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1. Full Text Regulated transcription of human matrix metalloproteinase 13 (MMP13) and interleukin-1β (IL1B) genes in chondrocytes depends on methylation of specific proximal promoter CpG sites
by Hashimoto, Ko and Otero, Miguel and Imagawa, Kei and De Andrés, María C and Coico, Jonathan M and Roach, Helmtrud I and Oreffo, Richard O.C and Marcu, Kenneth B and Goldring, Mary B
Journal of Biological Chemistry, ISSN 0021-9258, 04/2013, Volume 288, Issue 14, pp. 10061 - 10072
The role of DNA methylation in the regulation of catabolic genes such as MMP13 and IL1B, which have sparse CpG islands, is poorly understood in the context of... 
RHEUMATOID-ARTHRITIS | MOLECULAR TARGET | DNA METHYLATION | SYNOVIAL TISSUE | EPIGENETIC MEMORY | BIOCHEMISTRY & MOLECULAR BIOLOGY | IN-VIVO | DOWN-REGULATION | HUMAN OSTEOARTHRITIC CHONDROCYTES | HUMAN ARTICULAR CHONDROCYTES | THERAPEUTIC INTERVENTION | Promoter Regions, Genetic | Epigenesis, Genetic | Humans | Transcriptional Activation | Osteoarthritis - metabolism | Gene Expression Profiling | Cartilage - metabolism | Plasmids - metabolism | Sequence Analysis, DNA | Interleukins - metabolism | Matrix Metalloproteinase 13 - metabolism | Gene Expression Regulation, Enzymologic | Point Mutation | DNA Methylation | Interleukin-1beta - metabolism | CpG Islands | Models, Genetic | Chondrocytes - metabolism | Index Medicus | Transcription Promoter | Molecular Bases of Disease | Cartilage | Interleukin | Hypoxia-inducible Factor (HIF) | Matrix Metalloproteinase (MMP)
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2. Full Text Diverse matrix metalloproteinase functions regulate cancer amoeboid migration
by Orgaz, Jose L and Pandya, Pahini and Dalmeida, Rimple and Karagiannis, Panagiotis and Sanchez-Laorden, Berta and Viros, Amaya and Albrengues, Jean and Nestle, Frank O and Ridley, Anne J and Gaggioli, Cedric and Marais, Richard and Karagiannis, Sophia N and Sanz-Moreno, Victoria
Nature Communications, ISSN 2041-1723, 06/2014, Volume 5, Issue 1, pp. 4255 - 4255
Rounded-amoeboid cancer cells use actomyosin contractility driven by Rho-ROCK and JAK-STAT3 to migrate efficiently. It has been suggested that rounded-amoeboid... 
LUNG METASTASIS | PERICELLULAR PROTEOLYSIS | GLIOBLASTOMA XENOGRAFT | SIGNALING COOPERATE | MULTIDISCIPLINARY SCIENCES | MATRIX-METALLOPROTEINASE-9 | TUMOR-CELL INVASION | HEMOPEXIN DOMAIN | CYTOSKELETAL DYNAMICS | MMP-9 | FOCAL ADHESIONS | Melanoma - metabolism | Signal Transduction | Neoplasm Invasiveness | Humans | Janus Kinases - metabolism | Melanoma - pathology | Actomyosin - metabolism | Matrix Metalloproteinase 13 - metabolism | Matrix Metalloproteinase 9 - metabolism | rho-Associated Kinases - metabolism | Cell Line, Tumor | STAT3 Transcription Factor - metabolism | Cell Movement | Index Medicus
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3. Full Text Cathepsin H–Mediated Degradation of HDAC4 for Matrix Metalloproteinase Expression in Hepatic Stellate Cells: Implications of Epigenetic Suppression of Matrix Metalloproteinases in Fibrosis through Stabilization of Class IIa Histone Deacetylases
by Yang, Zemin and Liu, Yu and Qin, Lan and Wu, Pengfei and Xia, Zanxian and Luo, Mei and Zeng, Yilan and Tsukamoto, Hidekazu and Ju, Zongyun and Su, Danmei and Kang, Han and Xiao, Zhixiong and Zheng, Sujun and Duan, Zhongping and Hu, Richard and Wang, Qiang and Pandol, Stephen J and Han, Yuan-Ping
American Journal of Pathology, ISSN 0002-9440, 04/2017, Volume 187, Issue 4, pp. 781 - 797
In three-dimensional extracellular matrix, mesenchymal cells including hepatic stellate cells (HSCs) gain the ability to express matrix metalloproteinases... 
