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20 results on '"Fernandez-Cid, Alejandra"'

3. Performance characteristics of five immunoassays for SARS-CoV-2: a head-to-head benchmark comparison

Author

Ainsworth, Mark, Andersson, Monique, Auckland, Kathryn, Baillie, J Kenneth, Barnes, Eleanor, Beer, Sally, Beveridge, Amy, Bibi, Sagida, Blackwell, Luke, Borak, Martyna, Bown, Abbie, Brooks, Tim, Burgess-Brown, Nicola A, Camara, Susana, Catton, Matthew, Chau, Kevin K., Christott, Thomas, Clutterbuck, Elizabeth, Coker, Jesse, Cornall, Richard J, Cox, Stuart, Crawford-Jones, David, Crook, Derrick W, D'Arcangelo, Silvia, Dejnirattsai, Wanwisa, Dequaire, Julie M M, Dimitriadis, Stavros, Dingle, Kate E, Doherty, George, Dold, Christina, Dong, Tao, Dunachie, Susanna J, Ebner, Daniel, Emmenegger, Marc, Espinosa, Alexis, Eyre, David W, Fairhead, Rory, Fassih, Shayan, Feehily, Conor, Felle, Sally, Fernandez-Cid, Alejandra, Fernandez Mendoza, Maria, Foord, Thomas H, Fordwoh, Thomas, Fox McKee, Deborah, Frater, John, Gallardo Sanchez, Veronica, Gent, Nick, Georgiou, Dominique, Groves, Christopher J, Hallis, Bassam, Hammond, Peter M, Hatch, Stephanie B., Harvala, Heli J, Hill, Jennifer, Hoosdally, Sarah J, Horsington, Bryn, Howarth, Alison, James, Tim, Jeffery, Katie, Jones, Elizabeth, Justice, Anita, Karpe, Fredrik, Kavanagh, James, Kim, David S, Kirton, Richard, Klenerman, Paul, Knight, Julian C, Koukouflis, Leonidas, Kwok, Andrew, Leuschner, Ullrich, Levin, Robert, Linder, Aline, Lockett, Teresa, Lumley, Sheila F, Marinou, Spyridoula, Marsden, Brian D, Martinez, Jose, Martins Ferreira, Lucas, Mason, Lara, Matthews, Philippa C, Mentzer, Alexander J, Mobbs, Alexander, Mongkolsapaya, Juthathip, Morrow, Jordan, Mukhopadhyay, Shubhashish M M, Neville, Matthew J, Oakley, Sarah, Oliveira, Marta, Otter, Ashley, Paddon, Kevin, Pascoe, Jordan, Peng, Yanchun, Perez, Elena, Perumal, Prem K, Peto, Timothy E A, Pickford, Hayleah, Ploeg, Rutger J, Pollard, Andrew J, Richardson, Anastasia, Ritter, Thomas G, Roberts, David J, Rodger, Gillian, Rollier, Christine S, Rowe, Cathy, Rudkin, Justine K, Screaton, Gavin, Semple, Malcolm G, Sienkiewicz, Alex, Silva-Reyes, Laura, Skelly, Donal T, Sobrino Diaz, Alberto, Stafford, Lizzie, Stockdale, Lisa, Stoesser, Nicole, Street, Teresa, Stuart, David I, Sweed, Angela, Taylor, Adan, Thraves, Hannah, Tsang, Hoi P, Verheul, Marije K, Vipond, Richard, Walker, Timothy M, Wareing, Susan, Warren, Yolanda, Wells, Charlie, Wilson, Clare, Withycombe, Kate, and Young, Rebecca K

Published
2020
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9. Phospho‐regulation, nucleotide binding and ion access control in potassium‐chloride cotransporters

Author

Chi, Gamma, Ebenhoch, Rebecca, Man, Henry, Tang, Haiping, Tremblay, Laurence E, Reggiano, Gabriella, Qiu, Xingyu, Bohstedt, Tina, Liko, Idlir, Almeida, Fernando G, Garneau, Alexandre P, Wang, Dong, McKinley, Gavin, Moreau, Christophe P, Bountra, Kiran D, Abrusci, Patrizia, Mukhopadhyay, Shubhashish M M, Fernandez‐Cid, Alejandra, Slimani, Samira, Lavoie, Julie L, Burgess‐Brown, Nicola A, Tehan, Ben, DiMaio, Frank, Jazayeri, Ali, Isenring, Paul, Robinson, Carol V, and Dürr, Katharina L

