Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Juliette Fortpied"'
Autor:
Juliette Fortpied, Sylvie Collignon, Nicolas Moniotte, Frédéric Renaud, Babak Bayat, Dominique Lemoine
Publikováno v:
Malaria Journal, Vol 19, Iss 1, Pp 1-15 (2020)
Abstract Background Developing thermostable vaccines is a challenge for pharmaceutical companies due to the inherent instability of biological molecules in aqueous solution. The problem is even more stringent in regions subjected to high temperatures
Externí odkaz:
https://doaj.org/article/8d2198b5cc0e4dd196e8beb8f0aa38ad
Autor:
Juliette Fortpied, Florence Wauters, Christelle Rochart, Philippe Hermand, Bernard Hoet, Nicolas Moniotte, Ivo Vojtek
Publikováno v:
Human Vaccines & Immunotherapeutics, Vol 14, Iss 5, Pp 1243-1250 (2018)
Accidental exposure of a vaccine containing an aluminum-salt adjuvant to temperatures below 0°C in the cold chain can lead to freeze damage. Our study evaluated the potential for freeze damage in a licensed aluminum-salt-containing protein-D-conjuga
Externí odkaz:
https://doaj.org/article/4102bb4916ca4d5fb0afba9f7da06586
Autor:
Babak Bayat, Frédéric Renaud, Nicolas Moniotte, Juliette Fortpied, Sylvie Collignon, Lemoine Dominique Ingrid
Publikováno v:
Malaria Journal, Vol 19, Iss 1, Pp 1-15 (2020)
Malaria Journal
Malaria Journal
Background Developing thermostable vaccines is a challenge for pharmaceutical companies due to the inherent instability of biological molecules in aqueous solution. The problem is even more stringent in regions subjected to high temperatures in which
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df785d0b0ba404efb333f09f44e1835b
http://link.springer.com/article/10.1186/s12936-020-03253-1
http://link.springer.com/article/10.1186/s12936-020-03253-1
Autor:
Philippe Hermand, Florence Emilie Jeanne Francoise Wauters, Ivo Vojtek, Nicolas Moniotte, Bernard Hoet, Christelle Rochart, Juliette Fortpied
Publikováno v:
Human Vaccines & Immunotherapeutics
Accidental exposure of a vaccine containing an aluminum-salt adjuvant to temperatures below 0°C in the cold chain can lead to freeze damage. Our study evaluated the potential for freeze damage in a licensed aluminum-salt-containing protein-D-conjuga
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01f882eadb540d7bd5e92165977d5ff4
http://europepmc.org/articles/PMC5989897
http://europepmc.org/articles/PMC5989897
Autor:
Rita Gemayel, Rim Rzem, Didier Vertommen, Juliette Fortpied, Maria Veiga-da-Cunha, Emile Van Schaftingen
Publikováno v:
FEBS Journal. 274:4360-4374
The purpose of this work was to identify the function of bacterial homologues of fructosamine 3-kinase (FN3K), a mammalian enzyme responsible for the removal of fructosamines from proteins. FN3K homologues were identified in approximately 200 (i.e. a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8e9f421f5f81f833a0ecb536e8be1184
https://doi.org/10.1111/j.1742-4658.2007.05948.x
https://doi.org/10.1111/j.1742-4658.2007.05948.x
Publikováno v:
Biochemical Journal. 388:795-802
FN3K (fructosamine 3-kinase) is a mammalian enzyme that catalyses the phosphorylation of fructosamines, which thereby becomes unstable and detaches from proteins. The homologous mammalian enzyme, FN3K-RP (FN3K-related protein), does not phosphorylate
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::03d8667680318bc699ea1f58a775249f
https://doi.org/10.1042/bj20041976
https://doi.org/10.1042/bj20041976
Publikováno v:
Diabetes/metabolism research and reviews. 26(4)
BACKGROUND: Complement activation via the MBL pathway has been proposed to play a role in the pathogenesis of diabetic complications. As protein glycation is increased in diabetes, we tested the possibility that the glycation product fructoselysine i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf9b0353448e4b3776dd3d1792513de8
https://pubmed.ncbi.nlm.nih.gov/20503257
https://pubmed.ncbi.nlm.nih.gov/20503257
Publikováno v:
The Biochemical journal, Vol. 406, no. 1, p. 139-45 (2007)
Ribulosamines, which are substrates for the deglycating enzyme fructosamine-3-kinase-related protein, are presumably formed intracellularly through glycation of proteins with ribose 5-phosphate followed by dephosphorylation of resulting RN5Ps (ribulo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d83a570e2d84533aedffff455dcece39
https://hdl.handle.net/2078.1/10948
https://hdl.handle.net/2078.1/10948
Publikováno v:
The Journal of biological chemistry. 281(27)
Fructosamine-3-kinase (FN3K) is a recently described protein-repair enzyme responsible for the removal of fructosamines, which are the products of a spontaneous reaction of glucose with amines. We show here that, compared with glucose, glucose 6-phos
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::12efeb76fbfc7cbf984af63299bece3e
https://pubmed.ncbi.nlm.nih.gov/16670083
https://pubmed.ncbi.nlm.nih.gov/16670083
Autor:
Ghislain Delpierre, Niki Bergans, Florent Vanstapel, Elsa Wiame, Emile Van Schaftingen, François Collard, Juliette Fortpied, Didier Vertommen
Publikováno v:
The Biochemical journal, Vol. 382, no. Pt 1, p. 137-43 (2004)
Fructosamine 3-kinase (FN3K), an enzyme initially identified in erythrocytes, catalyses the phosphorylation of fructosamines on their third carbon, leading to their destabilization and their removal from protein. We show that human erythrocytes also
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::909738e2c834d7ea20ffa1df4cafec3e
https://europepmc.org/articles/PMC1133924/
https://europepmc.org/articles/PMC1133924/