| R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions. The TNF Family Molecules LIGHT and Lymphotoxin alphabeta Induce a Distinct Steroid-Resistant Inflammatory Phenotype in Human Lung Epithelial Cells.
Authors: da Silva Antunes R, Madge L, Soroosh P, Tocker J, Croft M
J Immunol, 2015;195(5):2429-41.
Species: Human
Sample Type: Cell Culture Supernates
Regulation of MMP-9 by a WIN-binding site in the monocyte-macrophage system independent from cannabinoid receptors.
Authors: Tauber, Svantje, Paulsen, Katrin, Wolf, Susanne, Synwoldt, Peggy, Pahl, Andreas, Schneider-Stock, Regine, Ullrich, Oliver
PLoS ONE, 2012;7(11):e48272.
Species: Human
Sample Type: Cell Culture Supernates
Host gene-encoded severe lung TB: from genes to the potential pathways.
Authors: Ganachari, M, Guio, H, Zhao, N, Flores-Villanueva, P O
Genes Immun, 2012;13(8):605-20.
Species: Human
Sample Type: Serum
Early Elevation of Matrix Metalloproteinase-8 and -9 in Pediatric ARDS Is Associated with an Increased Risk of Prolonged Mechanical Ventilation.
Authors: Kong MY, Li Y, Oster R, Gaggar A, Clancy JP
PLoS ONE, 2011;6(8):e22596.
Species: Human
Sample Type: Tracheal Aspirates
Primary human acute myelogenous leukemia cells release matrix metalloproteases and their inhibitors: release profile and pharmacological modulation.
Authors: Reikvam H, Hatfield KJ, Oyan AM, Kalland KH, Kittang AO, Bruserud O
Eur. J. Haematol., 2010;84(3):239-51.
Species: Human
Sample Type: Cell Culture Supernates
Salbutamol up-regulates matrix metalloproteinase-9 in the alveolar space in the acute respiratory distress syndrome.
Authors: OKane CM, McKeown SW, Perkins GD, Bassford CR, Gao F, Thickett DR, McAuley DF
Crit. Care Med., 2009;37(7):2242-9.
Species: Human
Sample Type: BALF
Serum matrix metalloproteinases in adult CF patients: Relation to pulmonary exacerbation.
Authors: Roderfeld M, Rath T, Schulz R, Seeger W, Tschuschner A, Graf J, Roeb E
J. Cyst. Fibros., 2009;8(5):338-47.
Species: Human
Sample Type: Serum
The presence of a matrix-derived neutrophil chemoattractant in bronchiolitis obliterans syndrome after lung transplantation.
Authors: Hardison MT, Galin FS, Calderon CE, Djekic UV, Parker SB, Wille KM, Jackson PL, Oster RA, Young KR, Blalock JE, Gaggar A
J. Immunol., 2009;182(7):4423-31.
Species: Human
Sample Type: BALF
Matrix metalloproteinase activity in pediatric acute lung injury.
Authors: Kong MY, Gaggar A, Li Y
Int J Med Sci, 2009;6(1):9-17.
Differential proteolytic enzyme activity in eosinophilic and neutrophilic asthma.
Authors: Simpson JL, Scott RJ, Boyle MJ, Gibson PG
Am. J. Respir. Crit. Care Med., 2005;172(5):559-65.
Species: Human
Sample Type: Sputum
Comparative effects of AT1-antagonism and angiotensin-converting enzyme inhibition on markers of inflammation and platelet aggregation in patients with coronary artery disease.
Authors: Schieffer B, Bunte C, Witte J, Hoeper K, Boger RH, Schwedhelm E, Drexler H
J. Am. Coll. Cardiol., 2004;44(2):362-8.
Species: Human
Sample Type: Serum
Implications for matrix metalloproteinases as modulators of pediatric lung disease.
Authors: Winkler MK, Foldes JK, Bunn RC, Fowlkes JL
Am. J. Physiol. Lung Cell Mol. Physiol., 2003;284(4):L557-65.
Species: Human
Sample Type: Saliva
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| 背景 | The matrix metalloproteinases (MMPs) consist of 24 known human zinc proteases with essential roles in breaking down components of the extracellular matrix (ECM). Additional MMP substrates include cytokines, chemokines, growth factors and binding proteins, cell/cell adhesion molecules, and other proteinases. With a few exceptions, MMPs share common structural motifs including a pro-peptide domain, a catalytic domain, a hinge region, and a hemopexin-like domain. Synthesized as pro-enzymes, most MMPs are secreted before conversion to their active form. MMP activities are modulated on several levels including transcription, pro-enzyme activation, or by their endogenous inhibitors, tissue inhibitors of metalloproteinases (TIMPs). A subset of MMPs are associated with membranes and designated as membrane-type metalloproteinases (MT-MMP). |
