Zobrazeno 1 - 10
of 341
pro vyhledávání: '"G. Sgourakis"'
Autor:
Andrew C. McShan, David Flores-Solis, Yi Sun, Samuel E. Garfinkle, Jugmohit S. Toor, Michael C. Young, Nikolaos G. Sgourakis
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-19 (2023)
Abstract The conformational landscapes of peptide/human leucocyte antigen (pHLA) protein complexes encompassing tumor neoantigens provide a rationale for target selection towards autologous T cell, vaccine, and antibody-based therapeutic modalities.
Externí odkaz:
https://doaj.org/article/3d091fa11d8640f789c98250daa34e87
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-13 (2023)
Abstract The class I proteins of the major histocompatibility complex (MHC-I) display epitopic peptides derived from endogenous proteins on the cell surface for immune surveillance. Accurate modeling of peptides bound to the human MHC, HLA, has been
Externí odkaz:
https://doaj.org/article/e05b9ea7d65d4b9e8b5486e25b3a7ba8
Autor:
Jiansheng Jiang, Daniel K. Taylor, Ellen J. Kim, Lisa F. Boyd, Javeed Ahmad, Michael G. Mage, Hau V. Truong, Claire H. Woodward, Nikolaos G. Sgourakis, Peter Cresswell, David H. Margulies, Kannan Natarajan
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-13 (2022)
The catalytic chaperone tapasin assists peptide loading onto MHC-I molecules for antigen presentation and immune recognition. Here, the authors present crystal structures that provide insights into the molecular mechanism of tapasin-mediated peptide
Externí odkaz:
https://doaj.org/article/c0903e0c423a49729d8d0a758d83bc5c
Decoupling peptide binding from T cell receptor recognition with engineered chimeric MHC-I molecules
Autor:
Georgia F. Papadaki, Omar Ani, Tyler J. Florio, Michael C. Young, Julia N. Danon, Yi Sun, Devin Dersh, Nikolaos G. Sgourakis
Publikováno v:
Frontiers in Immunology, Vol 14 (2023)
Major Histocompatibility Complex class I (MHC-I) molecules display self, viral or aberrant epitopic peptides to T cell receptors (TCRs), which employ interactions between complementarity-determining regions with both peptide and MHC-I heavy chain ‘
Externí odkaz:
https://doaj.org/article/302e579d551846d78a6301c84be31c34
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
Externí odkaz:
https://doaj.org/article/10377cc98cea457a86b8741fbfdcf201
Autor:
Andrew C. McShan, Christine A. Devlin, Giora I. Morozov, Sarah A. Overall, Danai Moschidi, Neha Akella, Erik Procko, Nikolaos G. Sgourakis
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-18 (2021)
The molecular chaperones tapasin and TAPBPR play important roles in defining the repertoire of peptides displayed by MHC class I. Here, the authors combine NMR, ITC, fluorescence polarization measurements and deep mutational scanning analyses to reve
Externí odkaz:
https://doaj.org/article/307b0a46ed7d4915b4300973f40e73c1
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-13 (2021)
Here, the authors present Methyl Assignments Using Satisfiability (MAUS), a method for the assignment of methyl groups using raw NOE data. They use eight proteins in the 10–45 kDa size range as test cases and show that MAUS yields 100% accurate ass
Externí odkaz:
https://doaj.org/article/cb22eaddf85f4c9698cd9093fadb2f6b
Autor:
Soumya P. Behera, Abhinav Dubey, Wan-Na Chen, Viviane S. De Paula, Meng Zhang, Nikolaos G. Sgourakis, Wolfgang Bermel, Gerhard Wagner, Paul W. Coote, Haribabu Arthanari
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-7 (2020)
The structure and dynamics of large proteins and complexes can be studied by methyl-NMR but resonance assignment is still challenging. Here, the authors present a NMR method that leverages optimal control pulse design to unambiguously distinguish bet
Externí odkaz:
https://doaj.org/article/6d3ce66bd2fb4ffa8c649ac9c398510f
Autor:
Sarah A. Overall, Jugmohit S. Toor, Stephanie Hao, Mark Yarmarkovich, Sara M. O’Rourke, Giora I. Morozov, Son Nguyen, Alberto Sada Japp, Nicolas Gonzalez, Danai Moschidi, Michael R. Betts, John M. Maris, Peter Smibert, Nikolaos G. Sgourakis
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-13 (2020)
Peptide-MHC (pMHC) tetramers are important tools for probing T cell repertoire and adaptive immune responses. Here the authors use a molecular chaperone, TAPBPR, to develop a high-throughput, multiplexible platform for pMHC tetramer generation to fac
Externí odkaz:
https://doaj.org/article/975b9e150895476f87a40ab18d6ce573
Autor:
Jooyoung Park, Brinda Selvaraj, Andrew C McShan, Scott E Boyken, Kathy Y Wei, Gustav Oberdorfer, William DeGrado, Nikolaos G Sgourakis, Matthew J Cuneo, Dean AA Myles, David Baker
Publikováno v:
eLife, Vol 8 (2019)
The computational design of a symmetric protein homo-oligomer that binds a symmetry-matched small molecule larger than a metal ion has not yet been achieved. We used de novo protein design to create a homo-trimeric protein that binds the C3 symmetric
Externí odkaz:
https://doaj.org/article/322567187b15409490740d86572ec671