Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Florentine Gilis"'
Autor:
Emeline Puissant, Florentine Gilis, Virginie Tevel, Jean-Michel Vandeweerd, Bruno Flamion, Michel Jadot, Marielle Boonen
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-13 (2022)
Abstract Mucopolysaccharidosis IX is a lysosomal storage disorder caused by a deficiency in HYAL1, an enzyme that degrades hyaluronic acid at acidic pH. This disease causes juvenile arthritis in humans and osteoarthritis in the Hyal1 knockout mouse m
Externí odkaz:
https://doaj.org/article/03c97d9d9aa14651bd6e8ca906f12b2b
Autor:
Emeline Puissant, Florentine Gilis, Virginie Tevel, Jean-Michel Vandeweerd, Bruno Flamion, Michel Jadot, Marielle Boonen
Publikováno v:
Puissant, E, Gilis, F, Tevel, V, Vandeweerd, J-M, Flamion, B, Jadot, M & Boonen, M 2022, ' Hyaluronidase 1 deficiency decreases bone mineral density in mice ', Scientific Reports, vol. 12, no. 1, 10142 . https://doi.org/10.1038/s41598-022-14473-7
Mucopolysaccharidosis IX is a lysosomal storage disorder caused by a deficiency in HYAL1, an enzyme that degrades hyaluronic acid at acidic pH. This disease causes juvenile arthritis in humans and osteoarthritis in the Hyal1 knockout mouse model. Our
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::204df93bf1c7a4b2e647ee5fa4b95e3f
https://pubmed.ncbi.nlm.nih.gov/35710820
https://pubmed.ncbi.nlm.nih.gov/35710820
Publikováno v:
Biochemical and Biophysical Research Communications. 479(2):404-409
ATG9A is the only polytopic protein of the mammalian autophagy-related protein family whose members regulate autophagosome formation during macroautophagy. At steady state, ATG9A localizes to several intracellular sites, including the Golgi apparatus
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d543434e98b321deefffc5534f891bcd
https://doi.org/10.1016/j.bbrc.2016.09.097
https://doi.org/10.1016/j.bbrc.2016.09.097
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1863:2299-2310
ATG9A is a multispanning membrane protein required for autophagosome formation. Under basal conditions, neosynthesized ATG9A proteins travel to the Golgi apparatus and cycle between the trans-Golgi network and endosomes. In the present work, we searc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::27b73f1e789125a5ed55a402f1e640fe
https://doi.org/10.1016/j.bbamcr.2016.06.007
https://doi.org/10.1016/j.bbamcr.2016.06.007
Autor:
Sophie Dogné, Florentine Gilis, Marielle Boonen, Bruno Flamion, Emeline Puissant, Michel Jadot
Publikováno v:
Traffic. 15:500-515
The hyaluronidase Hyal-1 is an acid hydrolase that degrades hyaluronic acid (HA), a component of the extracellular matrix. It is often designated as a lysosomal protein. Yet few data are available on its intracellular localization and trafficking. We
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bc3ddd75dfc302bc211c82a8da2df34a
https://doi.org/10.1111/tra.12162
https://doi.org/10.1111/tra.12162
Publikováno v:
Biochemical and biophysical research communications. 446(4)
It has long been known that liver lysosomes contain an endoglycosidase activity able to degrade the high molecular mass glycosaminoglycan hyaluronic acid (HA). The identification and cloning of a hyaluronidase with an acidic pH optimum, Hyal-1, sugge
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::44c60345fb6d0ad5dcdc753620847fc4
https://pubmed.ncbi.nlm.nih.gov/24667601
https://pubmed.ncbi.nlm.nih.gov/24667601
Autor:
Emeline, Puissant, Florentine, Gilis, Sophie, Dogné, Bruno, Flamion, Michel, Jadot, Marielle, Boonen
Publikováno v:
Traffic (Copenhagen, Denmark). 15(5)
The hyaluronidase Hyal-1 is an acid hydrolase that degrades hyaluronic acid (HA), a component of the extracellular matrix. It is often designated as a lysosomal protein. Yet few data are available on its intracellular localization and trafficking. We
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::56f92193b194c41befa618328cfc212b
https://pubmed.ncbi.nlm.nih.gov/24502338
https://pubmed.ncbi.nlm.nih.gov/24502338