Search

Your search keyword '"Mok, Yee-Foong"' showing total 147 results
Start Over Author "Mok, Yee-Foong"
147 results on '"Mok, Yee-Foong"'

1. Freezing and Melting Hysteresis Measurements in Solutions of Hyperactive Antifreeze Protein from an Antarctic Bacteria

Author

Celik, Yeliz, Drori, Ran, Graham, Laurie, Mok, Yee-Foong, Davies, Peter L., and Braslavsky, Ido

Subjects
Condensed Matter - Soft Condensed Matter, Condensed Matter - Materials Science, Physics - Biological Physics
Abstract

Antifreeze proteins (AFPs) evolved in cold-adapted organisms and serve to protect them against freezing in cold conditions by arresting ice crystal growth. Recently, we have shown quantitatively that adsorption of AFPs not only prevents ice from growing but also from melting. This melting inhibition by AFPs, which results in superheated ice (Celik et al, PNAS 2010), is not a well-known phenomenon. Here we present our recent findings in which the Ca2+ - dependent hyperactive AFP from Marinomonas primoryensis (MpAFP) clearly displays this property. Additionally, we found that an ice crystal that is initially stabilized and protected by this type of AFP can be overgrown and then melted back to the original crystal. This repeatable process is likely due to melting inhibition, and supports the idea that AFPs bind irreversibly to ice surfaces., Comment: 7 pages, 5 figures

Published
2012

2. Transferrin receptor 1 is a reticulocyte-specific receptor for Plasmodium vivax

Author

Gruszczyk, Jakub, Kanjee, Usheer, Chan, Li-Jin, Menant, Sébastien, Malleret, Benoit, Lim, Nicholas T. Y., Schmidt, Christoph Q., Mok, Yee-Foong, Lin, Kai-Min, Pearson, Richard D., Rangel, Gabriel, Smith, Brian J., Call, Melissa J., Weekes, Michael P., Griffin, Michael D. W., Murphy, James M., Abraham, Jonathan, Sriprawat, Kanlaya, Menezes, Maria J., Ferreira, Marcelo U., Russell, Bruce, Renia, Laurent, Duraisingh, Manoj T., and Tham, Wai-Hong

Published
2018

5. Cryo-EM structure of an essential Plasmodium vivax invasion complex

Author

Gruszczyk, Jakub, Huang, Rick K., Chan, Li-Jin, Menant, Sébastien, Hong, Chuan, Murphy, James M., and Mok, Yee-Foong

Subjects
Protein binding -- Models, Monoclonal antibodies -- Models, Malaria -- Physiological aspects, Plasmodium vivax -- Physiological aspects, Antigens, Plasmodium falciparum, Medical research, Antibodies, Microscopy, Transferrin, Housekeeping, Electron microscopy, Antigenic determinants, Novels, Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Plasmodium vivax is the most widely distributed malaria parasite that infects humans.sup.1. P. vivax invades reticulocytes exclusively, and successful entry depends on specific interactions between the P. vivax reticulocyte-binding protein 2b (PvRBP2b) and transferrin receptor 1 (TfR1).sup.2. TfR1-deficient erythroid cells are refractory to invasion by P. vivax, and anti-PvRBP2b monoclonal antibodies inhibit reticulocyte binding and block P. vivax invasion in field isolates.sup.2. Here we report a high-resolution cryo-electron microscopy structure of a ternary complex of PvRBP2b bound to human TfR1 and transferrin, at 3.7 Å resolution. Mutational analyses show that PvRBP2b residues involved in complex formation are conserved; this suggests that antigens could be designed that act across P. vivax strains. Functional analyses of TfR1 highlight how P. vivax hijacks TfR1, an essential housekeeping protein, by binding to sites that govern host specificity, without affecting its cellular function of transporting iron. Crystal and solution structures of PvRBP2b in complex with antibody fragments characterize the inhibitory epitopes. Our results establish a structural framework for understanding how P. vivax reticulocyte-binding protein engages its receptor and the molecular mechanism of inhibitory monoclonal antibodies, providing important information for the design of novel vaccine candidates. Structural studies show that conserved residues in Plasmodium vivax reticulocyte-binding protein 2b determine interactions with transferrin receptor 1 that are essential for host invasion, suggesting avenues for designing vaccines that work across P. vivax strains., Author(s): Jakub Gruszczyk [sup.1] , Rick K. Huang [sup.2] , Li-Jin Chan [sup.1] [sup.3] , Sébastien Menant [sup.1] , Chuan Hong [sup.2] , James M. Murphy [sup.1] [sup.3] , Yee-Foong [...]

