1.Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril

作　　者：Marielle Aulikki Wälti ;Francesco Ravotti ;Hiromi Arai 等

出　　处：Proceedings of the National Academy of Sciences. 2016 ;113(34):E4976-E4984.doi:10.1073/pnas.1600749113

出版社：The National Academy of Sciences of the United States of America

文章 ID：182290806

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2.The fold of α-synuclein fibrils

作　　者：Marçal Vilar ;Hui-Ting Chou ;Thorsten Lührs 等

出　　处：Proceedings of the National Academy of Sciences. 2008 ;105(25):8637-8642.doi:10.1073/pnas.0712179105

出版社：The National Academy of Sciences of the United States of America

文章 ID：75178673

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3.3D structure of Alzheimer's amyloid-β(1–42) fibrils

作　　者：Thorsten Lührs ;Christiane Ritter ;Marc Adrian 等

出　　处：Proceedings of the National Academy of Sciences. 2005 ;102(48):17342-17347.doi:10.1073/pnas.0506723102

出版社：The National Academy of Sciences of the United States of America

文章 ID：75177125

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4.Structure based aggregation studies reveal the presence of helix-rich intermediate during α-Synuclein aggregation

作　　者：Dhiman Ghosh ;Pradeep K. Singh ;Shruti Sahay 等

出　　处：Scientific Reports. 2015 ;5.doi:10.1038/srep09228

出版社：Springer Nature

文章 ID：110738146

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5.Structure based aggregation studies reveal the presence of helix-rich intermediate during α-Synuclein aggregation

作　　者：Dhiman Ghosh ;Pradeep K. Singh ;Shruti Sahay 等

出　　处：Scientific Reports. 2015 ;5(1).doi:10.1038/srep09228

出版社：Springer Nature

文章 ID：235875624

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6.Cotranslational structure acquisition of nascent polypeptides monitored by NMR spectroscopy

作　　者：Cédric Eichmann ;Steffen Preissler ;Roland Riek 等

出　　处：Proceedings of the National Academy of Sciences. 2010 ;107(20):9111-9116.doi:10.1073/pnas.0914300107

出版社：The National Academy of Sciences of the United States of America

文章 ID：200517535

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7.TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain

作　　者：Eva-Maria Frickel ;Roland Riek ;Ilian Jelesarov 等

出　　处：Proceedings of the National Academy of Sciences. 2002 ;99(4):1954-1959.doi:10.1073/pnas.042699099

出版社：The National Academy of Sciences of the United States of America

文章 ID：200565215

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8.NMR structure and peptide hormone binding site of the first extracellular domain of a type B1 G protein-coupled receptor

作　　者：Christy R. R. Grace ;Marilyn H. Perrin ;Michael R. DiGruccio 等

出　　处：Proceedings of the National Academy of Sciences. 2004 ;101(35):12836-12841.doi:10.1073/pnas.0404702101

出版社：The National Academy of Sciences of the United States of America

文章 ID：200590904

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9.NMR structure of the calreticulin P-domain

作　　者：Lars Ellgaard ;Roland Riek ;Torsten Herrmann 等

出　　处：Proceedings of the National Academy of Sciences. 2001 ;98(6):3133-3138.doi:10.1073/pnas.051630098

出版社：The National Academy of Sciences of the United States of America

文章 ID：200559105

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10.Identifying the amylome, proteins capable of forming amyloid-like fibrils

作　　者：Lukasz Goldschmidt ;Poh K. Teng ;Roland Riek 等

出　　处：Proceedings of the National Academy of Sciences. 2010 ;107(8):3487-3492.doi:10.1073/pnas.0915166107

出版社：The National Academy of Sciences of the United States of America

文章 ID：200519058

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	Proceedings of the National Academy of Sciences	11篇
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