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Molecular Biotechnology, ISSN 1073-6085, 6/2003, Volume 24, Issue 2, pp. 157 - 202
Metalloendopeptidases are present across all kingdoms of living organisms; they are ubiquitous and widely involved in metabolism regulation through their... 
adamalysin | Neurosciences | astacin | reprolysin | serralysin | X-ray crystal structure | Neurology | ADAM | MMP | metzincin | Biomedicine | three-dimensional structure | Zinc metalloproteinase | vertebrate collagenase | leishmanolysin | matrix metalloproteinase | metalloendopeptidase | Metalloendopeptidase | Vertebrate collagenase | Astacin | Matrix metalloproteinase | Metzincin | Serralysin | Adamalysin | Three-dimensional structure | Reprolysin | Leishmanolysin | SNAKE-VENOM METALLOPROTEINASE | 1.8-ANGSTROM CRYSTAL-STRUCTURE | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | HUMAN NEUTROPHIL COLLAGENASE | zinc metalloproteinase | BIOCHEMISTRY & MOLECULAR BIOLOGY | ALPHA-CONVERTING-ENZYME | NECROSIS-FACTOR-ALPHA | HUMAN FIBROBLAST COLLAGENASE | SITE-DIRECTED MUTAGENESIS | AMINO-ACID-SEQUENCE | HUMAN MATRIX-METALLOPROTEINASE | ZINC-BINDING SITES | Metalloendopeptidases - genetics | Protein Structure, Tertiary | Amino Acid Sequence | Humans | Metalloproteases - genetics | Models, Molecular | Molecular Sequence Data | Metalloendopeptidases - classification | Zinc - chemistry | Animals | Metalloendopeptidases - chemistry | Conserved Sequence | Protein Binding | Protein Conformation | Enzyme Activation | Metalloproteases - classification | Binding Sites | Metalloproteases - chemistry | Physiological aspects | Structure | Crystals | Proteins | Peptides | Zinc | Binding sites
Journal Article
BIOCHEMICAL JOURNAL, ISSN 0264-6021, 02/2005, Volume 386, Issue Pt 1, pp. 15 - 27
The ADAMTSs ((a) under bar (d) under bar isintegrin (a) under bar nd (m) under bar etalloprotemase with (t) under bar hrombo (s) under bar pondin motifs) are a... 
aggrecanase | angiogenesis | metalloproteinase | MULTIPLE THROMBOSPONDIN-1 REPEATS | BIOCHEMISTRY & MOLECULAR BIOLOGY | I N-PROTEINASE | ALPHA-CONVERTING-ENZYME | NECROSIS-FACTOR-ALPHA | THROMBOTIC THROMBOCYTOPENIC PURPURA | VON-WILLEBRAND-FACTOR | FACTOR-CLEAVING PROTEASE | proteoglycan | CAENORHABDITIS-ELEGANS | tissue inhibitor of metalloprotemase (TIMP) | GENE FAMILY | EXTRACELLULAR-MATRIX | extracellular matrix | Metalloendopeptidases - genetics | Protein Structure, Tertiary | Multigene Family | Neoplasm Proteins - biosynthesis | Angiogenesis Inhibitors - physiology | Humans | Neoplasm Proteins - physiology | Rats | Substrate Specificity | Terminology as Topic | Metalloendopeptidases - classification | Forecasting | Gene Expression Regulation, Enzymologic | Metalloendopeptidases - biosynthesis | Protease Inhibitors - pharmacology | Animals | Cloning, Molecular | Metalloendopeptidases - chemistry | Metalloendopeptidases - physiology | Neoplasm Proteins - genetics | Extracellular Matrix Proteins - metabolism | SPC, subtilisin-like pro-protein convertase | TS, thrombospondin type I-like | ECM, extracellular matrix | TSP1 | embryonic sea urchin protein Uegf | Review | TTP, thrombotic thrombocytopaenic purpura | 2, thrombospondin 1 and 2 respectively | ADAMTSL, ADAMTS-like | ADAM, adisintegrin and metalloproteinase-like (or, alternatively, adamalysin) | ADAMTS, adisintegrin and metalloproteinase with thrombospondin motifs (or, alternatively, adamalysin–thrombospondin) | bone morphogenic protein 1 | CUB, complement subcomponent C1r | IGD, interglobular domain | C1s | EDS, Ehlers–Danlos syndrome | tissue inhibitor of metalloproteinase (TIMP) | GAG, glycosaminoglycan | VEGF, vascular endothelial growth factor | MMP(I), matrix metalloproteinase (inhibitor) | PLAC domain, protease and lacunin domain | IL, interleukin | TIMP, tissue inhibitor of metalloproteinase | vWF(CP), von Willebrand factor (cleaving protease)
Journal Article
Breast Cancer Research, ISSN 1465-5411, 2000, Volume 2, Issue 4, pp. 252 - 257
The matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases. Their primary function is degradation of proteins in the extracellular... 