Published
2018
Full Text
View/download PDF

12. Structural Insights into the Unique Modes of Relaxin-Binding and Tethered-Agonist Mediated Activation of RXFP1 and RXFP2

Author

Sethi, Ashish, primary, Bruell, Shoni, additional, Ryan, Tim, additional, Yan, Fei, additional, Tanipour, Mohammad Hossein, additional, Mok, Yee-Foong, additional, Draper-Joyce, Chris, additional, Khandokar, Yogesh, additional, Metcalfe, Riley D., additional, Griffin, Michael D.W., additional, Scott, Daniel J., additional, Hossain, Mohammad Akhter, additional, Petrie, Emma J., additional, Bathgate, Ross A.D., additional, and Gooley, Paul R., additional

Published
2021
Full Text
View/download PDF

15. Structural insights into the modes of relaxin-binding and tethered-agonist activation of RXFP1 and RXFP2

Author

Sethi, Ashish, primary, Bruell, Shoni, additional, Ryan, Tim, additional, Yan, Fei, additional, Tanipour, Mohammad, additional, Mok, Yee-Foong, additional, Draper-Joyce, Chris, additional, Khandokar, Yogesh, additional, Metcalfe, Riley D., additional, Griffin, Michael D. W., additional, Scott, Daniel J., additional, Hossain, Mohammad Akhter, additional, Petrie, Emma J., additional, Bathgate, Ross A. D., additional, and Gooley, Paul R., additional

