Zobrazeno 1 - 10
of 25
pro vyhledávání: '"Mireille Rivière"'
Autor:
Mireille Rivière, Nabil Miled, Cécile Bussetta, Christian Cambillau, Liliane Berti-Dupuis, Gérard Buono, Alain Roussel, Robert Verger, Stéphane Canaan
Publikováno v:
Biochemistry. 42:11587-11593
The crystal structures of gastric lipases in the apo form [Roussel, A., et al. (1999) J. Biol. Chem. 274, 16995-17002] or in complex with the (R(P))-undecyl butyl phosphonate [C(11)Y(4)(+)] [Roussel, A., et al. (2002) J. Biol. Chem. 277, 2266-2274] h
Publikováno v:
Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology. 136:131-138
Human gastric lipase (HGL) is an enzyme secreted by the stomach, which is stable and active despite the highly acidic environment. It has been clearly established that this enzyme is responsible for 30% of the fat digestion processes occurring in hum
Autor:
Robert Verger, Alain Roussel, Stéphane Canaan, Liliane Dupuis, Nabil Miled, Mireille Rivière, Frédéric Carrière, Christian Cambillau, De Caro A
Publikováno v:
Biochimie. 82:973-986
Human gastric lipase (HGL) is a lipolytic enzyme that is secreted by the chief cells located in the fundic part of the stomach. HGL plays an important role in lipid digestion, since it promotes the subsequent hydrolytic action of pancreatic lipase in
Publikováno v:
European Journal of Biochemistry. 262:644-651
Human gastric lipase (HGL) is a highly glycosylated protein, as glycan chains account for about 15% of the molecular mass of the native HGL. Four potential N-glycosylation consensus sites (Asn15, 80, 252 and 308) can be identified from the HGL amino
Autor:
Mireille Rivière, Robert Verger, Anne-Marie Moustacas-Gardies, Abdelkarim Abousalham, Sabine Chenivesse, Chantal Abergel
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 57:320-322
The plant phospholipase D (PLD) is considered to be a key enzyme involved in various physiological processes such as signal transduction and membrane metabolism. Crystals of the PLD protein from Vigna unguiculata have been produced from the recombina
Autor:
Germain Puzo, Mireille Rivière
Publikováno v:
Journal of Biological Chemistry. 266:9057-9063
An unknown immunogenic glycopeptidolipid, named GPL X-1, was isolated from Mycobacterium xenopi, which is a nontuberculous mycobacterium responsible for pulmonary and disseminated infectious diseases mainly occurring in immunocompromised patients. Th
Publikováno v:
Biochimica et biophysica acta. 1645(2)
In human adults, the enzymatic hydrolysis of dietary fat along the digestive tract is sequentially catalyzed by two main enzymes, human gastric lipase (HGL) and human pancreatic lipase (HPL). Both a chemically inhibited form of HPL as well as an inac
Publikováno v:
Intestinal Lipid Metabolism ISBN: 9781461354352
Under normal physiological conditions the digestion and absorption of dietary lipids are highly efficiently processed. In humans, the diet generally contains 90 to 120 g of lipids (mostly triacylglycerols), more than 95% of which are absorbed, due to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ca1c11af44a9fbd98ac946ca5d192776
https://doi.org/10.1007/978-1-4615-1195-3_2
https://doi.org/10.1007/978-1-4615-1195-3_2
Autor:
Robert Verger, Stéphane Canaan, Liliane Dupuis, Christian Cambillau, Mireille Rivière, Marie-Pierre Egloff, Alain Roussel
Publikováno v:
The Journal of biological chemistry. 274(24)
Fat digestion in humans requires not only the classical pancreatic lipase but also gastric lipase, which is stable and active despite the highly acidic stomach environment. We report here the structure of recombinant human gastric lipase at 3.0-A res
Publikováno v:
Biochemical and biophysical research communications. 257(3)
Recombinant human gastric lipase (rHGL) and three of its cysteine mutants (cysteine 227, 236, and 244 substitued for threonine or serine) were expressed in the baculovirus/insect cell system and purified to homogeneity by performing a two-step proced