Zobrazeno 1 - 10
of 46
pro vyhledávání: '"Catherine Chapus"'
Publikováno v:
International Journal of Obesity. 27:319-325
Previous in vitro experiments, as well as acute assays in rat showed that the C-terminal domain (CT-domain) of porcine pancreatic lipase behaves as a potent specific noncovalent inhibitor of pancreatic lipase. Nevertheless, the potential use of the C
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a446e8f1d1dbc4554e121fdab6850c2e
https://doi.org/10.1038/sj.ijo.0802245
https://doi.org/10.1038/sj.ijo.0802245
Autor:
Brigitte Kerfelec, Sandrine Jayne, Catherine Chapus, Simone Granon, Juan A. Hermoso, Edith Foglizzo, Isabelle Crenon
Publikováno v:
Biochemistry. 41:8422-8428
Although structurally similar to pancreatic lipase (PL), the key enzyme of intestinal fat digestion, pancreatic lipase-related protein type 2 (PLRP2) differs from PL in certain functional properties. Notably, PLRP2 has a broader substrate specificity
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a6739d623e4a53b6ab19a74f47b4a20
https://doi.org/10.1021/bi025867j
https://doi.org/10.1021/bi025867j
Autor:
Catherine Chapus, Laurence Ayvazian, Simone Granon, Brigitte Kerfelec, Isabelle Crenon, Edith Foglizzo, Christophe Dubois
Publikováno v:
Journal of Biological Chemistry. 276:14014-14018
In vertebrates, dietary fat digestion mainly results from the combined effect of pancreatic lipase, colipase, and bile. It has been proposed that in vivo lipase adsorption on oil-water emulsion is mediated by a preformed lipase-colipase-mixed micelle
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1d2dbc73e346b7dc02843e17755debd9
https://doi.org/10.1074/jbc.m010328200
https://doi.org/10.1074/jbc.m010328200
Autor:
Catherine Chapus, Cyril Dominguez, Brigitte Kerfelec, Corinne Sebban-Kreuzer, Olivier Bornet, Françoise Guerlesquin
Publikováno v:
FEBS Letters. 482:109-112
Colipase is a small protein (10 kDa), which acts as a protein cofactor for the pancreatic lipase. Various models of the activated ternary complex (lipase–colipase–bile salt micelles) have been proposed using detergent micelles, but no structural
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1cbac3749d88292d98eaa2969283e87f
https://doi.org/10.1016/s0014-5793(00)02034-2
https://doi.org/10.1016/s0014-5793(00)02034-2
Autor:
David Pignol, Catherine Chapus, Juan A. Hermoso, Isabelle Crenon, Juan C. Fontecilla-Camps, Brigitte Kerfelec
Publikováno v:
Chemistry and Physics of Lipids. 93:123-129
The catalytic activity of most lipases depends on the aggregation state of their substrates. It is supposed that lipase activation requires the unmasking and structuring of the enzyme's active site through conformational changes involving the presenc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9079928228a216cd901b236667f04c1
https://doi.org/10.1016/s0009-3084(98)00036-x
https://doi.org/10.1016/s0009-3084(98)00036-x
Autor:
Juan A. Hermoso, Catherine Chapus, Sandrine Jayne, Isabelle Crenon, David Pignol, Brigitte Kerfelec
Publikováno v:
Biochemical and Biophysical Research Communications. 246:513-517
Besides the active pancreatic lipase (PL) which plays a major role in dietary fat digestion, the presence of a pancreatic lipase related protein 1 (PLRP1) displaying a very low lipolytic activity has been reported in vertebrates. It has been suggeste
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d7f92481c5cbb61bae52b936a0e659e7
https://doi.org/10.1006/bbrc.1998.8651
https://doi.org/10.1006/bbrc.1998.8651
Autor:
David Pignol, Isabelle Crenon, Brigitte Kerfelec, Catherine Chapus, Juan C. Fontecilla-Camps, Juan A. Hermoso
Publikováno v:
Journal of Biological Chemistry. 271:18007-18016
The crystal structure of the ternary porcine lipase-colipase-tetra ethylene glycol monooctyl ether (TGME) complex has been determined at 2.8 A resolution. The crystals belong to the cubic space group F23 with a = 289.1 A and display a strong pseudo-s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::652c38e846d61ded8ea2a4eb40b36395
https://doi.org/10.1074/jbc.271.30.18007
https://doi.org/10.1074/jbc.271.30.18007
Autor:
Juan A. Hermoso, Isabelle Crenon, José M. Mancheño, Catherine Chapus, Brigritte Kerfelec, Sandrine Jayne
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 60:2107-2109
Horse pancreatic lipase-related proteins PLRP1 and PLRP2 are produced by the pancreas together with pancreatic lipase (PL). Sequence-comparison analyses reveal that the three proteins possess the same two-domain organization: an N-terminal catalytic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::91b03282013411dfbae4693ce724a01f
https://doi.org/10.1107/s0907444904024229
https://doi.org/10.1107/s0907444904024229
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism. 1213:357-360
Pancreatic colipase plays an essential role in the intestinal fat digestion by anchoring lipase on lipid/water interfaces in the presence of bile salts. In contrast to other species, two molecular forms of colipase, A and B, have been found in horse.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::810fb6f1fbed99aecad8e282b8803fd1
https://doi.org/10.1016/0005-2760(94)00096-4
https://doi.org/10.1016/0005-2760(94)00096-4
Autor:
Dominique Lombardo, Chrislaine Martinez, Brigitte Kerfelec, Catherine Chapus, Christian Cambillau, Yves Bourne
Publikováno v:
Journal of Molecular Biology. 238:709-732
Pancreatic lipase (EC 3.1.1.3) plays a key role in dietary fat digestion by converting triacylglycerols into 2-monoacylglycerols and free fatty acids in the intestine. Although the crystallographic structures of the human pancreatic lipase and of a h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c5521455d4434d4cfdd1ee1b2cc0c1b5
https://doi.org/10.1006/jmbi.1994.1331
https://doi.org/10.1006/jmbi.1994.1331