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TIMP-1 and TIMP-2 Levels in Vitreous and Subretinal Fluid

Japanese Journal of Ophthalmology, 1998
To 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 ...
Toshihiko Matsuo   +2 more
exaly   +3 more sources

A TIMP-1 splice variant transcript: Possible role in regulation of TIMP-1 expression

open access: yesCancer Letters, 2008
A splice variant of tissue inhibitor of metalloproteinases-1 (TIMP-1) mRNA lacking exon 2 (TIMP-1-v2) has been identified in human cancer cells and in colorectal and breast cancer tumors.
Karin Birkenkamp-Demtröder
exaly   +2 more sources

Engineering of Selective TIMPs

Annals of the New York Academy of Sciences, 1999
ABSTRACT: Differences in proteinase susceptibility between free TIMP‐1 and the TIMP‐1‐MMP‐3 complex and mutagenesis studies suggested that the residues around the disulfide bond between Cys1 and Cys70 in TIMP‐1 may interact with MMPs. The crystal structure of the complex between TIMP‐1 and the catalytic domain of MMP‐3 has revealed that the α‐amino ...
H, Nagase   +7 more
openaire   +2 more sources

TIMPs as multifacial proteins

Critical Reviews in Oncology/Hematology, 2004
Tissue inhibitors of metalloproteinases (TIMPs) are natural inhibitors of matrix metalloproteinases (MMPs) found in most tissues and body fluids. By inhibiting MMPs activities, they participate in tissue remodeling of the extracellular matrix (ECM). The balance between MMPs and TIMPs activities is involved in both normal and pathological events such as
Elise, Lambert   +3 more
openaire   +2 more sources

Tissue inhibitors of metalloproteinases-1 (TIMP-1) and -2(TIMP-2) are major serum factors that stimulate the TIMP-1 gene in human gingival fibroblasts [PDF]

open access: yesBiochimica Et Biophysica Acta - Molecular Cell Research, 2006
We demonstrate in this study that both TIMP-1 and TIMP-2 are major serum factors that stimulate the induction of TIMP-1 mRNA in quiescent human gingival fibroblasts (Gin-1 cells) at mid-G1 (6–9 h after serum stimulation) of the cell cycle, but not that ...
Taro Hayakawa, Kyoko Yamashita
exaly   +2 more sources

Clinicopathological correlations of TIMP‐1 and TIMP‐2 in Hodgkin's lymphoma

European Journal of Haematology, 2003
Abstract:Objectives:  The influence of matrix–tumour interactions in Hodgkin's lymphoma is poorly characterised, although a large part of the tumour often consists of reactive tissue. The aim of the present study was to assess the clinicopathological role of two main inhibitors of matrix metalloproteinases, TIMP‐1 and TIMP‐2, in Hodgkin's lymphoma ...
Heli, Pennanen   +3 more
openaire   +2 more sources

Inhibition of stimulated bone resorption in vitro by TIMP-1 and TIMP-2

Biochimica Et Biophysica Acta - Molecular Cell Research, 1993
Recombinant 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.
John J Reynolds, P A Hill, J J Reynolds
exaly   +3 more sources

Localization of TIMP-1, TIMP-2, TIMP-3, gelatinase A and gelatinase B in pathological human corneas

Current Eye Research, 1998
Determine 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
openaire   +2 more sources

Insights into MMP‐TIMP Interactions

Annals of the New York Academy of Sciences, 1999
ABSTRACT: 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
openaire   +3 more sources

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