π€ Hilgenfeld, Rolf
Keywords
Articles (24)
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An efficient method for the synthesis of peptide aldehyde libraries employed in the discovery of reversible SARS coronavirus main protease (SARS-Cov Mpro) inhibitors
π€ Al-Gharabli, Samer I. π€ Ali Shah, Syed T. π€ Weik, Steffen π€ Schmidt, Marco F. π€ Mesters, Jeroen R. π€ Kuhn, Daniel π€ Klebe, Gerhard π€ Hilgenfeld, Rolf π€ Rademann, JΓΆrg β° 2006 π ChemBioChem
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Structure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra Ξ±-helical domain
π€ Anand, Kanchan π€ Palm, Gottfried J. π€ Mesters, Jeroen R. π€ Siddell, Stuart G. π€ Ziebuhr, John π€ Hilgenfeld, Rolf β° 2002 π EMBO Journal
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Coronavirus main proteinase (3CLpro) Structure: Basis for design of anti-SARS drugs
π€ Anand, Kanchan π€ Ziebuhr, John π€ Wadhwani, Parvesh π€ Mesters, Jeroen R. π€ Hilgenfeld, Rolf β° 2003 π Science
- From SARS to MERS: crystallographic studies on coronaviral proteases enable antiviral drug design
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From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses
π€ Hilgenfeld, Rolf π€ Peiris, Malik β° 2013 π Antiviral Research
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A G-quadruplex-binding macrodomain within the "SARS-unique domain" is essential for the activity of the SARS-coronavirus replication-transcription complex
π€ Kusov, Yuri π€ Tan, Jinzhi π€ Alvarez, Enrique π€ Enjuanes, Luis π€ Hilgenfeld, Rolf β° 2015 π Virology
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Structural and mutational analysis of the interaction between the Middle-East respiratory syndrome coronavirus (MERS-CoV) papain-like protease and human ubiquitin
π€ Lei, Jian π€ Hilgenfeld, Rolf β° 2016 π Virologica Sinica
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Nsp3 of coronaviruses: Structures and functions of a large multi-domain protein
π€ Lei, Jian π€ Kusov, Yuri π€ Hilgenfeld, Rolf β° 2018 π Antiviral Research
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Crystal structure of the papain-like protease of MERS coronavirus reveals unusual, potentially druggable active-site features
π€ Lei, Jian π€ Mesters, Jeroen R. π€ Drosten, Christian π€ AnemΓΌller, Stefan π€ Ma, Qingjun π€ Hilgenfeld, Rolf β° 2014 π Antiviral Research
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Accessory proteins of SARS-CoV and other coronaviruses
π€ Liu, Ding Xiang π€ Fung, To Sing π€ Chong, Kelvin Kian Long π€ Shukla, Aditi π€ Hilgenfeld, Rolf β° 2014 π Antiviral Research
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Nucleocapsid protein of SARS coronavirus tightly binds to human cyclophilin A
π€ Luo, Cheng π€ Luo, Haibin π€ Zheng, Suxin π€ Gui, Chunshan π€ Yue, Liduo π€ Yu, Changying π€ Sun, Tao π€ He, Peilan π€ Chen, Jing π€ Shen, Jianhua π€ Luo, Xiaomin π€ Li, Yixue π€ Liu, Hong π€ Bai, Donglu π€ Shen, Jingkang π€ Yang, Yiming π€ Li, Fangqiu π€ Zuo, Jianping π€ Hilgenfeld, Rolf π€ Pei, Gang π€ Chen, Kaixian π€ Shen, Xu π€ Jiang, Hualiang β° 2004 π Biochemical and Biophysical Research Communications
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P53 down-regulates SARS coronavirus replication and is targeted by the SARS-unique domain and PLpro via E3 ubiquitin ligase RCHY1
π€ Ma-Lauer, Yue π€ Carbajo-Lozoya, Javier π€ Hein, Marco Y. π€ MΓΌller, Marcel A. π€ Deng, Wen π€ Lei, Jian π€ Meyer, Benjamin π€ Kusov, Yuri π€ Von Brunn, Brigitte π€ Bairad, Dev Raj π€ HΓΌnten, Sabine π€ Drosten, Christian π€ Hermeking, Heiko π€ Leonhardt, Heinrich π€ Mann, Matthias π€ Hilgenfeld, Rolf π€ Von Brunn, Albrecht β° 2016 π Proceedings of the National Academy of Sciences of the United States of America
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The SARS-Coronavirus-host interactome: Identification of cyclophilins as target for pan-Coronavirus inhibitors
