Zobrazeno 1 - 10
of 34
pro vyhledávání: '"Mainak Guharoy"'
Autor:
Kobe Janssen, Ramon Duran-Romaña, Guy Bottu, Mainak Guharoy, Alexander Botzki, Frederic Rousseau, Joost Schymkowitz
Publikováno v:
BMC Bioinformatics, Vol 24, Iss 1, Pp 1-9 (2023)
Abstract Background Next-generation sequencing technologies yield large numbers of genetic alterations, of which a subset are missense variants that alter an amino acid in the protein product. These variants can have a potentially destabilizing effec
Externí odkaz:
https://doaj.org/article/c87eed1678864af89b194b57ff135748
Publikováno v:
Communications Biology, Vol 5, Iss 1, Pp 1-15 (2022)
Systematic bioinformatics analysis of cooperative degradation of protein complexes indicates that degrons extensively overlap with protein-protein interaction sites, hiding degrons from ubiquitination machinery and suggesting the existence of co-degr
Externí odkaz:
https://doaj.org/article/417784a53de54cdcb8bbc91ae02dc19e
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-13 (2016)
Degrons are determinants within proteins that direct programmed degradation by the ubiquitinproteasome system. Here, the authors propose a three-part degron architecture which contains an E3-ligase recognition motif, a ubiquitination site(s), and a d
Externí odkaz:
https://doaj.org/article/ab59f1e65dfe4c0eb87197745c6290ec
Publikováno v:
PLoS ONE, Vol 10, Iss 10, p e0139731 (2015)
Proteins form large macromolecular assemblies with RNA that govern essential molecular processes. RNA-binding proteins have often been associated with conformational flexibility, yet the extent and functional implications of their intrinsic disorder
Externí odkaz:
https://doaj.org/article/185eae56446345a9a23f8cd931f928e8
Publikováno v:
PLoS ONE, Vol 8, Iss 5, p e65443 (2013)
The ubiquitin-proteasome system plays a central role in cellular regulation and protein quality control (PQC). The system is built as a pyramid of increasing complexity, with two E1 (ubiquitin activating), few dozen E2 (ubiquitin conjugating) and sev
Externí odkaz:
https://doaj.org/article/bc5e98eb2c4f4b26bf02a7a8619e70d1
Publikováno v:
Biophys J
Intrinsically disordered proteins (IDPs) are proteins whose native functional states represent ensembles of highly diverse conformations. Such ensembles are a challenge for quantitative structure comparisons as their conformational diversity preclude
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7aa9eadeb2af30996638f61ac3ab8ec8
The 20S proteasome is known to degrade intrinsically disordered proteins (IDPs) via an ubiquitin-independent, disorder-driven mechanism. Unless protected within protein complexes or macromolecular assemblies, certain IDPs can undergo degradation medi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7abfd60bee7e9c3217d93ffaa91a8f92
https://hdl.handle.net/20.500.14017/c1e86c74-9737-4092-bbcd-7b5161a96ad8
https://hdl.handle.net/20.500.14017/c1e86c74-9737-4092-bbcd-7b5161a96ad8
Protein-protein interactions can be characterized by high-resolution structures of complexes, from which diverse features of the interfaces can be derived. For the majority of protein-protein interactions identified, however, there is no information
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3f64ce51cb59269220726beb94d07be9
https://biblio.vub.ac.be/vubir/unique-physicochemical-patterns-of-residues-in-proteinprotein-interfaces(fa26ebf9-46ed-4bf2-b95a-0926a4839502).html
https://biblio.vub.ac.be/vubir/unique-physicochemical-patterns-of-residues-in-proteinprotein-interfaces(fa26ebf9-46ed-4bf2-b95a-0926a4839502).html
Publikováno v:
Journal of the American Chemical Society. 137:13807-13817
Intrinsically disordered proteins (IDPs) are important for health and disease, yet their lack of net structure precludes an understanding of their function using classical methods. Gas-phase techniques provide a promising alternative to access inform
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b626794163fa1ae5d3ec7ff3b27d4acd
https://doi.org/10.1021/jacs.5b06027
https://doi.org/10.1021/jacs.5b06027
Autor:
Philip Van Damme, Thomas Vercruysse, Paul A. Anderson, Elke Bogaert, Denes Kovacs, Pieter Baatsen, Veronica H Ryan, J. Paul Taylor, Mathias De Decker, Frederic Rousseau, Albert Konijnenberg, Nicolas L. Fawzi, Dirk Daelemans, Mainak Guharoy, Evy Timmerman, Regina-Maria Kolaitis, Peter Tompa, Abigail M. Janke, Frank Sobott, Nancy Kedersha, Joost Schymkowitz, Alex Volkov, Wim Robberecht, Francis Impens, Tom Jaspers, Steven Boeynaems, Ludo Van Den Bosch
Publikováno v:
Molecular Cell
Molecular cell
BASE-Bielefeld Academic Search Engine
MOLECULAR CELL
Molecular cell
BASE-Bielefeld Academic Search Engine
MOLECULAR CELL
Summary Liquid-liquid phase separation (LLPS) of RNA-binding proteins plays an important role in the formation of multiple membrane-less organelles involved in RNA metabolism, including stress granules. Defects in stress granule homeostasis constitut
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c68846746fd56e19b061db65351ffaa