ACTIVATION | TGF-BETA | LIVER | SEQUENCE | INJURY | II HISTONE DEACETYLASES | PATHOLOGY | INHIBITOR | TRANSCRIPTION FACTOR | MYOCYTE ENHANCER FACTOR-2 | MYOFIBROBLASTIC DIFFERENTIATION | Rats, Wistar | Humans | Extracellular Matrix - metabolism | Hepatic Stellate Cells - metabolism | Male | Cathepsin L - metabolism | Enzyme Stability - drug effects | Liver Cirrhosis - enzymology | RNA, Messenger - metabolism | Myofibroblasts - metabolism | Proteolysis - drug effects | Matrix Metalloproteinase 9 - metabolism | Cell Nucleus - metabolism | Biocatalysis - drug effects | Cell Transdifferentiation - drug effects | Protein Binding - drug effects | Liver Cirrhosis - metabolism | Epigenesis, Genetic - drug effects | Liver Cirrhosis - genetics | Repressor Proteins - metabolism | Recombinant Proteins - metabolism | Cell Line | Myofibroblasts - pathology | Extracellular Matrix - drug effects | Matrix Metalloproteinase 13 - genetics | RNA, Messenger - genetics | Histone Deacetylases - metabolism | Down-Regulation - drug effects | Myofibroblasts - drug effects | Subcellular Fractions - metabolism | Down-Regulation - genetics | Matrix Metalloproteinase 13 - metabolism | Cathepsin H - metabolism | Tumor Necrosis Factor-alpha - pharmacology | Animals | Liver Cirrhosis - pathology | Mice | Cell Nucleus - drug effects | Index Medicus | Abridged Index Medicus | Regular
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4. Full Text Matrix Metalloproteinase 12-Deficiency Augments Extracellular Matrix Degrading Metalloproteinases and Attenuates IL-13-Dependent Fibrosis
by Madala, Satish K and Pesce, John T and Ramalingam, Thirumalai R and Wilson, Mark S and Minnicozzi, Samantha and Cheever, Allen W and Thompson, Robert W and Mentink-Kane, Margaret M and Wynn, Thomas A
The Journal of Immunology, ISSN 0022-1767, 04/2010, Volume 184, Issue 7, pp. 3955 - 3963
Infection with the parasitic helminth Schistosoma mansoni causes significant liver fibrosis and extracellular matrix (ECM) remodeling. Matrix... 
RESPONSES | ACTIVATION | SCHISTOSOMA-MANSONI | INFLAMMATION | LIVER FIBROSIS | GENE-EXPRESSION PROFILES | MICE | IL-13 | IMMUNOLOGY | REVEAL | HEPATIC-FIBROSIS | Lung Diseases - metabolism | Cytokines - metabolism | Matrix Metalloproteinase 2 - metabolism | Extracellular Matrix - metabolism | Matrix Metalloproteinase 12 - metabolism | Interleukin-13 - metabolism | Liver Cirrhosis - enzymology | Reverse Transcriptase Polymerase Chain Reaction | Blotting, Western | Tissue Inhibitor of Metalloproteinases - metabolism | Matrix Metalloproteinase 13 - metabolism | Mice, Knockout | Schistosomiasis mansoni - metabolism | Microscopy, Confocal | Matrix Metalloproteinase 9 - metabolism | Animals | Fibrosis | Liver Cirrhosis - pathology | Mice | Lung Diseases - pathology | Schistosomiasis mansoni - pathology | Index Medicus | Abridged Index Medicus
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5. Full Text Matrix metalloproteinase 13‐containing exosomes promote nasopharyngeal carcinoma metastasis
by You, Yiwen and Shan, Ying and Chen, Jing and Yue, Huijun and You, Bo and Shi, Si and Li, Xingyu and Cao, Xiaolei
Cancer Science, ISSN 1347-9032, 12/2015, Volume 106, Issue 12, pp. 1669 - 1677
Nasopharyngeal cancer ( NPC ) is an endemic type of head and neck cancer with a high rate of cervical lymph node metastasis. Metastasis is the major cause of... 
