Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Isabelle Dewerte"'
Autor:
Saskia De Keyser, Peter Schotte, Isabelle Dewerte, Manu De Groeve, Veronique De Brabandere, Patrick Stanssens
Publikováno v:
Microbial Cell Factories
Background Over the last few decades the methylotrophic yeast Pichia pastoris has become a popular host for a wide range of products such as vaccines and therapeutic proteins. Several P. pastoris engineered strains and mutants have been developed to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3409a4109036ea9ebd5fb86c4cb1a440
http://europepmc.org/articles/PMC4897801
http://europepmc.org/articles/PMC4897801
Autor:
Roland Contreras, Nico Callewaert, Sylviane Dewaele, Stefan Ryckaert, Pieter P. Jacobs, Isabelle Dewerte
Publikováno v:
Glycobiology. 18:137-144
The establishment of a robust technology platform for the expression cloning of carbohydrate-binding proteins remains a key challenge in glycomics. Here we explore the utility of using yeast surface display (YSD) technology in the interaction-based l
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::89121a02e37865c433b5840a2e53404f
https://doi.org/10.1093/glycob/cwm131
https://doi.org/10.1093/glycob/cwm131
Autor:
Hugo Ceulemans, Mathieu Bollen, Silvia Jansen, Nico Callewaert, Maria Andries, Isabelle Dewerte
Publikováno v:
Journal of Biological Chemistry. 282:11084-11091
Autotaxin/NPP2, a secreted lysophospholipase-D, promotes cell proliferation, survival, and motility by generating the signaling molecule lysophosphatidic acid. Here we show that ectonucleotide pyrophosphatase/phosphodiesterase 2 (NPP2) is N-glycosyla
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::56d09829a7488e731c1d048d58b4e3f0
https://doi.org/10.1074/jbc.m611503200
https://doi.org/10.1074/jbc.m611503200
Autor:
Merja Penttilä, Wim Martinet, Marleen Maras, Sylviane Dewaele, Marc Claeyssens, Isabelle Dewerte, Kathleen Piens, Roland Contreras, Hans Contreras, Nico Callewaert
Publikováno v:
Maras, M, Callewaert, N, Piens, K, Claeyssens, M, Martinet, W, Dewaele, S, Contreras, H, Dewerte, I, Penttilä, M & Contreras, R 2000, ' Molecular cloning and enzymatic characterization of a Trichoderma reesei 1,2-α-D-mannosidase ', Journal of Biotechnology, vol. 77, no. 2-3, pp. 255-263 . https://doi.org/10.1016/S0168-1656(99)00222-9
A cDNA encoding 1,2-α-D-mannosidase mds1 from Trichoderma reesei was cloned. The largest open reading frame occupied 1571 bp. The predicted sequence contains 523 amino acid residues for a calculated molecular mass of 56 266 Da and shows high similar
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::45cf83bcec34f17a240325b3d26df672
https://doi.org/10.1016/s0168-1656(99)00222-9
https://doi.org/10.1016/s0168-1656(99)00222-9
Autor:
Karen De Pourcq, Nico Callewaert, Albena Vergilieva Valevska, Isabelle Dewerte, Wouter Vervecken, Annelies Van Hecke
Publikováno v:
Microbial Cell Factories, Vol 11, Iss 1, p 53 (2012)
Microbial Cell Factories
Microbial Cell Factories
Background Protein-based therapeutics represent the fastest growing class of compounds in the pharmaceutical industry. This has created an increasing demand for powerful expression systems. Yeast systems are widely used, convenient and cost-effective
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9b135b1453e2e7cb53c2e4bb3c3cda8
http://www.microbialcellfactories.com/content/11/1/53
http://www.microbialcellfactories.com/content/11/1/53
Autor:
Steven Geysens, Tiina Pakula, Isabelle Dewerte, Jaana Uusitalo, Merja Penttilä, Roland Contreras
Publikováno v:
Geysens, S, Pakula, T, Uusitalo, J, Dewerte, I, Penttilä, M & Contreras, R 2005, ' Cloning and characterization of the glucosidase II alpha subunit gene of Trichoderma reesei : A frameshift mutation results in the aberrant glycosylation profile of the hypercellulolytic strain Rut-C30 ', Applied and Environmental Microbiology, vol. 71, no. 6, pp. 2910-2924 . https://doi.org/10.1128/AEM.71.6.2910-2924.2005
We describe isolation and characterization of the gene encoding the glucosidase II alpha subunit (GIIα) of the industrially important fungus Trichoderma reesei . This subunit is the catalytic part of the glucosidase II heterodimeric enzyme involved
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6bbad1f1d15d2b4c88792458f0f5565f
https://europepmc.org/articles/PMC1151825/
https://europepmc.org/articles/PMC1151825/
Autor:
Marleen Maras, Nico Callewaert, Kathleen Piens, Marc Claeyssens, Wim Martinet, Sylviane Dewaele, Hans Contreras, Isabelle Dewerte, Merja Penttilä, Roland Contreras
Publikováno v:
VTT Technical Research Centre of Finland-PURE
Maras, M, Callewaert, N, Piens, K, Claeyssens, M, Martinet, W, Dewaele, S, Contreras, H, Dewerte, I, Penttilä, M & Contreras, R 2000, ' Molecular cloning and enzymatic characterization of a Trichoderma reesei 1,2-alfa-D-mannosidase ', Journal of Biotechnology, vol. 77, no. 2-3, pp. 255-263 .
Maras, M, Callewaert, N, Piens, K, Claeyssens, M, Martinet, W, Dewaele, S, Contreras, H, Dewerte, I, Penttilä, M & Contreras, R 2000, ' Molecular cloning and enzymatic characterization of a Trichoderma reesei 1,2-alfa-D-mannosidase ', Journal of Biotechnology, vol. 77, no. 2-3, pp. 255-263 .
A cDNA encoding 1,2-alpha-D-mannosidase mds 1 from Trichoderma reesei was cloned. The largest open reading frame occupied 1571 bp. The predicted sequence contains 523 amino acid residues for a calculated molecular mass of 56,266 Da and shows high sim
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=dedup_wf_001::ddd993c423e3e1e3a09e39ff5ae26dfb
https://cris.vtt.fi/en/publications/3d1d615e-bab5-49cb-991a-a0b2896a1621
https://cris.vtt.fi/en/publications/3d1d615e-bab5-49cb-991a-a0b2896a1621
Fishing for lectins from diverse sequence libraries by yeast surface display - An exploratory study.
Autor:
Stefan Ryckaert, Nico Callewaert, Pieter P. Jacobs, Sylviane Dewaele, Isabelle Dewerte, Roland Contreras
Publikováno v:
Glycobiology; Feb2008, Vol. 18 Issue 2, p137-137, 1p