Published
2021
Full Text
View/download PDF

16. Contributors

Author

Aguilar, Marie-Isabel, primary, Andreasen, Maria, additional, Anthony, Neil R., additional, Teran Arce, Fernando, additional, Arnhold, Florian, additional, Arya, Shruti, additional, Attar, Aida, additional, Barbosa, Silvia, additional, Behrens, Manja A., additional, Bekard, Innocent B., additional, Belfort, Georges, additional, Bennink, Martin L., additional, Bereza, Magdalena, additional, Berland, Keith M., additional, Bitan, Gal, additional, Bonn, Mischa, additional, Botelho, Hugo M., additional, Branco dos Santos, Joana, additional, Breydo, Leonid, additional, Cao, Yi, additional, Cappai, Roberto, additional, Cardoso, Isabel, additional, Carrión-Vázquez, Mariano, additional, Carvalho, Sofia B., additional, Carver, John A., additional, Chan, Fiona T.S., additional, Childers, W. Seth, additional, Collins, Jason C., additional, Connelly, Laura, additional, Curtain, Cyril, additional, Dalal, Vijit, additional, De Simone, Alfonso, additional, Donald, Athene M., additional, Dunstan, Dave E., additional, Ecroyd, Heath, additional, Enghild, Jan Johannes, additional, Abelleira, Laura Esther, additional, Fändrich, Marcus, additional, Fernández-Ramírez, María del Carmen, additional, Foderà, Vito, additional, Fritz, Günter, additional, Furukawa, Yoshiaki, additional, Ghodke, Shirin D., additional, Gianni, Stefano, additional, Giese, Armin, additional, Gomes, Cláudio M., additional, Gonçalves, Susana, additional, Greene, Lesley H., additional, Griffin, Michael D.W., additional, Griggs, Amy M., additional, Haass, Christian, additional, Hammarström, Per, additional, Harris, J. Robin, additional, Herrera, Federico, additional, Hervás, Rubén, additional, Hill, Shannon E., additional, Hou, Xu, additional, Howlett, Geoffrey J., additional, Ikezu, Tsuneya, additional, Jang, Hyunbum, additional, Jensen, Grethe V., additional, Kagan, Bruce L., additional, Kaminski, Clemens F., additional, Kawai-Noma, Shigeko, additional, Klechikov, Alexei, additional, Koenderink, Gijsje H., additional, Lal, Ratnesh, additional, Laurents, Douglas V., additional, Le Lan Pham, Chi, additional, LeVine, Harry, additional, Losic, Dusan, additional, Lynn, David G., additional, Malmos, Kirsten G., additional, Martin, Lisandra L., additional, Mechler, Adam I., additional, Mehta, Anil K., additional, Meral, Derya, additional, Milton, Nathaniel G.N., additional, Mok, Yee-Foong, additional, Morozova-Roche, Ludmilla A., additional, Mosquera, Víctor, additional, Mukhopadhyay, Samrat, additional, Mulaj, Mentor, additional, Muschol, Martin, additional, Nielsen, Niels Chr, additional, Nilsson, R., additional, Nübling, Georg, additional, Nussinov, Ruth, additional, Otzen, Daniel E., additional, Outeiro, Tiago Fleming, additional, Pedersen, Jan Skov, additional, Pedersen, Jesper Søndergaard, additional, Peter, K., additional, Pinotsi, Dorothea, additional, Qin, Meng, additional, Ramachandran, Srinivasan, additional, Rekas, Agata, additional, Relini, Annalisa, additional, Rochet, Jean-Christophe, additional, Rothhämel, Sophie, additional, Rudinskiy, Nikita, additional, Sauer, Markus, additional, Kaminski Schierle, Gabriele S., additional, Schleeger, Michael, additional, Schmid, Bettina, additional, Small, David H., additional, Søndergaard, Anne, additional, Sorci, Mirco, additional, Spires-Jones, Tara L., additional, Stenvang, Marcel, additional, Stöckl, Martin, additional, Strecker, Katrin, additional, Subramaniam, Vinod, additional, Svane, Anna S.P., additional, Sweers, Kim K.M., additional, Taboada, Pablo, additional, Taguchi, Hideki, additional, Teoh, Chai Lean, additional, Thorn, David C., additional, Tokuraku, Kiyotaka, additional, Tycko, Robert, additional, Urbanc, Brigita, additional, Uversky, Vladimir N., additional, van den Akker, Corianne C., additional, Vendruscolo, Michele, additional, von Mikecz, Anna, additional, Vukojević, Vladana, additional, Wang, Wei, additional, Weise, Katrin, additional, Winter, Roland, additional, Wu, Jessica W., additional, Xue, Wei-Feng, additional, Yanamandra, Kiran, additional, Ysselstein, Daniel, additional, Žerovnik, Eva, additional, and Zou, Dawei, additional

Published
2014
Full Text
View/download PDF

23. Structural Elucidation of Viral Antagonism of Innate Immunity at the STAT1 Interface

Author

Hossain, Md. Alamgir, primary, Larrous, Florence, additional, Rawlinson, Stephen M., additional, Zhan, Jingyu, additional, Sethi, Ashish, additional, Ibrahim, Youssef, additional, Aloi, Maria, additional, Lieu, Kim G., additional, Mok, Yee-Foong, additional, Griffin, Michael D.W., additional, Ito, Naoto, additional, Ose, Toyoyuki, additional, Bourhy, Hervé, additional, Moseley, Gregory W., additional, and Gooley, Paul R., additional

Published
2019
Full Text
View/download PDF

25. Structural elucidation of viral antagonism of innate immunity: the STAT1 interface

Author

Moseley, Gregory W., primary, Hossain, Alamgir, additional, Larrous, Florence, additional, Zhan, Jingyu, additional, Sethi, Ashish, additional, Ibrahim, Youssef, additional, Aloi, Maria, additional, Rawlinson, Stephen M., additional, Lieu, Kim G., additional, Mok, Yee-Foong, additional, Griffin, Michael D. W., additional, Ito, Naoto, additional, Ose, Toyoyuki, additional, Bourhy, Hervé, additional, and Gooley, Paul R., additional

Published
2019
Full Text
View/download PDF

29. A Multilaboratory Comparison of Calibration Accuracy and the Performance of External References in Analytical Ultracentrifugation