Tissue inhibitor of metalloproteinase | Breast cancer | Matrix metalloproteinases | Metastasis | Carcinogenesis | Invasion | CANCER-CELLS | ANGIOGENESIS | BATIMASTAT | breast cancer | carcinogenesis | invasion | ONCOLOGY | metastasis | tissue inhibitor of metalloproteinase | ECTODOMAIN | GROWTH | STROMELYSIN-3 | TISSUE INHIBITOR | matrix metalloproteinases | EXPRESSION | CARCINOMA | Metalloendopeptidases - genetics | Prognosis | Humans | Neoplasm Proteins - physiology | Substrate Specificity | Neoplasm Proteins - antagonists & inhibitors | Biomarkers, Tumor | Neovascularization, Pathologic - enzymology | Breast Neoplasms - enzymology | Neoplasm Metastasis | Female | Neoplasm Proteins - genetics | Protease Inhibitors - therapeutic use | Extracellular Matrix Proteins - metabolism | Metalloendopeptidases - antagonists & inhibitors | Protein Structure, Tertiary | Neoplasm Proteins - classification | Neoplasm Invasiveness | Neoplasm Proteins - chemistry | Metalloendopeptidases - classification | Basement Membrane - metabolism | Breast Neoplasms - drug therapy | Disease Progression | Breast Neoplasms - genetics | Breast Neoplasms - pathology | Metalloendopeptidases - chemistry | Metalloendopeptidases - physiology | Apoptosis | Growth Substances - metabolism | Receptors, Growth Factor - metabolism | Proteins | Prevention | Proteases | Proteolysis | Analysis | Development and progression | Cancer | Review
Journal Article
Nature, ISSN 0028-0836, 03/2005, Volume 434, Issue 7033, pp. 648 - 652
Journal Article
Biochemical Journal, ISSN 0264-6021, 09/2007, Volume 406, Issue 2, pp. 355 - 363
Injuries caused by brown spiders (Loxosceles genus) are associated with dermonecrotic lesions with gravitational spreading and systemic manifestations. The... 
Metalloprotease | Spider | Toxin | Astacin | Venom | Loxosceles astacin-like protease (LALP) | astacin | SNAKE-VENOM | PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | METALLOENDOPEPTIDASES | FAMILY | DERMONECROTIC TOXIN | venom | toxin | RECLUSA | ENDOTHELIAL-CELLS | MOLECULAR-CLONING | EXTRACELLULAR-MATRIX | metalloprotease | spider | HYALURONIDASES | Metalloendopeptidases - genetics | Spider Venoms - genetics | Humans | DNA, Complementary - genetics | Molecular Sequence Data | Metalloendopeptidases - metabolism | Phylogeny | Base Sequence | Cloning, Molecular | Spiders - genetics | Circular Dichroism | Spider Venoms - chemistry | Spiders - chemistry | Amino Acid Sequence | Rabbits | Gene Expression | Protein Structure, Secondary | Cells, Cultured | Spiders - classification | Fibronectins - metabolism | Spider Venoms - enzymology | Sequence Homology, Amino Acid | Metalloendopeptidases - toxicity | Sequence Alignment | Animals | Fibrinogen - metabolism | Metalloendopeptidases - chemistry | Spider Venoms - toxicity | Cell Proliferation - drug effects | Gelatin - metabolism | Spiders - enzymology | Endothelial Cells - drug effects | LALP, Loxosceles astacin-like protease | Ni-NTA, Ni2+-nitrilotriacetate | IPTG, isopropyl β-D-thiogalactoside | LB, Luria–Bertani | SPAN, Strongylocentrotus purpuratus astacin-like protease
Journal Article
Journal Article
Proceedings of the National Academy of Sciences, ISSN 0027-8424, 07/2011, Volume 108, Issue 30, pp. 12325 - 12330
Journal Article
Cell Metabolism, ISSN 1550-4131, 12/2012, Volume 16, Issue 6, pp. 738 - 750
Journal Article