Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Ari Tuuttila"'
Publikováno v:
Journal of Biological Chemistry. 282:16654-16666
MARCO is a trimeric class A scavenger receptor of macrophages and dendritic cells that recognizes polyanionic particles and pathogens. The distal, scavenger receptor cysteine-rich (SRCR) domain of the extracellular part of this receptor has been impl
Autor:
Timo Pikkarainen, Ari Tuuttila, Karl Tryggvason, Marko Sankala, David E. Isenman, Juha R.M. Ojala, Yi Sun, Yunying Chen
Publikováno v:
Journal of Biological Chemistry. 281:12767-12775
MARCO is a class A scavenger receptor capable of binding both gram-negative and -positive bacteria. Using the surface plasmon resonance technique, we show here that a recombinant, soluble form of MARCO, sMARCO, binds the major gram-negative and -posi
Publikováno v:
Proceedings of the National Academy of Sciences. 99:7414-7419
Matrix metalloproteinases (MMPs) are a family of multidomain enzymes involved in the physiological degradation of connective tissue, as well as in pathological states such as tumor invasion and arthritis. Apart from transcriptional regulation, MMPs a
Autor:
Ulrich Bergmann, Ylva Lindqvist, Ari Tuuttila, Wolfram Bode, Karl Tryggvason, Carlos Fernandez-Catalan, Gunter Schneider, Ekaterina Morgunova, Klaus Maskos
Publikováno v:
Journal of Molecular Biology. 284:1133-1140
The three-dimensional structure of human tissue inhibitor of metalloproteinases-2 (TIMP-2) was determined by X-ray crystallography to 2.1 A resolution. The structure of the inhibitor consists of two domains. The N-terminal domain (residues 1-110) is
Publikováno v:
Archives of Biochemistry and Biophysics. 347:62-68
The binding of matrix metalloproteinases-2 and -9 to pregnancy zone protein and α 2 -macroglobulin was studied. The binding was demonstrated by formation of dimeric as well as tetrameric complexes of pregnancy zone protein and by the formation of α
Autor:
Tiina Hurskainen, Ari Tuuttila, Aarne Oikarinen, Helena Autio-Harmainen, Ylermi Soini, Matti Höyhtyä
Publikováno v:
Human Pathology. 27:42-49
The expression of tissue inhibitors of metalloproteinases (TIMP-1 and TIMP-2) was studied in eight malignant fibrous histiocytomas (MFH) and in eight dermatofibromas (DF) using in situ hybridization methods (ISH). Immunohistochemical stainings were a
Publikováno v:
Scopus-Elsevier
Human 72 kDa type IV collagenase (gelatinase A, MMP-2) was expressed in a baculovirus/insect cell system. The enzyme was produced in the wild-type form and in two mutant forms, where the active site Glu375 was substituted by Asp or Gln. The mutated p
Publikováno v:
Experimental Cell Research. 202:471-476
Regulation of the activity of proteolytic enzymes is of major importance in the turnover of connective tissues. The search for physiologically relevant activation mechanisms of principal tissue-degrading enzymes, e.g., metalloproteinases, has therefo
Publikováno v:
Journal of Biological Chemistry. 266:16485-16490
The complete structure of the human gene for 92-kDa type IV collagenase was determined. Two overlapping genomic clones spanning 26 kilobases (kb) of genomic DNA were shown to contain the entire 7.7-kb structural gene together with 15 and 3.5 kb of 5'
Publikováno v:
Cell Differentiation and Development. 32:307-312