Published
2021
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10. High-Throughput Expression and Purification of Human Solute Carriers for Structural and Biochemical Studies

Author

Raturi, Sagar, primary, Li, Huanyu, additional, Chang, Yung-Ning, additional, Scacioc, Andreea, additional, Bohstedt, Tina, additional, Fernandez-Cid, Alejandra, additional, Evans, Adam, additional, Abrusci, Patrizia, additional, Balakrishnan, Abilasha, additional, Pascoa, Tomas C., additional, He, Didi, additional, Chi, Gamma, additional, Kaur Singh, Nanki, additional, Ye, Mingda, additional, Li, Anna, additional, Shrestha, Leela, additional, Wang, Dong, additional, Williams, Eleanor P., additional, Burgess-Brown, Nicola A., additional, Dürr, Katharina L., additional, Puetter, Vera, additional, Ingles-Prieto, Alvaro, additional, and Sauer, David B., additional

Published
2023
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14. Cryo-EM structure of the human Kv3.1 channel reveals gating control by the cytoplasmic T1 domain

Author

Chi, Gamma, primary, Liang, Qiansheng, additional, Srid, Akshay, additional, Sader, Kasim, additional, Radjainia, Mazdak, additional, Qian, Pu, additional, Castro-Hartmann, Pablo, additional, Venkaya, Shayla, additional, Singh, Nanki Kaur, additional, McKinley, Gavin, additional, Fernandez-Cid, Alejandra, additional, Mukhopadhyay, Shubhashish, additional, Burgess-Brown, Nicola, additional, Delemotte, Lucie, additional, Covarrubias, Manuel, additional, and Duerr, Katharina, additional

Published
2021
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16. Structural and mechanistic insights into Mcm2-7 double-hexamer assembly and function.

Author

Jingchuan Sun, Fernandez-Cid, Alejandra, Riera, Alberto, Tognetti, Silvia, Zuanning Yuan, Stillman, Bruce, Speck, Christian, and Huilin Li

Subjects
*MINICHROMOSOME maintenance proteins, *DNA replication, *DNA helicases, *CELL cycle regulation, *MOLECULAR structure, *ORIGIN recognition complex
Abstract

Eukaryotic cells license each DNA replication origin during G1 phase by assembling a prereplication complex that contains a Mcm2-7 (minichromosome maintenance proteins 2-7) double hexamer. During S phase, each Mcm2-7 hexamer forms the core of a replicative DNA helicase. However, the mechanisms of origin licensing and helicase activation are poorly understood. The helicase loaders ORC-Cdc6 function to recruit a single Cdt1-Mcm2-7 heptamer to replication origins prior to Cdt1 release and ORC-Cdc6-Mcm2-7 complex formation, but how the second Mcm2-7 hexamer is recruited to promote double-hexamer formation is not well understood. Here, structural evidence for intermediates consisting of an ORC-Cdc6-Mcm2-7 complex and an ORC-Cdc6-Mcm2- 7-Mcm2-7 complex are reported, which together provide new insights into DNA licensing. Detailed structural analysis of the loaded Mcm2-7 double-hexamer complex demonstrates that the two hexamers are interlocked and misaligned along the DNA axis and lack ATP hydrolysis activity that is essential for DNA helicase activity. Moreover, we show that the head-to-head juxtaposition of the Mcm2-7 double hexamer generates a new protein interaction surface that creates a multisubunit-binding site for an S-phase protein kinase that is known to activate DNA replication. The data suggest how the double hexamer is assembled and how helicase activity is regulated during DNA licensing, with implications for cell cycle control of DNA replication and genome stability. [ABSTRACT FROM AUTHOR]

Published
2014
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17. Screening and Production of Recombinant Human Proteins: Protein Production in Insect Cells.

