Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Janik Kokot"'
Autor:
Monica L. Fernández-Quintero, Janik Kokot, Franz Waibl, Anna-Lena M. Fischer, Patrick K. Quoika, Charlotte M. Deane, Klaus R. Liedl
Publikováno v:
mAbs, Vol 15, Iss 1 (2023)
ABSTRACTAdvances in structural biology and the exponential increase in the amount of high-quality experimental structural data available in the Protein Data Bank has motivated numerous studies to tackle the grand challenge of predicting protein struc
Externí odkaz:
https://doaj.org/article/3a42b424031444ed92eeaed275b5f9d3
Autor:
Monica L. Fernández-Quintero, Anna-Lena M. Fischer, Janik Kokot, Franz Waibl, Clarissa A. Seidler, Klaus R. Liedl
Publikováno v:
Frontiers in Immunology, Vol 13 (2022)
Sharks and other cartilaginous fish produce new antigen receptor (IgNAR) antibodies, as key part of their humoral immune response and are the phylogenetically oldest living organisms that possess an immunoglobulin (Ig)-based adaptive immune system. I
Externí odkaz:
https://doaj.org/article/1003c6cfbbab470690e0908c67085ab0
Autor:
Nancy D. Pomarici, Roberta Cacciato, Janik Kokot, Monica L. Fernández-Quintero, Klaus R. Liedl
Publikováno v:
Biomolecules, Vol 13, Iss 5, p 801 (2023)
The adaptive immune system arose around 500 million years ago in jawed fish, and, since then, it has mediated the immune defense against pathogens in all vertebrates. Antibodies play a central role in the immune reaction, recognizing and attacking ex
Externí odkaz:
https://doaj.org/article/2231e26d39cf4c8aaa97a1d8c9ba401a
Publikováno v:
Biomolecules, Vol 13, Iss 2, p 380 (2023)
Camelid heavy-chain antibody variable domains (VHH), nanobodies, are the smallest-known functional antibody fragments with high therapeutic potential. In this study, we investigate a VHH binding to hen egg-white lysozyme (HEL). We structurally and dy
Externí odkaz:
https://doaj.org/article/3613f649a09c43c3b41ee78b31478fba
Autor:
Monica L. Fernández-Quintero, Janik Kokot, Franz Waibl, Anna-Lena M. Fischer, Patrick K. Quoika, Charlotte M. Deane, Klaus R. Liedl
The tremendous advances in structural biology and the exponential increase of high-quality experimental structures available in the PDB motivated numerous studies to tackle the grand challenge of predicting protein structures. AlphaFold2 revolutioniz
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::458e4654e1f06e7df1b73816b6409687
https://doi.org/10.1101/2022.11.09.515600
https://doi.org/10.1101/2022.11.09.515600
