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pro vyhledávání: '"Susana Vázquez Torres"'
Autor:
Susana Vázquez Torres, Philip J. Y. Leung, Isaac D. Lutz, Preetham Venkatesh, Joseph L. Watson, Fabian Hink, Huu-Hien Huynh, Andy Hsien-Wei Yeh, David Juergens, Nathaniel R. Bennett, Andrew N. Hoofnagle, Eric Huang, Michael J MacCoss, Marc Expòsit, Gyu Rie Lee, Paul M. Levine, Xinting Li, Mila Lamb, Elif Nihal Korkmaz, Jeff Nivala, Lance Stewart, Joseph M. Rogers, David Baker
Many peptide hormones form an alpha-helix upon binding their receptors1–4, and sensitive detection methods for them could contribute to better clinical management.De novoprotein design can now generate binders with high affinity and specificity to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a1f71e8af52449b591ee281d1a65d41b
https://doi.org/10.1101/2022.12.10.519862
https://doi.org/10.1101/2022.12.10.519862
Autor:
Joseph L. Watson, David Juergens, Nathaniel R. Bennett, Brian L. Trippe, Jason Yim, Helen E. Eisenach, Woody Ahern, Andrew J. Borst, Robert J. Ragotte, Lukas F. Milles, Basile I. M. Wicky, Nikita Hanikel, Samuel J. Pellock, Alexis Courbet, William Sheffler, Jue Wang, Preetham Venkatesh, Isaac Sappington, Susana Vázquez Torres, Anna Lauko, Valentin De Bortoli, Emile Mathieu, Regina Barzilay, Tommi S. Jaakkola, Frank DiMaio, Minkyung Baek, David Baker
There has been considerable recent progress in designing new proteins using deep learning methods1–9. Despite this progress, a general deep learning framework for protein design that enables solution of a wide range of design challenges, includingd
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::33b3dc2111101afaf7ffd55bbbc5fd12
https://doi.org/10.1101/2022.12.09.519842
https://doi.org/10.1101/2022.12.09.519842
Publikováno v:
Protein Engineering, Design & Selection, 32(12), 555-564
Staphylococcus aureus sortase A (SaSrtA) is an enzyme that anchors proteins to the cell surface of Gram-positive bacteria. During the transpeptidation reaction performed by SaSrtA, proteins containing an N-terminal glycine can be covalently linked to