نتایج جستجو برای: type vii collagen

تعداد نتایج: 1402056  

Journal: :medical journal of islamic republic of iran 0
kamran mousavi hosseini blood transfusion research center, high institute for research and education in transfusion medicine, tehran, iran.سازمان اصلی تایید شده: سازمان انتقال خون ایران (blood transfusion research center)سازمان های دیگر: blood transfusion research center, saleh nasiri blood transfusion research center, high institute for research and education in transfusion medicine, tehran, iran.سازمان اصلی تایید شده: سازمان انتقال خون ایران (blood transfusion research center)سازمان های دیگر: blood transfusion research center,

background: factor vii concentrates are used in patients with congenital or acquired factor vii deficiency or treatment of hemophilia patients with inhibitors. in this research, immunoaffinity chromatography was used to purify factor vii from prothrombin complex (prothrombin-proconvertin-stuart factor-antihemophilic factor b or ppsb) which contains coagulation factors ii, vii, ix and x. the aim...

Journal: :The Biochemical journal 2003
Ryan J Medeck Sergio Sosa Nicholas Morris Julia Thom Oxford

Collagen type XI is a minor constituent of heterotypic collagen fibrils of developing cartilage and plays a regulatory role in fibril diameter. Collagen type XI is a heterotrimer composed of the alpha1, alpha2 and alpha3 chains. The mRNA encoding exons 6a, 6b and 8 of the alpha1 chain are expressed alternatively to generate six possible isoforms. The 6b-containing isoform has the most restricte...

Journal: :Journal of cosmetic dermatology 2012
Moetaz El-Domyati Tarek S El-Ammawi Walid Medhat Osama Moawad Mỹ G Mahoney Jouni Uitto

BACKGROUND As the demand for minimally invasive rejuvenation is increasing, micropeel resurfacing using Erbium:Yttrium Aluminum Garnet (Er:YAG) laser 2940 nm has been reported for the treatment of photoaged skin without ablation of the epidermis. However, little is known about the efficacy and underlying histologic changes associated with this type of treatment. AIMS The aims of this study ar...

Journal: :Cell 2006
Roy Morello Terry K. Bertin Yuqing Chen John Hicks Laura Tonachini Massimiliano Monticone Patrizio Castagnola Frank Rauch Francis H. Glorieux Janice Vranka Hans Peter Bächinger James M. Pace Ulrike Schwarze Peter H. Byers MaryAnn Weis Russell J. Fernandes David R. Eyre Zhenqiang Yao Brendan F. Boyce Brendan Lee

Prolyl hydroxylation is a critical posttranslational modification that affects structure, function, and turnover of target proteins. Prolyl 3-hydroxylation occurs at only one position in the triple-helical domain of fibrillar collagen chains, and its biological significance is unknown. CRTAP shares homology with a family of putative prolyl 3-hydroxylases (P3Hs), but it does not contain their co...

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