Large-Scale Recombinant Production of the SARS-CoV-2 Proteome for High-Throughput and Structural Biology Applications

Autor: Nadide Altincekic, Sophie Marianne Korn, Nusrat Shahin Qureshi, Marie Dujardin, Martí Ninot-Pedrosa, Rupert Abele, Marie Jose Abi Saad, Caterina Alfano, Fabio C. L. Almeida, Islam Alshamleh, Gisele Cardoso de Amorim, Thomas K. Anderson, Cristiane D. Anobom, Chelsea Anorma, Jasleen Kaur Bains, Adriaan Bax, Martin Blackledge, Julius Blechar, Anja Böckmann, Louis Brigandat, Anna Bula, Matthias Bütikofer, Aldo R. Camacho-Zarco, Teresa Carlomagno, Icaro Putinhon Caruso, Betül Ceylan, Apirat Chaikuad, Feixia Chu, Laura Cole, Marquise G. Crosby, Vanessa de Jesus, Karthikeyan Dhamotharan, Isabella C. Felli, Jan Ferner, Yanick Fleischmann, Marie-Laure Fogeron, Nikolaos K. Fourkiotis, Christin Fuks, Boris Fürtig, Angelo Gallo, Santosh L. Gande, Juan Atilio Gerez, Dhiman Ghosh, Francisco Gomes-Neto, Oksana Gorbatyuk, Serafima Guseva, Carolin Hacker, Sabine Häfner, Bing Hao, Bruno Hargittay, K. Henzler-Wildman, Jeffrey C. Hoch, Katharina F. Hohmann, Marie T. Hutchison, Kristaps Jaudzems, Katarina Jović, Janina Kaderli, Gints Kalniņš, Iveta Kaņepe, Robert N. Kirchdoerfer, John Kirkpatrick, Stefan Knapp, Robin Krishnathas, Felicitas Kutz, Susanne zur Lage, Roderick Lambertz, Andras Lang, Douglas Laurents, Lauriane Lecoq, Verena Linhard, Frank Löhr, Anas Malki, Luiza Mamigonian Bessa, Rachel W. Martin, Tobias Matzel, Damien Maurin, Seth W. McNutt, Nathane Cunha Mebus-Antunes, Beat H. Meier, Nathalie Meiser, Miguel Mompeán, Elisa Monaca, Roland Montserret, Laura Mariño Perez, Celine Moser, Claudia Muhle-Goll, Thais Cristtina Neves-Martins, Xiamonin Ni, Brenna Norton-Baker, Roberta Pierattelli, Letizia Pontoriero, Yulia Pustovalova, Oliver Ohlenschläger, Julien Orts, Andrea T. Da Poian, Dennis J. Pyper, Christian Richter, Roland Riek, Chad M. Rienstra, Angus Robertson, Anderson S. Pinheiro, Raffaele Sabbatella, Nicola Salvi, Krishna Saxena, Linda Schulte, Marco Schiavina, Harald Schwalbe, Mara Silber, Marcius da Silva Almeida, Marc A. Sprague-Piercy, Georgios A. Spyroulias, Sridhar Sreeramulu, Jan-Niklas Tants, Kaspars Tārs, Felix Torres, Sabrina Töws, Miguel Á. Treviño, Sven Trucks, Aikaterini C. Tsika, Krisztina Varga, Ying Wang, Marco E. Weber, Julia E. Weigand, Christoph Wiedemann, Julia Wirmer-Bartoschek, Maria Alexandra Wirtz Martin, Johannes Zehnder, Martin Hengesbach, Andreas Schlundt

Publikováno v: Frontiers in Molecular Biosciences, Vol 8 (2021)

The highly infectious disease COVID-19 caused by the Betacoronavirus SARS-CoV-2 poses a severe threat to humanity and demands the redirection of scientific efforts and criteria to organized research projects. The international COVID19-NMR consortium