microenvironment nasopharyngeal carcinoma | MMP13 | Exosomes | metastasis | Metastasis | Microenvironment nasopharyngeal carcinoma | MIGRATION | COLLAGENASE-3 EXPRESSION | CELLS | ANGIOGENESIS | IDENTIFICATION | CANCER | SECRETED EXOSOMES | INVASION | ONCOLOGY | PROGRESSION | Exosomes - metabolism | Immunohistochemistry | Nasopharyngeal Carcinoma | Carcinoma | Neoplasm Invasiveness | Epithelial-Mesenchymal Transition - physiology | Humans | Nasopharyngeal Neoplasms - enzymology | Neovascularization, Pathologic | Tumor Microenvironment - physiology | Blotting, Western | Matrix Metalloproteinase 13 - metabolism | Nasopharyngeal Neoplasms - pathology | Nasopharyngeal Neoplasms - blood supply | Neoplasm Metastasis | Transfection | RNA, Small Interfering | Real-Time Polymerase Chain Reaction | Analysis | Cancer | Index Medicus | Original
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6. Full Text Interaction of HIF1α and β-catenin inhibits matrix metalloproteinase 13 expression and prevents cartilage damage in mice
by Wafa Bouaziz and Johanna Sigaux and Dominique Modrowski and Claire-Sophie Devignes and Thomas Funck-Brentano and Pascal Richette and Hang-Korng Ea and Sylvain Provot and Martine Cohen-Solal and Eric Haÿ
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 5/2016, Volume 113, Issue 19, pp. 5453 - 5458
Low oxygen tension (hypoxia) regulates chondrocyte differentiation and metabolism. Hypoxia-inducible factor 1α (HIF1α) is a crucial hypoxic factor for... 
Matrix metalloprotease 13 | Hypoxia-inducible factor 1α | Chondrocyte | Osteoarthritis|Wnt signaling | PATHWAYS | STEM-CELLS | osteoarthritis | MULTIDISCIPLINARY SCIENCES | matrix metalloprotease 13 | HYPOXIA | Wnt signaling | chondrocyte | WNT/BETA-CATENIN | DISEASE | ARTICULAR CHONDROCYTES | DIFFERENTIATION | TRANSCRIPTIONAL REGULATION | PROMOTES | hypoxia-inducible factor 1 alpha | Signal Transduction | Mice, Inbred C57BL | Osteoarthritis - metabolism | Male | beta Catenin - metabolism | Matrix Metalloproteinase 13 - metabolism | Cartilage, Articular - pathology | Animals | Cartilage, Articular - metabolism | Hypoxia-Inducible Factor 1, alpha Subunit - metabolism | Protein Binding | Mice | Osteoarthritis - pathology | Index Medicus | Life Sciences | Human health and pathology | Rhumatology and musculoskeletal system | Cellular Biology | hypoxia-inducible factor 1α | Biological Sciences
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7. Full Text Metalloproteinases and Their Inhibitors in Patients with Inguinal Hernia
by Isik, Arda and Gursul, Cebrail and Peker, Kemal and Aydın, Merve and Fırat, Deniz and Yılmaz, İsmayil
World Journal of Surgery, ISSN 0364-2313, 05/2017, Volume 41, Issue 5, pp. 1259 - 1266
Aim The aim of this prospective study is to investigate if there is a relationship between inguinal hernia, matrix metalloproteinases (MMPs), and tissue... 