Author

Zhao, Huaying, Ghirlando, Rodolfo, Alfonso, Carlos, Arisaka, Fumio, Attali, Ilan, Bain, David L., Bakhtina, Marina M., Becker, Donald F., Bedwell, Gregory J., Bekdemir, Ahmet, Besong, Tabot M.D., Birck, Catherine, Brautigam, Chad A., Brennerman, William, Byron, Olwyn, Bzowska, Agnieszka, Chaires, Jonathan B., Chaton, Catherine T., Connaghan, Keith D., Crowley, Kimberly A., Curth, Ute, Daviter, Tina, Dean, William L., Ebel, Christine, Eckert, Debra M., Eisele, Leslie E., Eisenstein, Edward, England, Patrick, Escalante, Carlos, Fagan, Jeffrey A., Fairman, Robert, Finn, Ron M., Fischle, Wolfgang, Gor, Jayesh, Gustafsson, Henning, Hall, Damien, Harding, Stephen E., Herr, Andrew B., Howell, Elizabeth E., Isaac, Richard S., Jao, Shu-Chuan, Jose, Davis, Kim, Soon-Jong, Kokona, Bashkim, Kornblatt, Jack A., Kosek, Dalibor, Krayukhina, Elena, Krzizike, Daniel, Kusznir, Eric A., Kwon, Hyewon, Larson, Adam, Laue, Thomas M., Le Roy, Aline, Leech, Andrew P., Lilie, Hauke, Luger, Karolin, Luque-Ortega, Juan R., Ma, Jia, May, Carrie A., Maynard, Ernest L., Modrak-Wojcik, Anna, Mok, Yee-Foong, Nagel-Steger, Luitgard, Narlikar, Geeta J., Noda, Masanori, Nourse, Amanda, Obsil, Tomas, Park, Chad K., Park, Jin-Ku, Pawelek, Peter D., Perdue, Erby E., Perkins, Stephen J., Perugini, Matthew A., Peterson, Craig L., Peverelli, Martin G., Piszczek, Grzegorz, Prag, Gali, Prevelige, Peter E., Raynal, Bertrand D.E., Rezabkova, Lenka, Richter, Klaus, Ringel, Alison E., Rosenberg, Rose, Rowe, Arthur J., Rufer, Arne C., Scott, David J., Seravalli, Javier G., Solovyova, Alexandra S., Song, Renjie, Staunton, David, Stoddard, Caitlin, Stott, Katherine, Strauss, Holger M., Streicher, Werner W., Sumida, John P., Swygert, Sarah G., Szczepanowski, Roman H., Tessmer, Ingrid, Toth, Ronald T., Tripathy, Ashutosh, Uchiyama, Susumu, Uebel, Stephan F.W., Unzai, Satoru, Gruber, Anna Vitlin, von Hippel, Peter H., Wandrey, Christine, Wang, Szu-Huan, Weitzel, Steven E., Wielgus-Kutrowska, Beata, Wolberger, Cynthia, Wolff, Martin, Wright, Edward, Wu, Yu-Sung, Wubben, Jacinta M., and Schuck, Peter

Abstract

Analytical ultracentrifugation (AUC) is a first principles based method to determine absolute sedimentation coefficients and buoyant molar masses of macromolecules and their complexes, reporting on their size and shape in free solution. The purpose of this multi-laboratory study was to establish the precision and accuracy of basic data dimensions in AUC and validate previously proposed calibration techniques. Three kits of AUC cell assemblies containing radial and temperature calibration tools and a bovine serum albumin (BSA) reference sample were shared among 67 laboratories, generating 129 comprehensive data sets. These allowed for an assessment of many parameters of instrument performance, including accuracy of the reported scan time after the start of centrifugation, the accuracy of the temperature calibration, and the accuracy of the radial magnification. The range of sedimentation coefficients obtained for BSA monomer in different instruments and using different optical systems was from 3.655 S to 4.949 S, with a mean and standard deviation of (4.304 ± 0.188) S (4.4%). After the combined application of correction factors derived from the external calibration references for elapsed time, scan velocity, temperature, and radial magnification, the range of s-values was reduced 7-fold with a mean of 4.325 S and a 6-fold reduced standard deviation of ± 0.030 S (0.7%). In addition, the large data set provided an opportunity to determine the instrument-to-instrument variation of the absolute radial positions reported in the scan files, the precision of photometric or refractometric signal magnitudes, and the precision of the calculated apparent molar mass of BSA monomer and the fraction of BSA dimers. These results highlight the necessity and effectiveness of independent calibration of basic AUC data dimensions for reliable quantitative studies.

