Zobrazeno 1 - 10
of 23
pro vyhledávání: '"Guylaine Hoffner"'
Autor:
Scott Ensel, Lynn Uhrig, Ayberk Ozkirli, Guylaine Hoffner, Jordy Tasserie, Stanislas Dehaene, Dimitri Van De Ville, Béchir Jarraya, Elvira Pirondini
Publikováno v:
Communications Biology, Vol 7, Iss 1, Pp 1-12 (2024)
Abstract The awake mammalian brain is functionally organized in terms of large-scale distributed networks that are constantly interacting. Loss of consciousness might disrupt this temporal organization leaving patients unresponsive. We hypothesize th
Externí odkaz:
https://doaj.org/article/b1fbf760e45644f38f94f5a4e0bc0d7b
Autor:
William André, Isabelle Nondier, Maud Valensi, François Guillonneau, Christian Federici, Guylaine Hoffner, Philippe Djian
Publikováno v:
Neurobiology of Disease, Vol 101, Iss , Pp 40-58 (2017)
Transglutaminases are calcium-dependent enzymes that catalyze the formation of ε-(γ-glutamyl)lysine isopeptide bonds between specific glutamine and lysine residues. Some transglutaminase isoforms are present in the brain and are thought to particip
Externí odkaz:
https://doaj.org/article/538499010a52458a90017019abd21ea1
Autor:
Guylaine Hoffner, Philippe Djian
Publikováno v:
Brain Sciences, Vol 4, Iss 1, Pp 91-122 (2014)
Huntington disease and other diseases of polyglutamine expansion are each caused by a different protein bearing an excessively long polyglutamine sequence and are associated with neuronal death. Although these diseases affect largely different brain
Externí odkaz:
https://doaj.org/article/1ef4d64c14cf4d54a619eb638f93f9e6
Autor:
François Guillonneau, William André, Christian Federici, Maud Valensi, Philippe Djian, Guylaine Hoffner, Isabelle Nondier
Publikováno v:
Neurobiology of Disease
Neurobiology of Disease, Elsevier, 2017, 101, pp.40-58. ⟨10.1016/j.nbd.2017.01.007⟩
Neurobiology of Disease, Vol 101, Iss, Pp 40-58 (2017)
Neurobiology of Disease, Elsevier, 2017, 101, pp.40-58. ⟨10.1016/j.nbd.2017.01.007⟩
Neurobiology of Disease, Vol 101, Iss, Pp 40-58 (2017)
Transglutaminases are calcium-dependent enzymes that catalyze the formation of ε-(γ-glutamyl)lysine isopeptide bonds between specific glutamine and lysine residues. Some transglutaminase isoforms are present in the brain and are thought to particip
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d3d0016de38d91ae224a1fc03ae15157
https://hal.archives-ouvertes.fr/hal-03036725
https://hal.archives-ouvertes.fr/hal-03036725
Publikováno v:
Analytical Chemistry
Analytical Chemistry, American Chemical Society, 2017, 89 (10), pp.5201-5209. ⟨10.1021/acs.analchem.6b04199⟩
Analytical Chemistry, American Chemical Society, 2017, 89 (10), pp.5201-5209. ⟨10.1021/acs.analchem.6b04199⟩
R6/2 mice contain an N-terminal fragment of human huntingtin with an expanded polyQ and develop a neurological disease resembling Huntington disease. Although the brain of R6/2 mice contains numerous inclusions, there is very little neuronal death. I
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56536d3f85220f87bf357630b5b680b0
https://hal.archives-ouvertes.fr/hal-03036727
https://hal.archives-ouvertes.fr/hal-03036727
Autor:
Philippe Djian, Guylaine Hoffner
Publikováno v:
Brain Sciences, Vol 4, Iss 1, Pp 91-122 (2014)
Brain Sciences
Brain Sciences
Huntington disease and other diseases of polyglutamine expansion are each caused by a different protein bearing an excessively long polyglutamine sequence and are associated with neuronal death. Although these diseases affect largely different brain
Publikováno v:
Analytical Chemistry. 85:3765-3773
Huntington's disease is caused by a polyglutamine expansion in huntingtin. Affected brain regions contain characteristic aggregates of the misfolded expanded protein. Studies in cells and animals show that aggregates are polymorphic and that the seco
Autor:
Guylaine Hoffner, Philippe Djian
Publikováno v:
Oncotarget
Oncotarget, Impact journals, 2017, 8 (34), pp.55772-55773. ⟨10.18632/oncotarget.19694⟩
Oncotarget, Impact journals, 2017, 8 (34), pp.55772-55773. ⟨10.18632/oncotarget.19694⟩
International audience
Publikováno v:
The Journal of Biological Chemistry
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2008, epub ahead of print. ⟨10.1074/jbc.M806256200⟩
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2008, epub ahead of print. ⟨10.1074/jbc.M806256200⟩
International audience; Deposition of misfolded proteins with a polyglutamine expansion is a hallmark of Huntington's disease and other neurodegenerative disorders. Impairment of the proteolytic function of the proteasome has been reported to be both
Publikováno v:
Journal of Neurochemistry. 95:125-136
Huntington's disease resulting from huntingtin containing an expanded polyglutamine is associated with aggregates largely confined to neuronal inclusions, and with neuronal death. Inclusions are thought to originate from discrete N-terminal fragments