Externí odkaz: https://doaj.org/article/201170fa84b8450e9b468d9fb4480774

Backbone 1H, 15N, and 13C resonance assignments of the non-structural protein NS2B of Zika virus

Autor: Beatriz Rosa Penna, Cristiane D. Anobom, Danielle M.P. Oliveira, Ana Paula Valente

Publikováno v: Biomolecular NMR Assignments. 16:31-35

Zika virus (ZIKV) emerged as a global public health concern due to its relationship with severe neurological disorders. Non-structural (NS) proteins of ZIKV are essential for viral replication, regulatory function, and subversion of host responses. N

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::6e912604d9406b31035b0ea2f47f53fb
https://doi.org/10.1007/s12104-021-10055-2

Structure insights, thermodynamic profiles, dsDNA melting activity, and liquid-liquid phase separation of the SARS-CoV-2 nucleocapsid N-terminal domain binding to DNA

Autor: Thais Cristtina Neves-Martins, Aline de Luna Marques, Gabriela R. Araujo, Mariana J. do Amaral, Isabella Otenio de Lourenço, Vitor S. Almeida, Ícaro Putinhon Caruso, Francisco Gomes-Neto, Guilherme Caldas Andrade, Andrea T. Da Poian, Talita S. Araujo, Glauce M. Barbosa, Karoline Sanches, Ariana A. Vasconcelos, Clara L. F. Malizia-Motta, Katia M. S. Cabral, Peter Reis Bezerra, Marcos Caique Santana-Silva, Nathane C. Mebus-Antunes, Jessica M. Azevedo, Cristiane D. Anobom, Leonardo Bartkevihi, Gisele Cardoso Amorim, Fabio C. L. Almeida, Jessica M. Sa, Anderson S. Pinheiro, Marcius S. Almeida

The SARS-CoV-2 nucleocapsid protein (N) is a multifunctional promiscuous nucleic acid-binding protein, which plays a major role in nucleocapsid assembly and discontinuous RNA transcription, facilitating the template switch of transcriptional regulato

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::2ba4092d34b6208964bdc927921ac0ff
https://doi.org/10.1101/2021.07.21.453232

A ligand peptide motif selected from a cancer patient is a receptor-interacting site within human interleukin-11.

Autor: Marina Cardó-Vila, Amado J Zurita, Ricardo J Giordano, Jessica Sun, Roberto Rangel, Liliana Guzman-Rojas, Cristiane D Anobom, Ana P Valente, Fábio C L Almeida, Johanna Lahdenranta, Mikhail G Kolonin, Wadih Arap, Renata Pasqualini

Publikováno v: PLoS ONE, Vol 3, Iss 10, p e3452 (2008)

Interleukin-11 (IL-11) is a pleiotropic cytokine approved by the FDA against chemotherapy-induced thrombocytopenia. From a combinatorial selection in a cancer patient, we isolated an IL-11-like peptide mapping to domain I of the IL-11 (sequence CGRRA

Externí odkaz: https://doaj.org/article/312aff42208e4999b42e49e1ed95db38

Refolding, purification, and preliminary structural characterization of the DNA-binding domain of the quorum sensing receptor RhlR from Pseudomonas aeruginosa

Autor: Carolina Lixa, Luís Maurício T.R. Lima, Adriana Fonseca Marques, Anderson S. Pinheiro, Cristiane D. Anobom, Juliana R. Cortines, Bianca Cruz Neves, Danielle M.P. Oliveira

Publikováno v: Protein Expression and Purification. 121:31-40

RhlR is a 241-residue quorum sensing receptor that controls the expression of a myriad of virulence genes in Pseudomonas aeruginosa. Here, the DNA sequence encoding the carboxi-terminal DNA-binding domain of RhlR was cloned into the pET-RP1B plasmid

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c58be07721ac5e3099ede91abc9a17bc
https://doi.org/10.1016/j.pep.2016.01.006