFICIENT MICE | EPILEPSY | MUTATIONS | PROTEINS | CELL | BRAIN | PROTEOMICS | Index Medicus
Journal Article