Results 21 to 30 of about 100,799 (312)

The possibilities of using the inhibitors of matrix metalloproteinases for keratoplasty

Трансплантология (Москва), 2023
Introduction. The review is devoted to the actual problem of treating patients with keratolysis. The role of matrix metalloproteinases in the pathogenesis of cornea and corneal graft melting is discussed as well as the practical experience of using ...
K. V. Sirotkina, E. V. Chentsova
doaj   +1 more source

Inhibitory antibodies designed for matrix metalloproteinase modulation [PDF]

, 2019
The family of matrix metalloproteinases (MMPs) consists of a set of biological targets that are involved in a multitude of severe pathogenic events such as different forms of cancers or arthritis.
Fischer, Thomas, Riedl, Rainer
core   +1 more source

Activity of matrix metalloproteinases and their tissue inhibitors in serum in chronic granulating periodontitis

Patologìâ, 2019
Aim. The aim of the work is to study the activity of matrix metalloproteinases and their tissue inhibitors in chronic granular periodontitis. Materials and methods. We examined serum of 15 patients with chronic granulating periodontitis and 15 healthy
D. I. Haidash, I. S. Haidash, O. О. Bondar, Yu. О. Yevtushenko, O. I. Haidash   +4 more
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Role of matrix metalloproteinases in diabetic foot ulcers: Potential therapeutic targets

Frontiers in Pharmacology, 2022
Diabetic foot ulcers (DFUs) are pathological states of tissue destruction of the foot or lower extremity in diabetic patients and are one of the serious chronic complications of diabetes mellitus.
Kang Fu, Xueyao Zheng, Yuhan Chen, Yuhan Chen, Liuying Wu, Liuying Wu, Zhiming Yang, Zhiming Yang, Xu Chen, Xu Chen, Wei Song, Wei Song   +11 more
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Implications of MMP9 for Blood Brain Barrier Disruption and Hemorrhagic Transformation Following Ischemic Stroke. [PDF]

, 2016
Numerous studies have documented increases in matrix metalloproteinases (MMPs), specifically MMP-9 levels following stroke, with such perturbations associated with disruption of the blood brain barrier (BBB), increased risk of hemorrhagic complications ...
Adibhatla, Agrawal, Alcaide, Amantea, Amantea, Anthony, Asahi, Asahi, Asahi, Bajor, Bakowski, Bauer, Benarroch, Burk, Candelario-Jalil, Carbone, Castellanos, Castellanos, Chang, Chesler, Choi, Clark, Clark, Conant, Copin, Cuadrado, Cuadrado, Cunningham, Dejonckheere, Fanjul-Fernández, Fernandez-Patron, Ferry, Fiorelli, Frank R. Sharp, Fujimoto, Fujimura, Fujimura, Gasche, Gasche, Gasche, Gautier, Gidday, Golab, Gu, Gurney, Gürsoy-Ozdemir, Hacke, Harris, Heo, Heo, Horstmann, Hu, Inzitari, Jickling, Justicia, Keck, Kelly, Khandoga, Kim, Kuroiwa, Kurzepa, Lapchak, Lee, Lenglet, Lenglet, Li, Lucivero, Lukes, Lynch, Machado, Maier, Manabe, McCarthy, Moldes, Montaner, Montaner, Montaner, Montaner, Montaner, Montaner, Mun-Bryce, Murata, Nguyen, Ning, Oda, Opdenakker, Orbe, Piccardi, Planas, Ra, Ramos-Fernandez, Ranasinghe, Renée J. Turner, Reynolds, Rivera, Rodrigues, Rodríguez, Rodríguez-Yáñez, Romanic, Rosell, Rosell, Rosell, Rosenberg, Rosenberg, Rosenberg, Rosenberg, Sandoval, Schnoor, Shigemori, Si-Tayeb, Sotgiu, Steadman, Sternlicht, Sumii, Svedin, Tan, Tang, Tsuji, Tsuruoka, Turba, Van den Steen, Vandooren, Vukasovic, Wang, Wang, Wang, Yan, Yang, Yang, Yushchenko, Zhao, Zhao, Zhao, Zozulya   +133 more
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Expression profiling of metalloproteinases and tissue inhibitors of metalloproteinases in normal and degenerate human achilles tendon [PDF]

