1.Transient HIV-1 Gag–protease interactions revealed by paramagnetic NMR suggest origins of compensatory drug resistance mutations

作　　者：Lalit Deshmukh ;John M. Louis ;Rodolfo Ghirlando 等

出　　处：Proceedings of the National Academy of Sciences. 2016 ;113(44):12456-12461.doi:10.1073/pnas.1615342113

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

文章 ID：184627837

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2.Conformation and dynamics of the Gag polyprotein of the human immunodeficiency virus 1 studied by NMR spectroscopy

作　　者：Lalit Deshmukh ;Rodolfo Ghirlando ;G. Marius Clore

出　　处：Proceedings of the National Academy of Sciences. 2015 ;112(11):3374-3379.doi:10.1073/pnas.1501985112

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

文章 ID：103255027

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3.Binding kinetics and substrate selectivity in HIV-1 protease−Gag interactions probed at atomic resolution by chemical exchange NMR

作　　者：Lalit Deshmukh ;Vitali Tugarinov ;John M. Louis 等

出　　处：Proceedings of the National Academy of Sciences. 2017 ;114(46):E9855-E9862.doi:10.1073/pnas.1716098114

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

文章 ID：206856137

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4.Proline-rich domain of human ALIX contains multiple TSG101-UEV interaction sites and forms phosphorylation-mediated reversible amyloids

作　　者：Ruben D. Elias ;Wen Ma ;Rodolfo Ghirlando 等

出　　处：Proceedings of the National Academy of Sciences. 2020 ;117(39):24274-24284.doi:10.1073/pnas.2010635117

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

文章 ID：260994610

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