PATHOGENESIS | SURGERY | MATRIX METALLOPROTEINASES | REPAIR | COLLAGEN | DOXYCYCLINE | TRANSVERSALIS | ANEURYSM | OUTCOMES | EXPRESSION | INCISIONAL HERNIAS | Prospective Studies | Humans | Middle Aged | Male | Case-Control Studies | Tissue Inhibitor of Metalloproteinase-1 - metabolism | Tissue Inhibitor of Metalloproteinase-2 - metabolism | Matrix Metalloproteinase 9 - metabolism | Hydroxyproline - blood | Tissue Inhibitor of Metalloproteinase-3 - blood | Tissue Inhibitor of Metalloproteinase-3 - metabolism | Adult | Female | Tissue Inhibitor of Metalloproteinase-2 - blood | Matrix Metalloproteinases - blood | Matrix Metalloproteinase 9 - blood | Tissue Inhibitor of Metalloproteinase-1 - blood | Hernia, Inguinal - blood | Matrix Metalloproteinase 2 - metabolism | Hydroxyproline - metabolism | Tissue Inhibitor of Metalloproteinases - metabolism | Matrix Metalloproteinase 13 - metabolism | Hernia, Inguinal - metabolism | Matrix Metalloproteinase 2 - blood | Matrix Metalloproteinase 1 - blood | Matrix Metalloproteinase 13 - blood | Matrix Metalloproteinases - metabolism | Matrix Metalloproteinase 1 - metabolism | Tissue Inhibitor of Metalloproteinases - blood | Medicine, Experimental | Medical research | Medical colleges | Inguinal hernia | Index Medicus
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8. Full Text In Vivo Imaging of Matrix Metalloproteinase 12 and Matrix Metalloproteinase 13 Activities in the Mouse Model of Collagen‐Induced Arthritis
by Lim, Ngee Han and Meinjohanns, Ernst and Bou‐Gharios, George and Gompels, Luke L and Nuti, Elisa and Rossello, Armando and Devel, Laurent and Dive, Vincent and Meldal, Morten and Nagase, Hideaki
Arthritis & Rheumatology, ISSN 2326-5191, 03/2014, Volume 66, Issue 3, pp. 589 - 598
Objective. To develop enzyme-activatable Forster resonance energy transfer (FRET) substrate probes to detect matrix metalloproteinase 12 (MMP-12) and MMP-13... 
RHEUMATOID-ARTHRITIS | ACTIVATION | MACROPHAGE | MICE | OSTEOARTHRITIS | INHIBITORS | RHEUMATOLOGY | PROTEASE ACTIVITY | EXPRESSION | ACTIVITY-BASED PROBES | CARTILAGE | Diagnostic Imaging | Matrix Metalloproteinase Inhibitors - pharmacology | Animals | Synovial Membrane - enzymology | Fluorescence Resonance Energy Transfer | Mice | Synovial Membrane - drug effects | Arthritis, Experimental - enzymology | Matrix Metalloproteinase 12 - metabolism | Matrix Metalloproteinase 13 - metabolism | Index Medicus | Abridged Index Medicus
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9. Full Text Matrix metalloproteinase (MMP)-13 regulates mammary tumor-induced osteolysis by activating MMP9 and transforming growth factor-β signaling at the tumor-bone interface
by Nannuru, Kalyan C and Futakuchi, Mitsuru and Varney, Michelle L and Vincent, Thomas M and Marcusson, Eric G and Singh, Rakesh K
Cancer Research, ISSN 0008-5472, 05/2010, Volume 70, Issue 9, pp. 3494 - 3504
The tropism of breast cancer cells for bone and their tendency to induce an osteolytic phenotype are a result of interactions between breast cancer cells and... 
