Zobrazeno 1 - 10
of 44
pro vyhledávání: '"Daniel TETAERT"'
Autor:
Jean Luc Desseyn, Ann Harris, Yamin Liu, Valérie Gouyer, Frédéric Gottrand, Shih Hsing Leir, Daniel Tetaert
Publikováno v:
Histochemistry and Cell Biology. 133:517-525
Gel-forming mucins are large high-molecular weight secreted O-glycoproteins responsible for the gel-properties of the mucus blanket. Five orthologous gel-forming mucins have been cloned in human and mouse. Among them, the mucin MUC6 has been less stu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0f9725f63ef21942755ff0bc6d0d341e
https://doi.org/10.1007/s00418-010-0688-8
https://doi.org/10.1007/s00418-010-0688-8
Autor:
Yves Pétillot, Benoit Soudan, Dominique Demeyer, Sylviane Hennebicq, Daniel Tetaert, Colette Richet, Jean Gagnon, Gilbert Briand, Farid Zerimech, Pierre Degand
Publikováno v:
The Journal of Peptide Research. 51:346-354
The in vitroO-glycosylation reaction of the MUCSAC mucin motif peptide, TTSAPTTS (in one-letter code), was achieved with human gastric microsomal homogenates. The analyses using capillary electrophoresis online coupled with electrospray mass spectrom
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::57602d85ea31e5a3a5eceec3556bd936
https://doi.org/10.1111/j.1399-3011.1998.tb01225.x
https://doi.org/10.1111/j.1399-3011.1998.tb01225.x
Publikováno v:
Gene. 410:215-222
Epithelial membrane-bound mucins are high molecular mass glycoproteins that may be also secreted or released into the extracellular environment. The genomic and multi-domain organizations of human large epithelial membrane-bound mucins are reviewed h
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::85950c98b92026f670c2dcb4d12a33d0
https://doi.org/10.1016/j.gene.2007.12.014
https://doi.org/10.1016/j.gene.2007.12.014
Autor:
Daniel Tetaert, Edgar Zenteno, Raúl Chávez, Georgina Alvarez, Patricia Gorocica, Pedro Hernández-Cruz, Pierre Degand, Ricardo Lascurain, Blanca Espinosa
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1760:1235-1240
Differentiation of T lymphocytes is characterized by variable expression of CD8/CD4 co-receptor molecules and changes in the glycosylation pattern. In this work, O-glycosylation was analyzed in microsomes from murine thymocytes purified with the PNA
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b5a660bb1970b282199478f60b5ae05a
https://doi.org/10.1016/j.bbagen.2006.03.024
https://doi.org/10.1016/j.bbagen.2006.03.024
Autor:
Maria Jimenez, Pedro Hernández, Gérard Vergoten, Georgina Fernández, Daniel Tetaert, Concepción Agundis, Edgar Zenteno, Henri Debray, Pierre Degand
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1674:282-290
Amaranthus leucocarpus syn. hypochondriacus lectin (ALL) has been shown to be specific for N-acetyl-D-galactosamine (GalNAc). In this work, we determined a value of 1.0 x 10(-2) M for the association constant of ALL for GalNAc, calculated using fluor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5f59633c2939228d1c40443cee5572ea
https://doi.org/10.1016/j.bbagen.2004.07.008
https://doi.org/10.1016/j.bbagen.2004.07.008
Autor:
Brian C. VanWuyckhuyse, Pierre Degand, Lawrence A. Tabak, Fred K. Hagen, Colette Richet, Gurrinder S. Bedi, Jean Gagnon, Marlene Balys, Thomas M. Beres, Daniel Tetaert, Kelly G. Ten Hagen
Publikováno v:
Journal of Biological Chemistry. 274:27867-27874
We report the cloning, expression, and characterization of a novel member of the mammalian UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (ppGaNTase) family that transfers GalNAc to a GalNAc-containing glycopeptide. Northern blot analysis r
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::531a01b926ccb20e87cd1a8a550b6fc9
https://doi.org/10.1074/jbc.274.39.27867
https://doi.org/10.1074/jbc.274.39.27867
Autor:
Colette Richet, Benoit Soudan, Arnold Boersma, Gilbert Briand, Dominique Demeyer, Sylviane Hennebicq, Daniel Tetaert, Pierre Degand
Publikováno v:
Europe PubMed Central
The in vitro N-acetylgalactosaminylation by human gastric UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases was assessed using the peptide motif GTTPSPVPTTSTTSAP, which is found naturally in the tandem repeat domains of the apomucin encoded b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef095443facb2b13ac9094a981b12d3c
https://doi.org/10.1016/s0378-4347(99)00124-3
https://doi.org/10.1016/s0378-4347(99)00124-3
Autor:
Benoit Soudan, Daniel Tetaert, Pierre Degand, Colette Richet, Sylviane Hennebicq, M.A. Vijayalakshmi, Karsten Haupt, Y Boulis
Publikováno v:
Journal of Chromatography A. 805:285-293
A method for the analysis of O-glycosylation of peptides has been developed, combining capillary electrophoretic (CE) separation and electrospray ionization mass spectrometry. Synthetic peptides with apomucin 'tandem repeat' sequences which present p
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b9fb72a6c236dc0438570b2ee36e2a9
https://doi.org/10.1016/s0021-9673(97)01303-4
https://doi.org/10.1016/s0021-9673(97)01303-4
Autor:
Arnold Boersma, Gilbert Briand, Colette Richet, Jean Gagnon, Pierre Degand, Sylviane Hennebicq, Daniel Tetaert, Benoit Soudan
Publikováno v:
Glycoconjugate Journal. 15:275-282
The present work was carried out to study the role of the peptide moiety in the addition of O-linked N-acetylgalactosamineto human apomucin using human crude microsomal homogenates from gastric mucosa (as enzyme source) and a series of peptide accept
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c9e90df40a8818dd1979d1e630daa79f
https://doi.org/10.1023/a:1006949129456
https://doi.org/10.1023/a:1006949129456
Autor:
Benoit Soudan, Michel Marraud, Alain Bac, Daniel Tetaert, Pierre Degand, Guy Boussard, Katell Rivoal, Manh Thong Cung
Publikováno v:
Letters in Peptide Science. 4:251-258
Consequences inherent to the substitution of aza-proline (AzPro) for proline in the octapeptide TTSAPTTS, representative of the tandem repeat motif present in the peptide backbone of MUC5AC mucin, were analysed in terms of conformational perturbation
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1ddd586bde777dbe1a239ae99e7cc22d
https://doi.org/10.1007/bf02442885
https://doi.org/10.1007/bf02442885