Author

Mahajan P, Strain-Damerell C, Mukhopadhyay S, Fernandez-Cid A, Gileadi O, and Burgess-Brown NA

Subjects
Animals, Humans, Recombinant Proteins biosynthesis, Recombinant Proteins genetics, Sf9 Cells, Spodoptera, Baculoviridae genetics, Genetic Vectors genetics, Membrane Proteins biosynthesis, Membrane Proteins genetics
Abstract

This chapter describes the step-by-step methods employed by the Structural Genomics Consortium (SGC) for screening and producing proteins in the baculovirus expression vector system (BEVS). This eukaryotic expression system was selected and a screening process established in 2007 as a measure to tackle the more challenging kinase, RNA-DNA processing, and integral membrane protein families on our target list. Here, we discuss our platform for identifying soluble proteins from 3 mL of insect cell culture and describe the procedures involved in producing protein from liter-scale cultures.

Published
2021
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18. Screening and Production of Recombinant Human Proteins: Ligation-Independent Cloning.

Author

Strain-Damerell C, Mahajan P, Fernandez-Cid A, Gileadi O, and Burgess-Brown NA

Subjects
Humans, Baculoviridae genetics, Cloning, Molecular, Escherichia coli genetics, Escherichia coli metabolism, Gene Expression, Genetic Vectors genetics, Recombinant Proteins biosynthesis, Recombinant Proteins genetics
Abstract

Structural genomics groups have identified the need to generate multiple truncated versions of each target to improve their success in producing a well-expressed, soluble, and stable protein and one that crystallizes and diffracts to a sufficient resolution for structural determination. At the Structural Genomics Consortium, we opted for the ligation-independent cloning (LIC) method which provides the throughput we desire to produce and screen many proteins in a parallel process. Here, we describe our LIC protocol for generating constructs in 96-well format and provide a choice of vectors suitable for expressing proteins in both E. coli and the baculovirus expression vector system (BEVS).

Published
2021
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19. Screening and Production of Recombinant Human Proteins: Protein Production in E. coli.

Author

Burgess-Brown NA, Mahajan P, Strain-Damerell C, Fernandez-Cid A, Gileadi O, and Gräslund S

Subjects
Humans, Chromatography, Affinity, Chromatography, Gel, Escherichia coli genetics, Escherichia coli metabolism, Recombinant Proteins biosynthesis, Recombinant Proteins genetics, Recombinant Proteins isolation & purification
Abstract

In Chapter 3 , we described the Structural Genomics Consortium (SGC) process for generating multiple constructs of truncated versions of each protein using LIC. In this chapter we provide a step-by-step procedure of our E. coli system for test expressing intracellular (soluble) proteins in a 96-well format that enables us to identify which proteins or truncated versions are expressed in a soluble and stable form suitable for structural studies. In addition, we detail the process for scaling up cultures for large-scale protein purification. This level of production is required to obtain sufficient quantities (i.e., milligram amounts) of protein for further characterization and/or structural studies (e.g., crystallization or cryo-EM experiments). Our standard process is purification by immobilized metal affinity chromatography (IMAC) using nickel resin followed by size exclusion chromatography (SEC), with additional procedures arising from the complexity of the protein itself.

Published
2021
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20. Expression Screening of Human Integral Membrane Proteins Using BacMam.

Author

Mahajan P, Ellis K, Mukhopadhyay S, Fernandez-Cid A, Chi G, Man H, Dürr KL, and Burgess-Brown NA

Subjects
HEK293 Cells, Humans, Recombinant Proteins biosynthesis, Recombinant Proteins genetics, Gene Expression, Genetic Vectors genetics, Membrane Proteins biosynthesis, Membrane Proteins genetics
Abstract

This chapter describes the step-by-step methods employed by the Structural Genomics Consortium (SGC) for screening and producing proteins in the BacMam system. This eukaryotic expression system was selected and a screening process established in 2016 to enable production of highly challenging human integral membrane proteins (IMPs), which are a significant component of our target list. Here, we discuss our recently developed platform for identifying expression and monodispersity of IMPs from 3 mL of HEK293 cells.

Published
2021
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