Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Mariangela Dametto"'
Autor:
Jadson C. Santos, Mariangela Dametto, Ana Paula Masson, Vitor M. Faça, Rodrigo Bonacin, Eduardo A. Donadi, Geraldo Aleixo Passos
Publikováno v:
Frontiers in Immunology, Vol 13 (2022)
The autoimmune regulator (AIRE) protein functions as a tetramer, interacting with partner proteins to form the “AIRE complex,” which relieves RNA Pol II stalling in the chromatin of medullary thymic epithelial cells (mTECs). AIRE is the primary m
Externí odkaz:
https://doaj.org/article/de4dd8e5035c4a96966b7847a5474dd6
Publikováno v:
2022 E-Health and Bioengineering Conference (EHB).
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::282a2fa1c832d47ad7b28b8498db248a
https://doi.org/10.1109/ehb55594.2022.9991615
https://doi.org/10.1109/ehb55594.2022.9991615
Publikováno v:
2021 IEEE 30th International Conference on Enabling Technologies: Infrastructure for Collaborative Enterprises (WETICE).
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::19b9f43a10ed41381d97cf22fd45bb4e
https://doi.org/10.1109/wetice53228.2021.00041
https://doi.org/10.1109/wetice53228.2021.00041
Autor:
Jadson C. Santos, Eduardo Antônio Donadi, Geraldo Aleixo Silva Passos, Rodrigo Bonacin, Vitor M. Faça, Ana Paula Masson, Mariangela Dametto
The in silico and in vitro binding of a peptide covering a part of the autoimmune regulator (AIRE) SAND domain with the SIRT1 protein provides a powerful model system for studying the mechanism of the dominant SAND G228W mutation, which is the causat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::614647ccc6806552e05610e95e0c30c2
https://doi.org/10.1101/2021.08.24.457565
https://doi.org/10.1101/2021.08.24.457565
We have studied atomic motions during the chemical reaction catalysed by the enzyme dihydrofolate reductase of Escherichia coli (EcDHFR), an important enzyme for nucleic acid synthesis. In our earlier work on the enzymes human lactate dehydrogenase a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4f29c110e409015062140efefa4123df
https://europepmc.org/articles/PMC3430383/
https://europepmc.org/articles/PMC3430383/
Publikováno v:
The journal of physical chemistry. B. 112(31)
The refolding mechanism of apomyoglobin (apoMb) subsequent to high-temperature unfolding has been examined using computer simulations with atomic level detail. The folding of this protein has been extensively studied experimentally, providing a large
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4a23be35873d06b8369bde744cb81687
https://pubmed.ncbi.nlm.nih.gov/18616314
https://pubmed.ncbi.nlm.nih.gov/18616314