LYSYL OXIDASE | LUNG-CANCER | TGF-BETA | COLLAGENASE-3 MMP-13 | METASTASIS | HORMONE-RELATED PROTEIN | ONCOLOGY | GENE-EXPRESSION | MATRIX-METALLOPROTEINASE-9 | HUMAN BREAST-CANCER | SQUAMOUS-CELL CARCINOMAS | Bone and Bones - pathology | Up-Regulation | Adenocarcinoma - pathology | Osteoprotegerin - biosynthesis | Bone Neoplasms - secondary | Gene Expression Profiling | Mammary Neoplasms, Experimental - metabolism | Matrix Metalloproteinase 13 - biosynthesis | Bone Neoplasms - metabolism | RNA, Messenger - biosynthesis | Matrix Metalloproteinase 9 - metabolism | Matrix Metalloproteinase 9 - genetics | Bone and Bones - metabolism | Mammary Neoplasms, Experimental - pathology | Female | Mammary Neoplasms, Experimental - enzymology | Osteolysis - pathology | Matrix Metalloproteinase 9 - biosynthesis | Osteoclasts - pathology | Bone Neoplasms - enzymology | Signal Transduction | Osteolysis - genetics | Matrix Metalloproteinase 13 - genetics | RNA, Messenger - genetics | Adenocarcinoma - enzymology | Bone and Bones - enzymology | RANK Ligand - biosynthesis | Osteolysis - metabolism | Matrix Metalloproteinase 13 - metabolism | Animals | Osteolysis - enzymology | Cell Line, Tumor | Matrix Metalloproteinase Inhibitors | Mice | Mice, Inbred BALB C | Osteoclasts - enzymology | Enzyme Activation | Transforming Growth Factor beta - metabolism | Index Medicus
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10. Full Text Pivotal role of matrix metalloproteinase 13 in extracellular matrix turnover in idiopathic pulmonary fibrosis
by Nkyimbeng, Takwi and Ruppert, Clemens and Shiomi, Takayuki and Dahal, Bhola and Lang, György and Seeger, Werner and Okada, Yasunori and D'Armiento, Jeanine and Günther, Andreas
PloS one, ISSN 1932-6203, 2013, Volume 8, Issue 9, pp. e73279 - e73279
Rationale: Idiopathic pulmonary fibrosis (IPF) is a fatal disease characterized by excessive deposition of extracellular matrix (ECM). Objectives: We... 
LUNG FIBROSIS | COLLAGEN | MULTIDISCIPLINARY SCIENCES | TISSUE | EMPHYSEMA | DISEASE | INTERSTITIAL PNEUMONIA | MMP-13 | MICE | INHIBITORS | EXPRESSION | Humans | Middle Aged | Extracellular Matrix - metabolism | Idiopathic Pulmonary Fibrosis - chemically induced | Case-Control Studies | Idiopathic Pulmonary Fibrosis - metabolism | Lung - enzymology | Matrix Metalloproteinase 13 - deficiency | Proteolysis - drug effects | Adult | Matrix Metalloproteinase 1 - genetics | Lung - pathology | Extracellular Matrix - drug effects | Hydroxyproline - metabolism | Matrix Metalloproteinase 13 - genetics | Tissue Inhibitor of Metalloproteinases - metabolism | Matrix Metalloproteinase 13 - metabolism | Up-Regulation - drug effects | Collagen - metabolism | Animals | Lung - drug effects | Idiopathic Pulmonary Fibrosis - pathology | Bleomycin - pharmacology | Idiopathic Pulmonary Fibrosis - enzymology | Mice | Tissue Donors | Matrix Metalloproteinase 1 - metabolism | Pulmonary fibrosis | Proteases | Physiological aspects | Development and progression | Extracellular matrix | Genetic aspects | Research | Tissue inhibitor of metalloproteinases | Thoracic surgery | Pneumonia | Matrix metalloproteinases | Honeycomb construction | Pathogenesis | Lung | Inflammatory response | Matrix metalloproteinase | Bleomycin | Rodents | Metalloproteinase | Deposition | Lung diseases | Inflammation | Nitrogen | Gene expression | Collagenase 3 | Medicine | Hospitals | Lungs | Cysts | Collagen | Fibrosis | Neutrophil collagenase | Surgeons | Index Medicus
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11. Full Text Activation of Matrix Metalloproteinases 2, 9, and 13 by Activated Protein C in Human Osteoarthritic Cartilage Chondrocytes
by Jackson, Miriam T and Moradi, Babak and Smith, Margaret M and Jackson, Christopher J and Little, Christopher B
Arthritis & Rheumatology, ISSN 2326-5191, 06/2014, Volume 66, Issue 6, pp. 1525 - 1536
Objective. Levels of activated protein C (APC) are elevated in the synovial fluid of patients with osteoarthritis (OA), and increased APC levels are correlated... 
