نتایج جستجو برای: ایمنوهیستوشیمی cox2

تعداد نتایج: 1492  

Journal: :The Journal of biological chemistry 1994
K A Pritchard M K O'Banion J M Miano N Vlasic U G Bhatia D A Young M B Stemerman

Prostaglandins are synthesized from arachidonic acid by the rate-limiting enzyme cyclooxygenase (prostaglandin G/H synthase). Active cyclooxygenase is encoded by two distinct and independently regulated genes, termed cyclooxygenase-1 (cox1) and cyclooxygenase-2 (cox2). In this investigation, we examined the expression of cox1 and cox2 mRNA in rat aorta following balloon deendothelialization (BD...

2012
Maciej J. Czachorowski André F. S. Amaral Santiago Montes-Moreno Josep Lloreta Alfredo Carrato Adonina Tardón Manuel M. Morente Manolis Kogevinas Francisco X. Real Núria Malats

Aberrant overexpression of cyclooxygenase-2 (COX2) is observed in urothelial carcinoma of the bladder (UCB). Studies evaluating COX2 as a prognostic marker in UCB report contradictory results. We determined the prognostic potential of COX2 expression in UCB and quantitatively summarize the results with those of the literature through a meta-analysis. Newly diagnosed UCB patients recruited betwe...

ژورنال: :مجله علمی دانشگاه علوم پزشکی قزوین 0
محمدرضا جباری m. jabbari department of virology, faculty of medical sciences, tarbiat modares university, tehranگروه ویروس شناسی، دانشکده علوم پزشکی، دانشگاه تربیت مدرس، تهران فرزانه صباحی f. sabahi farzaneh sabahi, faculty of medicine, tarbiat modars university, tehran, iranتهران، دانشکده علوم پزشکی، دانشگاه تربیت مدرس، تلفن 82883836- 021 بهزاد خوانساری نژاد b. khansarinejad department of microbiology and immunology , arakگروه میکروب شناسی و ایمنی شناسی ، دانشگاه علوم پزشکی اراک ، اراک رضا شیرکوهی r. shirkoohi department of genetics, cancer research center, cancer institute of iran, tehran university of medical sciences, tehranگروه ژنتیک ، مرکز تحقیقات سرطان ، انستیتو کانسر ایران ،بیمارستان امام خمینی،دانشکده علوم پزشکی دانشگاه تهران، تهران هوشنگ صابری h. saberi محمود پروین m. parvin pathology department, labbafinejad hospital,shahid beheshti university of medical sciences,tehranگروه پاتولوژی، بیمارستان لبافی نژاد، دانشگاه علوم پزشکی شهید بهشتی، تهران

زمینه: سایتومگالوویروس­های انسانی ممکن است در ایجاد بیماری گلیوما که یکی از شایع­ترین تومورهای مغزی است، نقش داشته باشند.   هدف: مطالعه به منظور شناسایی سایتومگالوویروس­های انسانی در بیماران مبتلا به گلیوما در بیمارستان امام خمینی تهران انجام شد.   مواد و روش­ها: این مطالعه تجربی در سال 1391 بر روی نمونه­های پارافینه تومور مغزی گلیومای بیماران مراجعه­کننده به بخش جراحی اعصاب بیمارستان امام خمین...

2007
MARCIN NOWAK JANUSZ A. MADEJ PIOTR DZIĘGIEL

Using imunohistochemical technique, localisation and intensity of COX2 expression were estimated in canine soft tissue fibrosarcomas. The obtained results were related to tumour grade of malignancy. The material was sampled in the course of surgery from 23 dogs of various breed, 5 to 18 years of age. The presence of COX2 was demonstrated in cell cytoplasm in over 43% tumours. Augmented expressi...

2011
Panagiotis A Konstantinopoulos Michalis V Karamouzis Athanasios G Papavassiliou

COX2 is an enzyme that belongs to the prostaglandin G/H synthase family. It consists of 604 amino acids and has a molecular weight of 68996 Da. COX2 possesses two catalytic activities and respective active sites: a cyclooxygenase (COX) that converts arachidonic acid to a prostaglandin endoperoxide, prostaglandin G2 (PGG2), and; a peroxidase (POX) that reduces PGG2 to PGH2. COX2 functions as hom...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2012
Ye Gao Björn Meyer Lucie Sokolova Klaus Zwicker Michael Karas Bernd Brutschy Guohong Peng Hartmut Michel

The cytochrome c oxidase Cox2 has been purified from native membranes of the hyperthermophilic eubacterium Aquifex aeolicus. It is a cytochrome ba(3) oxidase belonging to the family B of the heme-copper containing terminal oxidases. It consists of three subunits, subunit I (CoxA2, 63.9 kDa), subunit II (CoxB2, 16.8 kDa), and an additional subunit IIa of 5.2 kDa. Surprisingly it is able to oxidi...

Journal: :Genetics 2009
Heather L Fiumera Maitreya J Dunham Scott A Saracco Christine A Butler Jessica A Kelly Thomas D Fox

Members of the Oxa1/YidC/Alb3 family of protein translocases are essential for assembly of energy-transducing membrane complexes. In Saccharomyces cerevisiae, Oxa1 and its paralog, Cox18, are required for assembly of Cox2, a mitochondrially encoded subunit of cytochrome c oxidase. Oxa1 is known to be required for cotranslational export of the Cox2 N-terminal domain across the inner mitochondria...

2017
Sheeja Aravindan Satishkumar Ramraj Kathiresan Kandasamy Somasundaram S. Thirugnanasambandan Dinesh Babu Somasundaram Terence S. Herman Natarajan Aravindan

Therapy-resistant pancreatic cancer (PC) cells play a crucial role in tumor relapse, recurrence, and metastasis. Recently, we showed the anti-PC potential of an array of seaweed polyphenols and identified efficient drug deliverables. Herein, we investigated the benefit of one such deliverable, Hormophysa triquerta polyphenol (HT-EA), in regulating the dissemination physiognomy of therapy-resist...

Journal: :Genetics and molecular research : GMR 2015
Y-Q Feng Y U Li W-D Xiao G-X Wang Y O Li

The aim of this study was to investigate the association between the cyclooxygenase 2 (COX2) -765G>C (rs20417) polymorphism and prostate cancer (PC) risk using meta-analysis. A systematic literature search was performed using the PubMed, Embase, Cochrane Library, and Google Scholar databases by using the terms "cyclooxygenase-2/COX-2/PTGs2", "polymorphism" or "variation", and "prostate" and "ca...

Journal: :The Journal of biological chemistry 2008
Kevin Rigby Paul A Cobine Oleh Khalimonchuk Dennis R Winge

Sco1 is implicated in the copper metallation of the Cu(A) site in Cox2 of cytochrome oxidase. The structure of Sco1 in the metallated and apo-conformers revealed structural dynamics primarily in an exposed region designated loop 8. The structural dynamics of loop 8 in Sco1 suggests it may be an interface for interactions with Cox17, the Cu(I) donor and/or Cox2. A series of conserved residues in...

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