π€ Pfefferle, Susanne π€ SchΓΆpf, Julia π€ KΓΆgl, Manfred π€ Friedel, Caroline C. π€ MΓΌller, Marcel A. π€ Carbajo-Lozoya, Javier π€ Stellberger, Thorsten π€ von Dall'Armi, Ekatarina π€ Herzog, Petra π€ Kallies, Stefan π€ Niemeyer, Daniela π€ Ditt, Vanessa π€ Kuri, Thomas π€ ZΓΌst, Roland π€ Pumpor, Ksenia π€ Hilgenfeld, Rolf π€ Schwarz, Frank π€ Zimmer, Ralf π€ Steffen, Imke π€ Weber, Friedemann π€ Thiel, Volker π€ Herrler, Georg π€ Thiel, Heinz JΓΌrgen π€ Schwegmann-WeΓels, Christel π€ PΓΆhlmann, Stefan π€ Haas, JΓΌrgen π€ Drosten, Christian π€ von Brunn, Albrecht β° 2011 π PLoS Pathogens
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Crystal structures of the X-domains of a Group-1 and a Group-3 coronavirus reveal that ADP-ribose-binding may not be a conserved property
π€ Piotrowski, Yvonne π€ Hansen, Guido π€ Boomaars-van Der Zanden, A. Linda π€ Snijder, Eric J. π€ Gorbalenya, Alexander E. π€ Hilgenfeld, Rolf β° 2009 π Protein Science
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Variable Oligomerization Modes in Coronavirus Non-structural Protein 9
π€ Ponnusamy, Rajesh π€ Moll, Ralf π€ Weimar, Thomas π€ Mesters, Jeroen R. π€ Hilgenfeld, Rolf β° 2008 π Journal of Molecular Biology
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Acquisition of new protein domains by coronaviruses: analysis of overlapping genes coding for proteins N and 9b in SARS coronavirus
π€ Shukla, Aditi π€ Hilgenfeld, Rolf β° 2015 π Virus Genes
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The "SARS-unique domain" (SUD) of SARS coronavirus is an oligo(G)-binding protein
π€ Tan, Jinzhi π€ Kusov, Yuri π€ Mutschall, Doris π€ Tech, Stefanie π€ Nagarajan, Krishna π€ Hilgenfeld, Rolf π€ Schmidt, Christian L. β° 2007 π Biochemical and Biophysical Research Communications
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The SARS-Unique Domain (SUD) of SARS coronavirus contains two macrodomains that bind G-quadruplexes
π€ Tan, Jinzhi π€ Vonrhein, Clemens π€ Smart, Oliver S. π€ Bricogne, Gerard π€ Bollati, Michela π€ Kusov, Yuri π€ Hansen, Guido π€ Mesters, Jeroen R. π€ Schmidt, Christian L. π€ Hilgenfeld, Rolf β° 2009 π PLoS Pathogens
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A Structural View of the Inactivation of the SARS Coronavirus Main Proteinase by Benzotriazole Esters
π€ Verschueren, Koen H.G. π€ Pumpor, Ksenia π€ AnemΓΌller, Stefan π€ Chen, Shuai π€ Mesters, Jeroen R. π€ Hilgenfeld, Rolf β° 2008 π Chemistry and Biology
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Structure of the X (ADRP) domain of nsp3 from feline coronavirus
π€ Wojdyla, Justyna A. π€ Manolaridis, Ioannis π€ Snijder, Eric J. π€ Gorbalenya, Alexander E. π€ Coutard, Bruno π€ Piotrowski, Yvonne π€ Hilgenfeld, Rolf π€ Tucker, Paul A. β° 2009 π Acta Crystallographica Section D: Biological Crystallography
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Nonstructural proteins 7 and 8 of feline coronavirus form a 2:1 heterotrimer that exhibits primer-independent RNA polymerase activity
π€ Xiao, Yibei π€ Ma, Qingjun π€ Restle, Tobias π€ Shang, Weifeng π€ Svergun, Dmitri I. π€ Ponnusamy, Rajesh π€ Sczakiel, Georg π€ Hilgenfeld, Rolf β° 2012 π Journal of Virology
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Design of wide-spectrum inhibitors targeting coronavirus main proteases
π€ Yang, Haitao π€ Xie, Weiqing π€ Xue, Xiaoyu π€ Yang, Kailin π€ Ma, Jing π€ Liang, Wenxue π€ Zhao, Qi π€ Zhou, Zhe π€ Pei, Duanqing π€ Ziebuhr, John π€ Hilgenfeld, Rolf π€ Kwok, Yung Yuen π€ Wong, Luet π€ Gao, Guangxia π€ Chen, Saijuan π€ Chen, Zhu π€ Ma, Dawei π€ Bartlam, Mark π€ Rao, Zihe β° 2005 π PLoS Biology
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Crystal structure of SARS-CoV-2 main protease provides a basis for design of improved alpha-ketoamide inhibitors.
π€ Zhang, Linlin π€ Lin, Daizong π€ Sun, Xinyuanyuan π€ Curth, Ute π€ Drosten, Christian π€ Sauerhering, Lucie π€ Becker, Stephan π€ Rox, Katharina π€ Hilgenfeld, Rolf β° 2020 π Science
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Peptide aldehyde inhibitors challenge the substrate specificity of the SARS-coronavirus main protease
π€ Zhu, Lili π€ George, Shyla π€ Schmidt, Marco F. π€ Al-Gharabli, Samer I. π€ Rademann, JΓΆrg π€ Hilgenfeld, Rolf β° 2011 π Antiviral Research