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bài báo khoa học 2003年論文 научна статия 2003年論文 επιστημονικό άρθρο 2003 թվականի հուլիսին հրատարակված գիտական հոդված articol științific wetenschappelijk artikel (gepubliceerd op 2003/07/11) artikulong pang-agham ২০০৩-এ প্রকাশিত বৈজ্ঞানিক নিবন্ধ tudományos cikk scientific article artículo científico publicado en 2003 2003年论文 2003年论文 2003년 논문 naučni članak article scientific artykuł naukowy наукова стаття, опублікована в липні 2003 2003年の論文 2003年论文 artigo científico (publicado na 2003/07/11) мақолаи илмӣ 2003年論文 2003 թուականի Յուլիսին հրատարակուած գիտական յօդուած 2003 nî lūn-bûn مقالهٔ علمی vetenskaplig artikel (publicerad på 2003/07/11) bilimsel makale articolo scientifico (pubblicato il 2003/07/11) artigo científico научная статья مقالة علمية (نشرت في 11-7-2003) vitenskapelig artikkel 2003年论文 2003年論文 บทความทางวิทยาศาสตร์ tieteellinen artikkeli מאמר מדעי teaduslik artikkel mokslinis straipsnis vitskapeleg artikkel videnskabelig artikel (udgivet 2003/07/11) научни чланак (објављен 2003/07/11) vedecký článok (publikovaný 2003/07/11) wissenschaftlicher Artikel artikull shkencor scienca artikolo 2003年论文 artigo científico (publicado na 2003) научни чланак artículu científicu espublizáu en 2003 article científic мақолаи илмӣ სამეცნიერო სტატია 2003年论文 vědecký článek publikovaný v roce 2003 2003年論文 article scientifique (publié 2003/07/11) سائنسی مضمون
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Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network
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Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network
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Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network
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Crystal structure of Escherichia coli thioesterase I/protease I/lysophospholipase L1: consensus sequence blocks constitute the catalytic center of SGNH-hydrolases through a conserved hydrogen bond network
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