Zobrazeno 1 - 10
of 20
pro vyhledávání: '"Alexis Courbet"'
Autor:
Yang Hsia, Rubul Mout, William Sheffler, Natasha I. Edman, Ivan Vulovic, Young-Jun Park, Rachel L. Redler, Matthew J. Bick, Asim K. Bera, Alexis Courbet, Alex Kang, T. J. Brunette, Una Nattermann, Evelyn Tsai, Ayesha Saleem, Cameron M. Chow, Damian Ekiert, Gira Bhabha, David Veesler, David Baker
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-10 (2021)
De novo design of self-assembling protein nanostructures and materials is of significant interest, however design of complex, multi-component assemblies is challenging. Here, the authors present a stepwise hierarchical approach to build such assembli
Externí odkaz:
https://doaj.org/article/8bb80e33cedb4e58856a97a798a217fd
Publikováno v:
EMBO Molecular Medicine, Vol 8, Iss 9, Pp 987-991 (2016)
The promise for real precision medicine is contingent on innovative technological solutions to diagnosis and therapy. In the post‐genomic era, rational and systematic approaches to biological design could provide new ways to dynamically probe, moni
Externí odkaz:
https://doaj.org/article/a7fba3e7cd12490d9eb38a390bc93e0c
Autor:
Alexis Courbet, Nicole Bec, Caroline Constant, Christian Larroque, Martine Pugniere, Safia El Messaoudi, Zahraa Zghaib, Sonia Khier, Carine Deleuze-Masquefa, Florence Gattacceca
Publikováno v:
PLoS ONE, Vol 12, Iss 8, p e0182022 (2017)
Displaying a strong antiproliferative activity on a wide variety of cancer cells, EAPB0203 and EAPB0503 belong to the imidazo[1,2-a]quinoxalines family of imiquimod structural analogues. EAPB0503 has been shown to inhibit tubulin polymerization. The
Externí odkaz:
https://doaj.org/article/4641e264c43e45a79d28c8192d42093a
Autor:
Isaac D. Lutz, Shunzhi Wang, Christoffer Norn, Alexis Courbet, Andrew J. Borst, Yan Ting Zhao, Annie Dosey, Longxing Cao, Jinwei Xu, Elizabeth M. Leaf, Catherine Treichel, Patrisia Litvicov, Zhe Li, Alexander D. Goodson, Paula Rivera-Sánchez, Ana-Maria Bratovianu, Minkyung Baek, Neil P. King, Hannele Ruohola-Baker, David Baker
Publikováno v:
Science. 380:266-273
As a result of evolutionary selection, the subunits of naturally occurring protein assemblies often fit together with substantial shape complementarity to generate architectures optimal for function in a manner not achievable by current design approa
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
Autor:
Zhe Li, Shunzhi Wang, Una Nattermann, Asim K. Bera, Andrew J. Borst, Matthew J. Bick, Erin C. Yang, William Sheffler, Byeongdu Lee, Soenke Seifert, Hannah Nguyen, Alex Kang, Radhika Dalal, Joshua M. Lubner, Yang Hsia, Hugh Haddox, Alexis Courbet, Quinton Dowling, Marcos Miranda, Andrew Favor, Ali Etemadi, Natasha I. Edman, Wei Yang, Banumathi Sankaran, Babak Negahdari, David Baker
SummaryProtein crystallization plays a central role in structural biology1, with broad impact2in pharmaceutical formulation3, drug delivery4, biosensing5, and biocatalysis6,7. Despite this importance, the process of protein crystallization remains po
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::97c9e49b9bf954ca7ba67cff48a16384
https://doi.org/10.1101/2022.11.18.517014
https://doi.org/10.1101/2022.11.18.517014
Autor:
Linna An, Derrick R Hicks, Dmitri Zorine, Justas Dauparas, Basile I. M. Wicky, Lukas F. Milles, Alexis Courbet, Asim K. Bera, Hannah Nguyen, Alex Kang, Lauren Carter, David Baker
In pseudocyclic proteins such as TIM barrels, β barrels, and some helical transmembrane channels, a single subunit is repeated in a cyclic pattern, giving rise to a central cavity which can serve as a pocket for ligand binding or enzymatic activity.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::65fa9895ece579b995a6f26482e5c841
https://doi.org/10.1101/2022.09.01.506251
https://doi.org/10.1101/2022.09.01.506251
Autor:
Danny D. Sahtoe, Florian Praetorius, Alexis Courbet, Yang Hsia, Basile I. M. Wicky, Natasha I. Edman, Lauren M. Miller, Bart J. R. Timmermans, Justin Decarreau, Hana M. Morris, Alex Kang, Asim K. Bera, David Baker
Publikováno v:
Science. 375
Asymmetric multiprotein complexes that undergo subunit exchange play central roles in biology but present a challenge for design because the components must not only contain interfaces that enable reversible association but also be stable and well be
Autor:
Joel Quispe, David Veesler, Philip Bradley, Scott E. Boyken, David Baker, Una Nattermann, William Sheffler, D. Nagarajan, George Ueda, Alexis Courbet, Young-Jun Park, Justin M. Kollman, J. P. Hansen, Bethel Np, Daniel-Adriano Silva, Adam Moyer, Chunfu Xu, Yang Hsia, Neil P. King
Natural nanomachines like the F1/F0-ATPase contain protein components that undergo rotation relative to each other. Designing such mechanically constrained nanoscale protein architectures with internal degrees of freedom is an outstanding challenge f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::d1980c347129ed6f10ca632fa616b536
https://doi.org/10.1101/2021.11.11.468255
https://doi.org/10.1101/2021.11.11.468255
Autor:
Lauren Miller, David Baker, Natasha I. Edman, Bart J. R. Timmermans, Basile I. M. Wicky, Asim K. Bera, Danny D. Sahtoe, Hana M. Morris, Florian Praetorius, Alexis Courbet, Yang Hsia, Alex Kang
Asymmetric multi-protein complexes that undergo subunit exchange play central roles in biology, but present a challenge for protein design. The individual components must contain interfaces enabling reversible addition to and dissociation from the co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::45fc92d25d4e26880d05c7f103e50a0c
https://doi.org/10.1101/2021.08.15.456388
https://doi.org/10.1101/2021.08.15.456388