Published
2015

31. Structurally conserved erythrocyte-binding domain in Plasmodium provides a versatile scaffold for alternate receptor engagement

Author

Gruszczyk, Jakub, primary, Lim, Nicholas T. Y., additional, Arnott, Alicia, additional, He, Wen-Qiang, additional, Nguitragool, Wang, additional, Roobsoong, Wanlapa, additional, Mok, Yee-Foong, additional, Murphy, James M., additional, Smith, Katherine R., additional, Lee, Stuart, additional, Bahlo, Melanie, additional, Mueller, Ivo, additional, Barry, Alyssa E., additional, and Tham, Wai-Hong, additional

Published
2015
Full Text
View/download PDF

35. Cryo-EM structure of an essential Plasmodium vivaxinvasion complex

Author

Gruszczyk, Jakub, Huang, Rick, Chan, Li-Jin, Menant, Sébastien, Hong, Chuan, Murphy, James, Mok, Yee-Foong, Griffin, Michael, Pearson, Richard, Wong, Wilson, Cowman, Alan, Yu, Zhiheng, and Tham, Wai-Hong

Abstract

Plasmodium vivaxis the most widely distributed malaria parasite that infects humans1. P. vivaxinvades reticulocytes exclusively, and successful entry depends on specific interactions between the P. vivaxreticulocyte-binding protein 2b (PvRBP2b) and transferrin receptor 1 (TfR1)2. TfR1-deficient erythroid cells are refractory to invasion by P. vivax, and anti-PvRBP2b monoclonal antibodies inhibit reticulocyte binding and block P. vivaxinvasion in field isolates2. Here we report a high-resolution cryo-electron microscopy structure of a ternary complex of PvRBP2b bound to human TfR1 and transferrin, at 3.7 Å resolution. Mutational analyses show that PvRBP2b residues involved in complex formation are conserved; this suggests that antigens could be designed that act across P. vivaxstrains. Functional analyses of TfR1 highlight how P. vivaxhijacks TfR1, an essential housekeeping protein, by binding to sites that govern host specificity, without affecting its cellular function of transporting iron. Crystal and solution structures of PvRBP2b in complex with antibody fragments characterize the inhibitory epitopes. Our results establish a structural framework for understanding how P. vivaxreticulocyte-binding protein engages its receptor and the molecular mechanism of inhibitory monoclonal antibodies, providing important information for the design of novel vaccine candidates. Structural studies show that conserved residues in Plasmodium vivaxreticulocyte-binding protein 2b determine interactions with transferrin receptor 1 that are essential for host invasion, suggesting avenues for designing vaccines that work across P. vivaxstrains.

Published
2018
Full Text
View/download PDF

44. Recognition and Detoxification of the Insecticide DDT by Drosophila melanogaster Glutathione S-Transferase D1

Author

Low, Wai Yee, primary, Feil, Susanne C., additional, Ng, Hooi Ling, additional, Gorman, Michael A., additional, Morton, Craig J., additional, Pyke, James, additional, McConville, Malcolm J., additional, Bieri, Michael, additional, Mok, Yee-Foong, additional, Robin, Charles, additional, Gooley, Paul R., additional, Parker, Michael W., additional, and Batterham, Philip, additional

Published
2010
Full Text
View/download PDF

46. Thioflavin T fluorescence in human serum: Correlations with vascular health and cardiovascular risk factors

Author

Griffin, Michael D.W., primary, Wilson, Leanne M., additional, Mok, Yee-Foong, additional, Januszewski, Andrzej S., additional, Wilson, Andrew M., additional, Karschimkus, Connie S., additional, Romas, Evange, additional, Lee, Allan B., additional, Godfrey, Tim, additional, Wong, Melinda, additional, Clemens, Laurence, additional, Jenkins, Alicia J., additional, and Howlett, Geoffrey J., additional

Published
2010
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results