RHEUMATOID-ARTHRITIS | INTERGLOBULAR DOMAIN | TUMOR-NECROSIS-FACTOR | ARTICULAR-CARTILAGE | PATHWAY | INTERLEUKIN-1-BETA | ENDOTHELIAL-CELLS | GENE-EXPRESSION | DEGRADATION | I COLLAGEN | RHEUMATOLOGY | Humans | Synovial Fluid - metabolism | Male | Protein C - pharmacology | Chondrocytes - drug effects | Tissue Inhibitor of Metalloproteinase-1 - metabolism | Matrix Metalloproteinase 9 - metabolism | Cartilage, Articular - metabolism | Tissue Inhibitor of Metalloproteinase-3 - metabolism | Aged, 80 and over | Female | Chondrocytes - metabolism | Serine Proteases - metabolism | Chondrocytes - pathology | Matrix Metalloproteinase 2 - metabolism | Cells, Cultured | Aggrecans - metabolism | Disease Progression | Matrix Metalloproteinase 13 - metabolism | Cartilage, Articular - pathology | Collagen - metabolism | Osteoarthritis, Knee - pathology | Aged | Cartilage, Articular - drug effects | Osteoarthritis, Knee - metabolism | Proteins | Gene expression | Proteases | Rodents | Index Medicus | Abridged Index Medicus
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12. Full Text Targeted Polypharmacology: Discovery of a Highly Potent Non-Hydroxamate Dual Matrix Metalloproteinase (MMP)-10/-13 Inhibitor
by Senn, Nicole and Ott, Michael and Lanz, Jan and Riedl, Rainer
Journal of Medicinal Chemistry, ISSN 0022-2623, 12/2017, Volume 60, Issue 23, pp. 9585 - 9598
Matrix metalloproteinases (MMPs) play a key role in many diseases like cancer, atherosclerosis or arthritis. Interest in MMP inhibition has been revitalized... 
ACTIVATION | CHEMISTRY, MEDICINAL | PHARMACOLOGY | MATRIX-METALLOPROTEINASE-10 | MMP-10 | SELECTIVITY | HOPE | PROCOLLAGENASE | STRUCTURE-BASED DESIGN | Matrix Metalloproteinase Inhibitors - pharmacology | Humans | Drug Design | Models, Molecular | Matrix Metalloproteinase 10 - metabolism | Matrix Metalloproteinase Inhibitors - chemistry | Structure-Activity Relationship | Polypharmacology | Matrix Metalloproteinase 13 - metabolism | Index Medicus
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13. Full Text Relaxin signals through a RXFP1-pERK-nNOS-NO-cGMP-dependent pathway to up-regulate matrix metalloproteinases: The additional involvement of iNOS
by Chow, Bryna Suet Man and Chew, Elaine Guo Yan and Zhao, Chongxin and Bathgate, Ross A. D and Hewitson, Tim D and Samuel, Chrishan S
PLoS ONE, ISSN 1932-6203, 08/2012, Volume 7, Issue 8, pp. e42714 - e42714
The hormone, relaxin, inhibits aberrant myofibroblast differentiation and collagen deposition by disrupting the TGF-beta 1/Smad2 axis, via its cognate... 
