Výsledky vyhledávání - Mertens, Haydyn D.T.
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Did evolution create a flexible ligand-binding cavity in the urokinase receptor through deletion of a plesiotypic disulfide bond? Autor Leth, Julie M., Mertens, Haydyn D. T., Leth-Espensen, Katrine Zinck, Jørgensen, Thomas J. D., Ploug, Michael
Vydáno 2019Text -
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A Flexible Multidomain Structure Drives the Function of the Urokinase-type Plasminogen Activator Receptor (uPAR) Autor Mertens, Haydyn D. T., Kjaergaard, Magnus, Mysling, Simon, Gårdsvoll, Henrik, Jørgensen, Thomas J. D., Svergun, Dmitri I., Ploug, Michael
Vydáno 2012Text -
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Structural role of essential light chains in the apicomplexan glideosome Autor Pazicky, Samuel, Dhamotharan, Karthikeyan, Kaszuba, Karol, Mertens, Haydyn D. T., Gilberger, Tim, Svergun, Dmitri, Kosinski, Jan, Weininger, Ulrich, Löw, Christian
Vydáno 2020Text -
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Epsin and Sla2 form assemblies through phospholipid interfaces Autor Garcia-Alai, Maria M., Heidemann, Johannes, Skruzny, Michal, Gieras, Anna, Mertens, Haydyn D. T., Svergun, Dmitri I., Kaksonen, Marko, Uetrecht, Charlotte, Meijers, Rob
Vydáno 2018Text -
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Structure of full-length wild-type human phenylalanine hydroxylase by small angle X-ray scattering reveals substrate-induced conformational stability Autor Tomé, Catarina S., Lopes, Raquel R., Sousa, Pedro M. F., Amaro, Mariana P., Leandro, João, Mertens, Haydyn D. T., Leandro, Paula, Vicente, João B.
Vydáno 2019Text -
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Author Correction: Structure of full-length wild-type human phenylalanine hydroxylase by small angle X-ray scattering reveals substrate-induced conformational stability Autor Tomé, Catarina S., Lopes, Raquel R., Sousa, Pedro M. F., Amaro, Mariana P., Leandro, João, Mertens, Haydyn D. T., Leandro, Paula, Vicente, João B.
Vydáno 2019Text -
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Structural Basis for Draxin-Modulated Axon Guidance and Fasciculation by Netrin-1 through DCC Autor Liu, Ying, Bhowmick, Tuhin, Liu, Yiqiong, Gao, Xuefan, Mertens, Haydyn D.T., Svergun, Dmitri I., Xiao, Junyu, Zhang, Yan, Wang, Jia-huai, Meijers, Rob
Vydáno 2018Text -
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Conformational flexibility of EptA driven by an interdomain helix provides insights for enzyme–substrate recognition Autor Anandan, Anandhi, Dunstan, Nicholas W., Ryan, Timothy M., Mertens, Haydyn D. T., Lim, Katherine Y. L., Evans, Genevieve L., Kahler, Charlene M., Vrielink, Alice
Vydáno 2021Text -
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Solution Structure of CCP Modules 10–12 Illuminates Functional Architecture of the Complement Regulator, Factor H Autor Makou, Elisavet, Mertens, Haydyn D.T., Maciejewski, Mateusz, Soares, Dinesh C., Matis, Ilias, Schmidt, Christoph Q., Herbert, Andrew P., Svergun, Dmitri I., Barlow, Paul N.
Vydáno 2012Text