Zobrazeno 1 - 10
of 105
pro vyhledávání: '"Thérèse E, Malliavin"'
Autor:
Daniel Förster, Jérôme Idier, Leo Liberti, Antonio Mucherino, Jung-Hsin Lin, Thérèse E. Malliavin
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-16 (2022)
Abstract Intrinsically disordered proteins (IDP) are at the center of numerous biological processes, and attract consequently extreme interest in structural biology. Numerous approaches have been developed for generating sets of IDP conformations ver
Externí odkaz:
https://doaj.org/article/8863178f48b94b30a8d5904f35239949
Autor:
Ibrahima Goudiaby, Thérèse E. Malliavin, Eva Mocchetti, Sandrine Mathiot, Samir Acherar, Céline Frochot, Muriel Barberi-Heyob, Benoît Guillot, Frédérique Favier, Claude Didierjean, Christian Jelsch
Publikováno v:
Molecules, Vol 28, Iss 14, p 5603 (2023)
Neuropilin 1 (NRP1), a cell-surface co-receptor of a number of growth factors and other signaling molecules, has long been the focus of attention due to its association with the development and the progression of several types of cancer. For example,
Externí odkaz:
https://doaj.org/article/4ed57c00a68845df925940f4ba6d8ed9
Autor:
Thérèse E. Malliavin
Publikováno v:
Scientific Reports, Vol 11, Iss 1, Pp 1-12 (2021)
Abstract Protein structure determination is undergoing a change of perspective due to the larger importance taken in biology by the disordered regions of biomolecules. In such cases, the convergence criterion is more difficult to set up and the size
Externí odkaz:
https://doaj.org/article/5b859c69229b48e990be57a652283d2d
Autor:
Grazia Cottone, Letizia Chiodo, Luca Maragliano, Michel-Robert Popoff, Christine Rasetti-Escargueil, Emmanuel Lemichez, Thérèse E. Malliavin
Publikováno v:
Toxins, Vol 14, Iss 9, p 644 (2022)
Although botulinum neurotoxins (BoNTs) are among the most toxic compounds found in nature, their molecular mechanism of action is far from being elucidated. A key event is the conformational transition due to acidification of the interior of synaptic
Externí odkaz:
https://doaj.org/article/8c182d48258645a7a88e64d3ad8d07ce
Publikováno v:
Frontiers in Molecular Biosciences, Vol 7 (2020)
Molecular dynamics (MD) simulations have been recorded on the complex between the edema factor (EF) of Bacilllus anthracis and calmodulin (CaM), starting from a structure with the orthosteric inhibitor adefovir bound in the EF catalytic site. The sta
Externí odkaz:
https://doaj.org/article/6d723c838e94431d8f36c10d0143f357
Publikováno v:
PLoS ONE, Vol 13, Iss 11, p e0207899 (2018)
In the histidine kinase family, the HAMP and DHp domains are considered to play an important role into the transmission of signal arising from environmental conditions to the auto-phosphorylation site and to the binding site of response regulator. Se
Externí odkaz:
https://doaj.org/article/26af95fe114340789293bc0c498d9c2c
Autor:
Grazia Cottone, Letizia Chiodo, Luca Maragliano, Michel-Robert Popoff, Christine Rasetti-Escargueil, Emmanuel Lemichez, Thérèse E. Malliavin
Although the botulinum neurotoxins (BoNTs) are among the most toxic compounds found in nature, their molecular mechanism of action is far from being elucidated. A key event is the conformational transition due to the acidification of the interior of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7e9538ac39b6b0e425d5d775a2f1fd2d
https://doi.org/10.1101/2022.09.01.506163
https://doi.org/10.1101/2022.09.01.506163
Autor:
Irène Pitard, Thérèse E Malliavin
Publikováno v:
Toxins, Vol 11, Iss 6, p 369 (2019)
Understanding the functions and mechanisms of biological systems is an outstanding challenge. One way to overcome it is to combine together several approaches such as molecular modeling and experimental structural biology techniques. Indeed, the inte
Externí odkaz:
https://doaj.org/article/0a420835a18840848a86d4cb85ae6a9b
Autor:
Thérèse E. Malliavin
Data-sets used to produce the plots of the article. Paillares E, Marechal M, Swistak L, Tsoumts Meda L, Lemichez E, Malliavin TE. International Journal of Molecular Sciences 2021.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0b52ffb348ff4f6e721652c29f9e25c8
Autor:
Aracelys López-Castilla, Olivera Francetic, Yasaman Karami, Thérèse E. Malliavin, Benjamin Bardiaux, Michael Nilges, Jenny-Lee Thomassin, Andrea Ori, Nadia Izadi-Pruneyre
Publikováno v:
Structure
Structure, Elsevier (Cell Press), 2021, 29, pp.1-13. ⟨10.1016/j.str.2021.07.008⟩
Structure, 2021, 29, pp.1-13. ⟨10.1016/j.str.2021.07.008⟩
Structure, Elsevier (Cell Press), 2021, 29, pp.1-13. ⟨10.1016/j.str.2021.07.008⟩
Structure, 2021, 29, pp.1-13. ⟨10.1016/j.str.2021.07.008⟩
SUMMARYType IV pili (T4P) are distinctive dynamic filaments at the surface of many bacteria that can rapidly extend, retract and withstand strong forces. T4P are important virulence factors in many human pathogens, including Enterohemorrhagic Escheri
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9cb315385e8be5e822a652bf1760c066
https://hal-pasteur.archives-ouvertes.fr/pasteur-03380000v2/file/PIIS0969212621002586.pdf
https://hal-pasteur.archives-ouvertes.fr/pasteur-03380000v2/file/PIIS0969212621002586.pdf