, 2006
To profile the messenger RNA (mRNA) expression for the 23 known genes of matrix metalloproteinases (MMPs), 19 genes of ADAMTS, 4 genes of tissue inhibitors of metalloproteinases (TIMPs), and ADAM genes 8, 10, 12, and 17 in normal, painful, and ruptured ...
Alfredson, Alfredson, Amour, Amour, Anthony N. Corps, Archambault, Arnoczky, Asakura, Astrom, Baker, BenEzra, Bjur, Black, Brew, Brian L. Hazleman, Caroline J. Pennington, Cawston, Clancy, Conover, Dickinson, Drummond, Dylan R. Edwards, Fenwick, Gavin C. Jones, Graham P. Riley, Hannafin, Hashimoto, Hieta, Ian M. Clark, Iba, Iba, Ireland, Jarvinen, Jones, Jozsa, Kannus, Kashiwagi, Kashiwagi, Killar, Kurisaki, Lavagnino, Lo, Loechel, Ma, Majima, Malfait, Michelle M. Bradley, Movin, Mueller, Muller, Nakamura, Nuttall, Pei, Pendas, Porter, Primakoff, Rees, Riley, Riley, Riley, Roy, Sandy, Sandy, Sedlacek, Somerville, Sternlicht, Thodeti, Tipton, Tsuzaki, Van Meurs, Van Meurs, Velasco, Yasuda, Yu   +73 more
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The Effect of Doxycycline on Glomerulosclerosis in 5/6 Renal Ablation Nephropathy

Ankara Üniversitesi Tıp Fakültesi Mecmuası, 2020
Objectives:The beneficial effect of matrix metalloproteinases (MMP) inhibitors in renal diseases has been reported. Their effect in segmental sclerosis is unknown.
Devrim Kahraman, Ali Çelik, Funda Sağlam, Osman Yılmaz, Efsun Kolatan, Zahide Çavdar, Sulen Sarıoğlu   +6 more
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Matrix Metalloproteinase/Tissue Inhibitors of Matrix Metalloproteinase Phenotype Identifies Poor Prognosis Colorectal Cancers [PDF]

Clinical Cancer Research, 2004
Abstract Purpose: The matrix metalloproteinases (MMPs) are a family of proteolytic enzymes involved in tumor invasion; several individual members of which have been implicated in tumor prognosis. These enzymes and their physiologic inhibitors, the tissue inhibitors of matrix metalloproteinases (TIMPs), act in a coordinated manner to form
Stephanie, Curran, Sinclair R, Dundas, Jenny, Buxton, Matthew F, Leeman, Robin, Ramsay, Graeme I, Murray   +5 more
openaire   +2 more sources

The relationship between the first episode of wheezing and matrix metalloproteinases-9 and MMP-2 and tissue inhibitors of MMP-1 levels in preterm infants

Annals of Thoracic Medicine, 2013
Aims: Matrix metalloproteinases (MMP) have been associated with neonatal lung morbidity and MMP dysregulation contributes to the pathology of chronic and acute lung disorders.
Rabia Gonul Sezer, Gokhan Aydemir, Abdulkadir Bozaykut, Serdar Hira, Ilhan Asya Tanju, Ömer Özcan   +5 more
doaj   +1 more source

Matrix metalloproteinases at key junctions in the pathomechanism of stroke [PDF]

, 2011
Matrix metalloproteinases play a crucial role in the remodelling of the extracellular matrix through direct degradation of its structural proteins and control of extracellular signaling.
Amento, Ang, Asahi, Asahi, Barkho, Bergers, Bini, Cao, Cardone, Chinopoulos, Cunningham, Denker, Dong, Fabunmi, Fisher, Frisch, Galis, Galis, Galis, Galis, Gidday, Godin, Gross, Gu, Gu, Gurney, Haas, Haddad, Halliwell, Hamann, Harkness, Herman, Hornig, Hyslop, Itoh, Kumura, Langton, Lapchak, Larsen, Lee, Lelongt, Loftus, Lucivero, Luttun, McQuibban, Meredith, Montaner, Montaner, Nagase, Nagel, Nagy, Nagy, Nikkari, Pagenstecher, Qi, Rajagopalan, Ramos, Rekhter, Rolfe, Romanic, Rosell, Rosenberg, Rosenberg, Rosenberg, Rosenberg, Sarén, Sato, Seo, Shrivastava, Shubayev, Siao, Sole, Sottrup, Sternlicht, Strongin, Sukhova, Suzuki, Suzuki, Svedin, Tsuji, Turner, Van, Vogel, Wang, Wang, Webersinke, Yepes, Ying, Zhang, Zhang, Zhang, Zhao   +91 more
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