Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Chrislaine Martinez"'
Publikováno v:
Current Opinion in Structural Biology. 6:449-455
The last five years have witnessed the solution of a large number of lipase structures, which has led, among other insights, to the structural interpretation of the interfacial activation phenomenon in terms of 'lid' opening. This interpretation has
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ec12ab8b2705c46c0b62770bf3878d2f
https://doi.org/10.1016/s0959-440x(96)80108-4
https://doi.org/10.1016/s0959-440x(96)80108-4
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
Autor:
C. Cudrey, H. van Tilbeurgh, Christian Cambillau, Robert Verger, M P Egloff, Aurélie Nicolas, Chrislaine Martinez
Publikováno v:
Biochemistry. 33:83-89
Cutinases, a group of cutin degrading enzymes with molecular masses of around 22-25 kDa (Kolattukudy, 1984), are also able to efficiently hydrolyse triglycerides (De Geus et al., 1989; Lauwereys et al., 1991), but without exhibiting the interfacial a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ebf6ee50188472eea2701f832785f8dc
https://doi.org/10.1021/bi00167a011
https://doi.org/10.1021/bi00167a011
Autor:
Christian Cambillau, C. Theo Verrips, Jakob De Vlieg, Anne Nicolas, Lucia Creveld, Maarten R. Egmond, Chrislaine Martinez, Sonia Longhi
Publikováno v:
Proteins. 26(4)
In characterizing mutants and covalently inhibited complexes of Fusarium solani cutinase, which is a 197-residue lipolytic enzyme, 34 variant structures, crystallizing in 8 different crystal forms, have been determined, mostly at high resolution. Tak
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ccc3667b8a0b45977bea898fb1b0c2fd
https://pubmed.ncbi.nlm.nih.gov/8990497
https://pubmed.ncbi.nlm.nih.gov/8990497
Autor:
C. T. Verrips, Chrislaine Martinez, J. De Vlieg, Sonia Longhi, Christian Cambillau, Maarten R. Egmond, Aurélie Nicolas
Publikováno v:
Biochemistry. 35(2)
Cutinase from the fungus Fusarium solani pisi is a lipolytic enzyme able to hydrolyze both aggregated and soluble substrates. It therefore provides a powerful tool for probing the mechanisms underlying lipid hydrolysis. Lipolytic enzymes have a catal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::358bc1027847cdf15ba2284dda19f776
https://pubmed.ncbi.nlm.nih.gov/8555209
https://pubmed.ncbi.nlm.nih.gov/8555209
Publikováno v:
Protein engineering. 6(2)
Cutinases are extracellular enzymes involved in the disruption of cutine, an insoluble polyester which covers the surface of plants. They belong to a class of serine esterases that are able to hydrolyse fatty acid esters and emulsified triglycerides
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77dd8c967d63827f8bf43f4c436d6a23
https://pubmed.ncbi.nlm.nih.gov/8475042
https://pubmed.ncbi.nlm.nih.gov/8475042
Publikováno v:
Nature. 356(6370)
Lipases belong to a class of esterases whose activity on triglycerides is greatly enhanced at lipid-water interfaces. This phenomenon, called interfacial activation, has a structural explanation: a hydrophobic lid, which at rest covers the catalytic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63fcc98bdca612fc9f74e7f70f52ef1a
https://pubmed.ncbi.nlm.nih.gov/1560844
https://pubmed.ncbi.nlm.nih.gov/1560844
Autor:
Chrislaine Martinez, P de Geus, Christian Cambillau, Chantal Abergel, Marc Lauwereys, Juan-Carlos Fontecilla-Camps
Publikováno v:
Journal of molecular biology. 215(2)
Recombinant cutinase from Fusarium solani pisi is expressed and excreted with very high yields in Escherichia coli cultures. Cutinase was crystallized at 20 degrees C using the vapour diffusion technique, with polyethylene glycol 6000 as precipitant.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7f1bd890e0a37c18ea1a554da38b4bfd
https://pubmed.ncbi.nlm.nih.gov/2213880
https://pubmed.ncbi.nlm.nih.gov/2213880
Autor:
Longhi, Sonia, Nicolas, Anne, Creveld, Lucia, Egmond, Maarten, Verrips, C. Theo, de Vlieg, Jakob, Martinez, Chrislaine, Cambillau, Christian
Publikováno v:
Proteins; Dec1996, Vol. 26 Issue 4, p442-458, 17p