Search

Your search keyword '"Bobo, Claude"' showing total 31 results
Start Over Author "Bobo, Claude"
31 results on '"Bobo, Claude"'

8. Synthetic toxic Aβ 1–42 oligomers can assemble in different morphologies

Author

Bobo, Claude, primary, Chaignepain, Stéphane, additional, Henry, Sarah, additional, Vignaud, Hélène, additional, Améadan, Alfred, additional, Marchal, Christelle, additional, Prado, Enora, additional, Doutch, James, additional, Schmitter, Jean-Marie, additional, Nardin, Corinne, additional, Lecomte, Sophie, additional, and Cullin, Christophe, additional

Published
2017
Full Text
View/download PDF

12. Structure/Function Analysis of Protein–Protein Interactions Developed by the Yeast Pih1 Platform Protein and Its Partners in Box C/D snoRNP Assembly

Author

Quinternet, Marc, primary, Rothé, Benjamin, additional, Barbier, Muriel, additional, Bobo, Claude, additional, Saliou, Jean-Michel, additional, Jacquemin, Clémence, additional, Back, Régis, additional, Chagot, Marie-Eve, additional, Cianférani, Sarah, additional, Meyer, Philippe, additional, Branlant, Christiane, additional, Charpentier, Bruno, additional, and Manival, Xavier, additional

Published
2015
Full Text
View/download PDF

15. Synthetic toxic Aβ1–42 oligomers can assemble in different morphologies.

Author

Bobo, Claude, Chaignepain, Stéphane, Henry, Sarah, Vignaud, Hélène, Améadan, Alfred, Marchal, Christelle, Prado, Enora, Doutch, James, Schmitter, Jean-Marie, Nardin, Corinne, Lecomte, Sophie, and Cullin, Christophe

Subjects
*OLIGOMERS, *ALZHEIMER'S disease, *PEPTIDES, *AMYLOID beta-protein, *CELL membranes
Abstract

Background Alzheimer's disease is the most common neurodegenerative disease associated with aggregation of Aβ peptides. Aβ toxicity is mostly related to the capacity of intermediate oligomers to disrupt membrane integrity. We previously expressed Aβ 1–42 in a eukaryotic cellular system and selected synthetic variants on their sole toxicity. The most toxic mutant G37C forms stable oligomers. Methods Different biophysical methods (Fluorescence spectroscopy, cross-linking, mass spectrometry (MS), Small Angle X-ray Scattering (SAXS), Atomic Force Microscopy (AFM), Transmission Electron Microscopy (TEM), calcein leakage) were used. Results The oligomers are mostly populated by a 14 mers resulting from the packing of homodimers. These homodimers come from the formation of a disulfide bridge between two monomers. This link stabilizes the multimers and prevents the assembly into amyloid fibrils. These oligomers affect the membrane integrity. The reduction of disulfide bonds leads to a rearrangement and redirects assembly of Aβ amyloid fibrils. Conclusion The toxic synthetic Aβ G37C mutant can assemble into an amyloid of unusual morphology through the formation of anti-parallel β-sheets. This pathway involves the formation of oligomers resulting from the arrangement of Aβ dimers linked by covalent di-sulfide link, being these oligomers harmful for the membranes. General significance The capacity to produce large amount of stable oligomers without additional detergents or extrinsic cross-linkers allow further structural and biophysical studies to understand their capacity to assemble and disrupt the membranes, a key event in Alzheimer's disease. [ABSTRACT FROM AUTHOR]

Published
2017
Full Text
View/download PDF

30. A Structure-Toxicity Study of Aß42 Reveals a New Anti-Parallel Aggregation Pathway.

Author

Vignaud, Hélène, Bobo, Claude, Lascu, Ioan, Sörgjerd, Karin Margareta, Zako, Tamotsu, Maeda, Mizuo, Salin, Benedicte, Lecomte, Sophie, and Cullin, Christophe

Subjects
*BIOLOGICAL aggregation, *AMYLOID beta-protein, *CLEAVAGE (Embryology), *ALZHEIMER'S disease, *PROTEIN structure, *OLIGOMERIZATION, *GENETIC mutation
Abstract

Amyloid beta (Aβ) peptides produced by APP cleavage are central to the pathology of Alzheimer’s disease. Despite widespread interest in this issue, the relationship between the auto-assembly and toxicity of these peptides remains controversial. One intriguing feature stems from their capacity to form anti-parallel ß-sheet oligomeric intermediates that can be converted into a parallel topology to allow the formation of protofibrillar and fibrillar Aβ. Here, we present a novel approach to determining the molecular aspects of Aß assembly that is responsible for its in vivo toxicity. We selected Aß mutants with varying intracellular toxicities. In vitro, only toxic Aß (including wild-type Aß42) formed urea-resistant oligomers. These oligomers were able to assemble into fibrils that are rich in anti-parallel ß-sheet structures. Our results support the existence of a new pathway that depends on the folding capacity of Aß . [ABSTRACT FROM AUTHOR]

Published
2013
Full Text
View/download PDF

31. Bcl-x L deamidation and cancer: Charting the fame trajectories of legitimate child and hidden siblings.

Author

Beaumatin F, El Dhaybi M, Bobo C, Verdier M, and Priault M

Subjects
Amidohydrolases genetics, Apoptosis genetics, Autophagy genetics, Humans, Neoplasms drug therapy, Neoplasms pathology, Protein Processing, Post-Translational genetics, Carcinogenesis genetics, Drug Resistance, Neoplasm genetics, Neoplasms genetics, bcl-X Protein genetics
Abstract

Bcl-2 family proteins control programmed cell death through a complex network of interactions within and outside of this family, that are modulated by post-translational modifications (PTM). Bcl-x L , an anti-apoptotic member of this family, is overexpressed in a number of cancers, plays an important role in tumorigenesis and is correlated with drug resistance. Bcl-x L is susceptible to a number of different PTMs. Here, we focus on deamidation. We will first provide an overview of protein deamidation. We will then review how the apoptotic and autophagic functions of Bcl-x L are modified by this PTM, and how this impacts on its oncogenic properties. Possible therapeutic outcomes will also be discussed. Finally, we will highlight how the specific case of Bcl-x L deamidation provides groundings to revisit some concepts related to protein deamidation in general., (Copyright © 2017 Elsevier B.V. All rights reserved.)

Published
2017
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results