RENAL FIBROSIS | LUNG FIBROSIS | COLLAGEN | MULTIDISCIPLINARY SCIENCES | GROWTH | INTERSTITIAL FIBROSIS | TISSUE INHIBITORS | SMOOTH-MUSCLE-CELLS | NITRIC-OXIDE PATHWAY | HORMONE RELAXIN | FIBROBLASTS | Relaxin - metabolism | Matrix Metalloproteinases - genetics | Receptors, G-Protein-Coupled - metabolism | Humans | Male | Receptors, Peptide - genetics | Matrix Metalloproteinase 9 - metabolism | Relaxin - genetics | Matrix Metalloproteinase 9 - genetics | Fibroblasts - metabolism | Cell Line | Matrix Metalloproteinase 2 - metabolism | Matrix Metalloproteinase 13 - genetics | Cells, Cultured | Rats | Kidney - cytology | Signal Transduction - genetics | Extracellular Signal-Regulated MAP Kinases | Rats, Sprague-Dawley | Matrix Metalloproteinase 13 - metabolism | Mice, Knockout | Matrix Metalloproteinase 2 - genetics | Animals | Cyclic GMP - metabolism | Nitric Oxide Synthase Type I - metabolism | Signal Transduction - physiology | Fibroblasts - cytology | Mice | Nitric Oxide Synthase Type I - genetics | Receptors, G-Protein-Coupled - genetics | Matrix Metalloproteinases - metabolism | Nitric Oxide - metabolism | Receptors, Peptide - metabolism | Physiological aspects | Genetic aspects | Research | Transforming growth factors | Metalloenzymes | Nitric oxide | Neurosciences | Phosphorylation | Matrix metalloproteinases | Guanosine | Smooth muscle | Genomes | Arthritis | Biochemistry | Matrix metalloproteinase | Guanylate cyclase | Western blotting | Signal transduction | Arginine | Gelatin | Rodents | Cyclic GMP | Fibroblasts | Metalloproteinase | Interstitial collagenase | Kidneys | Extracellular signal-regulated kinase | Collagenase 3 | Nitric-oxide synthase | Gelatinase B | NG-Nitroarginine methyl ester | Gelatinase A | Signaling | Inhibitors | Human performance | Collagen | Isoforms | Fibrosis | Skin | Aberration | Molecular biology | Ornithine | Index Medicus
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14. Full Text Identification of a central role for complement in osteoarthritis
by Wang, Qian and Rozelle, Andrew L and Lepus, Christin M and Scanzello, Carla R and Song, Jason J and Larsen, D. Meegan and Crish, James F and Bebek, Gurkan and Ritter, Susan Y and Lindstrom, Tamsin M and Hwang, Inyong and Wong, Heidi H and Punzi, Leonardo and Encarnacion, Angelo and Shamloo, Mehrdad and Goodman, Stuart B and Wyss-Coray, Tony and Goldring, Steven R and Banda, Nirmal K and Thurman, Joshua M and Gobezie, Reuben and Crow, Mary K and Holers, V. Michael and Lee, David M and Robinson, William H
Nature Medicine, ISSN 1078-8956, 12/2011, Volume 17, Issue 12, pp. 1674 - 1679
Osteoarthritis, characterized by the breakdown of articular cartilage in synovial joints, has long been viewed as the result of 'wear and tear'(1). Although... 
RHEUMATOID-ARTHRITIS | MEDICINE, RESEARCH & EXPERIMENTAL | ACTIVATION | SYNOVIAL-FLUID | BIOCHEMISTRY & MOLECULAR BIOLOGY | OLIGOMERIC MATRIX PROTEIN | INDUCTION | CARTILAGE DEGRADATION | CELL BIOLOGY | IN-VIVO | GENERATION | KNEE OSTEOARTHRITIS | EXPRESSION | Complement C5 - genetics | Cartilage - pathology | Complement Membrane Attack Complex - metabolism | Humans | Synovial Fluid - metabolism | Gene Expression Profiling | Extracellular Signal-Regulated MAP Kinases - metabolism | Extracellular Signal-Regulated MAP Kinases - genetics | Complement C6 - genetics | Osteoarthritis - pathology | Proteomics - methods | Chondrocytes - metabolism