W
Wilbert H.M. Heijne
Researcher at Laboratory of Molecular Biology
Publications - 11
Citations - 2500
Wilbert H.M. Heijne is an academic researcher from Laboratory of Molecular Biology. The author has contributed to research in topics: Toxicogenomics & Gene expression. The author has an hindex of 11, co-authored 11 publications receiving 2414 citations. Previous affiliations of Wilbert H.M. Heijne include Wageningen University and Research Centre.
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Journal Article
The major facilitator superfamily.
Milton H. Saier,Beatty Jt,André Goffeau,Kevin T. Harley,Wilbert H.M. Heijne,Huang Sc,Donald L. Jack,Jähn Ps,Lew K,Jun Liu,Stephanie S. Pao,Ian T. Paulsen,Tsai-Tien Tseng,Virk Ps +13 more
TL;DR: Evidence is presented substantiating the proposal that an internal tandem gene duplication event gave rise to a primordial MFS protein before divergence of the family members.
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Toxicogenomics of bromobenzene hepatotoxicity: a combined transcriptomics and proteomics approach
TL;DR: This work indicates that transcriptomics and proteomics technologies are complementary to each other and provide new possibilities in molecular toxicology.
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Profiles of Metabolites and Gene Expression in Rats with Chemically Induced Hepatic Necrosis
Wilbert H.M. Heijne,Robert-Jan A. N. Lamers,Peter J. van Bladeren,John P. Groten,Joop H. J. van Nesselrooij,Ben van Ommen +5 more
TL;DR: This integrated analysis of hepatic transcriptomics and plasma metabolomics was able to more sensitively detect changes related to hepatotoxicity and discover novel markers, including apoptosis and changes in glycolysis and amino acid metabolism.
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Bromobenzene-Induced Hepatotoxicity at the Transcriptome Level
Wilbert H.M. Heijne,Angela L. Slitt,T. Peter J. Van Bladeren,John P. Groten,Curtis D. Klaassen,Rob H. Stierum,Ben van Ommen +6 more
TL;DR: Recovery of the liver was suggested in response to BB by the altered expression of genes involved in protein synthesis and cytoskeleton rearrangement.
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Subsite Mapping of Aspergillus niger Endopolygalacturonase II by Site-directed Mutagenesis
TL;DR: To assess the subsites involved in substrate binding in Aspergillus niger endopolygalacturonase II, residues located in the potential substrate binding cleft stretching along the enzyme from the N to the C terminus were subjected to site-directed mutagenesis and established that the substrate binds with the nonreducing end toward the N terminus of the enzyme.