Results 201 to 210 of about 16,067 (252)
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TIMP-1 and TIMP-2 Levels in Vitreous and Subretinal Fluid
Japanese Journal of Ophthalmology, 1998To understand the role of tissue inhibitors of metalloproteinase-1 and -2 (TIMP-1 and TIMP-2) in intraocular diseases, levels of TIMP-1 and TIMP-2 were measured by enzyme immunoassay in 47 patients with various ocular diseases: in subretinal fluid of 7 patients with rhegmatogenous retinal detachment and in vitreous of 12 patients with proliferative ...
T, Matsuo +3 more
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Localization of TIMP-1, TIMP-2, TIMP-3, gelatinase A and gelatinase B in pathological human corneas
Current Eye Research, 1998Determine the tissue distribution patterns for tissue inhibitors of metalloproteinases (TIMP-1, TIMP-2, TIMP-3), gelatinase A and gelatinase B in normal and pathologic corneas.Corneas were examined by immunohistochemistry, using antibodies to TIMP-1, TIMP-2, TIMP-3, gelatinase A or gelatinase B.In normal corneas, TIMP-1 antibody stained the epithelium ...
M C, Kenney +5 more
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Insights into MMP‐TIMP Interactions
Annals of the New York Academy of Sciences, 1999ABSTRACT: The proteolytic activity of the matrix metalloproteinases (MMPs) involved in extracellular matrix degradation must be precisely regulated by their endogenous protein inhibitors, the tissue inhibitors of metalloproteinases (TIMPs). Disruption of this balance can result in serious diseases such as arthritis and tumor growth and metastasis ...
Bode, W +6 more
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MMPs and TIMPs-An Historical Perspective
Molecular Biotechnology, 2002There are currently 25 known vertebrate matrix metalloproteinases (MMPs) and 4 tissue inhibitors of metalloproteinases (TIMPs). This article reviews these proteases from an historical perspective in terms of who discovered each protein, when the sequence was established, when action on protein substrates was demonstrated, and what names have been used.
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Immunohistochemistry of MMPs and TIMPs
2003Immunohistochemistry is a useful and powerful method to determine the cells responsible for the production of MMPs and TIMPs and localize them to the tissue areas where they are functioning. This chapter describes the detailed methods of the immunohistochemistry applied to human pathological tissues using commercially available monoclonal antibodies ...
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Inhibition of stimulated bone resorption in vitro by TIMP-1 and TIMP-2
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 1993Recombinant human TIMP-1 and TIMP-2 (tissue inhibitors of metalloproteinases) inhibited bone resorption induced by either parathyroid hormone or 1,25-dihydroxyvitamin D3 in cultured neonatal mouse calvariae. The inhibition was reversible, dose-dependent and complete at 1 microgram/ml inhibitor concentration. TIMP-2 was more potent than TIMP-1.
P A, Hill, J J, Reynolds, M C, Meikle
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Equine TIMP‐1 and TIMP‐2: Identification, activity and cellular sources
Equine Veterinary Journal, 1998Summary Matrix metalloproteinases (MMPs) are the main enzymes involved in connective tissue turnover. Regulation of MMPs is achieved by controlling production, activation of the proenzymes together with the presence of inhibitors, such as, tissue inhibitors of metalloproteinases (TIMPS).
P D, Clegg, A R, Coughlan, S D, Carter
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2000
Abstract It is generally believed by those in the field that inhibition of proteolytic activity is the major function of the TIMPs. The growth effects are not widely recognized and have not received nearly the attention given to enzyme inhibition. The first point to be considered is whether all TlMPs inhibit all MMPs, and whether this is
J Frederick Woessner, Hideaki Nagase
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Abstract It is generally believed by those in the field that inhibition of proteolytic activity is the major function of the TIMPs. The growth effects are not widely recognized and have not received nearly the attention given to enzyme inhibition. The first point to be considered is whether all TlMPs inhibit all MMPs, and whether this is
J Frederick Woessner, Hideaki Nagase
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2000
Abstract Twenty-five amino acid alignments are presented at the end of the book. These are linked to a more complete description of each sequence presented in Table 4. For each item in Table 4 there is a number relating to the line number in the alignment.
J Frederick Woessner, Hideaki Nagase
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Abstract Twenty-five amino acid alignments are presented at the end of the book. These are linked to a more complete description of each sequence presented in Table 4. For each item in Table 4 there is a number relating to the line number in the alignment.
J Frederick Woessner, Hideaki Nagase
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