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artikulong pang-agham مقالة علمية نشرت بتاريخ 25-7-2014 teaduslik artikkel vitenskapelig artikkel article scientific artykuł naukowy บทความทางวิทยาศาสตร์ научна статия 2014年学术文章 vitskapeleg artikkel מאמר מדעי научни чланак 2014年学术文章 vedecký článok мақолаи илмӣ artículu científicu espublizáu en 2014 2014年學術文章 artigo científico 2014 թուականի Յուլիսին հրատարակուած գիտական յօդուած articolo scientifico bài báo khoa học mokslinis straipsnis videnskabelig artikel (udgivet 2014) 2014年學術文章 2014年学术文章 artikull shkencor bilimsel makale 2014年學術文章 наукова стаття, опублікована в липні 2014 article publié dans la revue scientifique Journal of Biological Chemistry articol științific სამეცნიერო სტატია tieteellinen artikkeli artigo científico (publicado na 2014) wetenschappelijk artikel vědecký článek artigo científico (publicado na 2014) naučni članak tudományos cikk 2014년 논문 2014 թվականի հուլիսին հրատարակված գիտական հոդված 2014年の論文 мақолаи илмӣ научная статья 2014 nî lūn-bûn artículo científico publicado en 2014 article científic ২০১৪-এ প্রকাশিত বৈজ্ঞানিক নিবন্ধ 2014年学术文章 مقالهٔ علمی 2014年學術文章 2014年学术文章 سائنسی مضمون 2014年學術文章 2014年學術文章 научни чланак scienca artikolo wissenschaftlicher Artikel scientific article vetenskaplig artikel επιστημονικό άρθρο
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The N- and C-terminal domains of tomosyn play distinct roles in soluble N-ethylmaleimide-sensitive factor attachment protein receptor binding and fusion regulation The N- and C-terminal domains of tomosyn play distinct roles in soluble N-ethylmaleimide-sensitive factor attachment protein receptor binding and fusion regulation The N- and C-terminal domains of tomosyn play distinct roles in soluble N-ethylmaleimide-sensitive factor attachment protein receptor binding and fusion regulation
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The N- and C-terminal domains of tomosyn play distinct roles in soluble N-ethylmaleimide-sensitive factor attachment protein receptor binding and fusion regulation The N- and C-terminal domains of tomosyn play distinct roles in soluble N-ethylmaleimide-sensitive factor attachment protein receptor binding and fusion regulation The N- and C-terminal domains of tomosyn play distinct roles in soluble N-ethylmaleimide-sensitive factor attachment protein receptor binding and fusion regulation
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The N- and C-terminal domains of tomosyn play distinct roles in soluble N-ethylmaleimide-sensitive factor attachment protein receptor binding and fusion regulation The N- and C-terminal domains of tomosyn play distinct roles in soluble N-ethylmaleimide-sensitive factor attachment protein receptor binding and fusion regulation The N- and C-terminal domains of tomosyn play distinct roles in soluble N-ethylmaleimide-sensitive factor attachment protein receptor binding and fusion regulation
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The N- and C-terminal domains of tomosyn play distinct roles in soluble N-ethylmaleimide-sensitive factor attachment protein receptor binding and fusion regulation
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