Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Pau, Bernado"'
Autor:
Nikola Arsic, Tania Slatter, Gilles Gadea, Etienne Villain, Aurelie Fournet, Marina Kazantseva, Frédéric Allemand, Nathalie Sibille, Martial Seveno, Sylvain de Rossi, Sunali Mehta, Serge Urbach, Jean-Christophe Bourdon, Pau Bernado, Andrey V. Kajava, Antony Braithwaite, Pierre Roux
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-18 (2021)
p53 isoform Δ133p53β is reported to promote intrinsic oncogenic functions. Here the authors show Δ133p53β is sequestered as aggregates in an inactive form, while association with interacting partners including p63 isoforms and the CCT chaperone c
Externí odkaz:
https://doaj.org/article/68225466d9dc4ec1bb5844837f0a0ec8
Autor:
Min-Kyu, Cho, Gabrielle, Nodet, Hai-Young, Kim, Malene R, Jensen, Pau, Bernado, Claudio O, Fernandez, Stefan, Becker, Martin, Blackledge, Markus, Zweckstetter
Publikováno v:
Protein science : a publication of the Protein Society. 18(9)
The relation of alpha-synuclein (alphaS) aggregation to Parkinson's disease has long been recognized, but the pathogenic species and its molecular properties have yet to be identified. To obtain insight into the properties of alphaS in an aggregation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::9ba349322c538d84206130e2d40bde88
https://pubmed.ncbi.nlm.nih.gov/19554627
https://pubmed.ncbi.nlm.nih.gov/19554627
Autor:
Miquel Pons, Pau Bernado
Publikováno v:
ChemInform. 34
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0661432d0dd1cb54c3d4c2f442adf54c
https://doi.org/10.1002/chin.200327292
https://doi.org/10.1002/chin.200327292
Autor:
Estaña Garcia, Alejandro
Publikováno v:
Biochemistry, Molecular Biology. INSA de Toulouse, 2020. English. ⟨NNT : 2020ISAT0012⟩
Bioinformatics [q-bio.QM]. Institut National des Sciences Appliquées de Toulouse, 2020. English
Bioinformatics [q-bio.QM]. Institut National des Sciences Appliquées de Toulouse, 2020. English
National audience; Intrinsically Disordered Proteins (IDPs) are involved in many biological processes. Their inherent plasticity facilitates very specialized tasks in cell regulation and signalling, and their malfunction is linked to severe pathologi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::5c4029e386d75d24e3dc493b058ff598
https://hal.laas.fr/tel-03185221v2/document
https://hal.laas.fr/tel-03185221v2/document
Autor:
Estaña Garcia, Alejandro
Publikováno v:
Bioinformatics [q-bio.QM]. Institut National des Sciences Appliquées de Toulouse, 2020. English. ⟨NNT : 2020ISAT0012⟩
Intrinsically Disordered Proteins (IDPs) are involved in many biological processes. Their inherent plasticity facilitates very specialized tasks in cell regulation and signalling, and their malfunction is linked to severe pathologies. Understanding t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::c53ed1ec31f987c27a8e3aa2ba28c3e5
https://hal.laas.fr/tel-03185221v2
https://hal.laas.fr/tel-03185221v2
Disentangling structural complexity in proteins by decomposing SAXS data with chemometric approaches
Autor:
Herranz-Trillo, Fatima
Publikováno v:
Human health and pathology. Université Montpellier, 2017. English. ⟨NNT : 2017MONTT044⟩
Many biological systems are inherently polydisperse, presenting multiple coexisting species differing in size, shape or conformation (i.e. oligomeric mixtures, weakly bound complexes, and species appearing along amyloidogenic processes). The study of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::274017606ef54eee186afe012c450ca5
https://tel.archives-ouvertes.fr/tel-01690749
https://tel.archives-ouvertes.fr/tel-01690749