نتایج جستجو برای: human epidermal growth factor hegf

تعداد نتایج: 2834881  

Journal: :Protein and peptide letters 2006
Zhijian Su Yadong Huang Quannan Zhou Zhiling Wu Xiaoping Wu Qing Zheng Changcai Ding Xiaokun Li

Human epidermal growth factor (hEGF) can stimulate the division of various cell types and has potential clinical applications. However, the high expression of active hEGF in Escherichia coli has not been successful, as the protein contains three intra-molecular disulfide bonds that are difficult to form correctly in the bacterial intracellular environment. To solve this problem, we fused the hE...

2009
Jorge Valdés Ernesto Mantilla Gabriel Márquez Regla M Bonilla Victoria M Lugo Mariela Pérez Yanara García Emilio Narciandi

Human Epidermal Growth Factor (hEGF) is a protein molecule with potent mitogenic activity, increasing the rate of wound and ulcer healing in different tissues of the human body. In recent years, the Center for Genetic Engineering and Biotechnology (CIGB) has carried out projects at the developmental stages for the application of hEGF in novel therapies. It is now necessary to increase productio...

Journal: :The Journal of clinical investigation 1991
S A Rogers S B Miller M R Hammerman

The renal collecting duct is a site of insulin-like growth factor I (IGF I) synthesis. Epidermal growth factor (EGF) is also synthesized within the kidney in the thick ascending limb of Henle's loop and the distal tubule. EGF has been shown to regulate IGF I expression in nonrenal tissues. To shed light upon a role of EGF in intrarenal regulation of IGF I gene expression, plasma membranes prepa...

2016
Sara Pouranvari Firouz Ebrahimi Gholamreza Javadi Bozorgmehr Maddah

BACKGROUND Epidermal growth factor (EGF) plays a fundamental role in the healing of wounds relating to skin damage, the cornea, and the gastrointestinal tract. OBJECTIVES The aim of this study is the cloning, expression, and purification of recombinant human EGF (rhEGF), and an assessment of its activity. MATERIALS AND METHODS In the present experimental study, a synthetic pET28a (+) -hEGF ...

Aftab Bashir, Mina Ebrahimi-Rad, Morteza Azarnoosh, Vladimir V. Bakayev,

Expression of eukaryotic proteins in E. coli often results in their aggregation. Proper folding and solubility of therapeutical proteins are the pre-requisite for their bioactivity. This is not achieved in cytoplasmic expression in E. coli because of the absence of disulfide bonds formation. A novel expression/secretion vector was constructed which exploited β-lactamase signal sequence to trans...

2017
Monique L. M. van de Poll Marianne J. H. van Vugt Anne E. G. Lenferink Everardus J. J. van Zoelen

Epidermal growth factor (EGF) 1 belongs to a family of structurally related growth factors which all exert their action by binding to the epidermal growth factor receptor (Carpenter & Wahl, 1991). Many tumor cells express this receptor, and also secrete members of this family of EGF-like molecules, thus creating the possibility of an autocrine growth factor cycle. In particular, the role of tra...

Journal: :Acta crystallographica. Section D, Biological crystallography 2000
J J Chai M Li B R Huang Y Luo M Luo R C Bi C H He

Human epidermal growth factor (hEGF), a 6.2 kDa protein of 53 amino acids with three internal disulfide bridges, has been crystallized by the hanging-drop method. hEGF crystallizes in space group P3(1)21 (or P3(2)21) using MgCl(2) as precipitant, with unit-cell parameters a = b = 61.4, c = 87.0 A. Another type of crystal, obtained using NaCl as precipitant, belongs to a tetragonal point group a...

Journal: :Investigative ophthalmology & visual science 1990
T Kitazawa S Kinoshita K Fujita K Araki H Watanabe Y Ohashi R Manabe

The effect of biosynthetic human epidermal growth factor (hEGF) was investigated on a 10-mm diameter corneal epithelial defect model in rabbits. Topical application of over 10 micrograms/ml of hEGF five times a day significantly enhanced the epithelial healing rate, in a dose-dependent manner. The maximum healing rate was observed in eyes treated with 20 micrograms/ml of hEGF (1.59 +/- 0.26 mm2...

Journal: :Journal of nuclear medicine : official publication, Society of Nuclear Medicine 2008
Zhongli Cai Zhuo Chen Kristy E Bailey Deborah A Scollard Raymond M Reilly Katherine A Vallis

UNLABELLED The Auger electron-emitting radiopharmaceutical 111In-diethylenetriaminepentaacetic acid human epidermal growth factor (111In-DTPA-hEGF) binds the epidermal growth factor receptor (EGFR), is internalized, and translocates to the nucleus. The purpose of this study was to investigate the relationship between EGFR expression, DNA damage, and cytotoxicity in cells exposed to 111In-DTPA-h...

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