نتائج البحث - "Role and putative double function of P-glycoprotein as multidrug transporter and chloride channel in the kidney"

1

Expression and immunolocalization of multidrug resistance protein 2 in small intestine

المؤلفون: Anita Hartog, Frans G. M. Russel, Carel H. van Os, René J. M. Bindels, Rémon A. M. H. Van Aubel

المصدر: European Journal of Pharmacology, 400, 195-198
European Journal of Pharmacology, 400, 2-3, pp. 195-198

مصطلحات موضوعية: Moleculaire en funktionele karakterisering van Ca2+-kanalen in enterocyten, Brush border, Duodenum, Anion Transport Proteins, Guinea Pigs, Immunoblotting, Biology, Antibodies, Antibody Specificity, Intestine, Small, medicine, Animals, Fluorescent Antibody Technique, Indirect, Pharmacology, Kidney, Role and putative double function of P-glycoprotein as multidrug transporter and chloride channel in the kidney, Microvilli, Rol en vermeende dubbelfunctie van P-glycoproteïne als multifarmacontransporter en chloridekanaal in de nier, Villus Tip, Multidrug resistance-associated protein 2, Transporter, Molecular biology, Molecular and functional characterization of Ca2+ channels in enterocytes, Small intestine, Rats, medicine.anatomical_structure, Membrane, Biochemistry, Rabbits, Efflux, Carrier Proteins

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::514f64e915897c475846f45106d8f8a2
https://hdl.handle.net/2066/260170

View record from ScienceDirect

2

Molecular cloning and expression of a cyclic AMP activated chloride conductance regulator : a novel ATP-binding cassette transporter

المؤلفون: Frans G. M. Russel, Peter M.T. Deen, M.A. van Kuijck, Andreas E. Busch, René J. M. Bindels, R.A.M.H. van Aubel, Florian Lang, C.H. van Os

المصدر: Proceedings of the National Academy of Sciences USA, 93, 5401-5406
Proceedings of the National Academy of Science USA, 93, 11, pp. 5401-5406
Proceedings of the National Academy of Science USA, 93, 5401-5406. Natl acad sciences
Proceedings of the National Academy of Science USA, 93, 5401-5406
Proceedings of the National Academy of Science USA, 93, pp. 5401-5406
Proceedings of the National Academy of Sciences USA, 9, pp. 5401-5406
Proceedings of the National Academy of Sciences USA, 93, pp. 5401-5406
Proceedings of the National Academy of Sciences USA, 9, 5401-5406

مصطلحات موضوعية: Cell Membrane Permeability, Patch-Clamp Techniques, algemeen [Geneeskunde], Physiology, Regulation of salt and water reabsorption in the renal collecting duct, ATP-binding cassette transporter, Kidney, Chloride, Physiology, General (Non MeSH), Polymerase Chain Reaction, General (Non MeSH), Epithelium, Protein Structure, Secondary, Medische Wetenschappen, Membrane Potentials, Kidney Concentrating Ability, Xenopus laevis, Adenosine Triphosphate, Adrenal Cortex Hormones, 1-Methyl-3-isobutylxanthine, Intestine, Small, Cloning, Molecular, Urinary Tract, GeneralLiterature_REFERENCE(e.g.,dictionaries,encyclopedias,glossaries), Cells, Cultured, Phylogeny, Niet-toepassingsgericht onderzoek, Multidisciplinary, Cultured, Hypothalamic Hormones, Reabsorption, Rol en vermeende dubbelfunctie van P-glycoproteïne als multifarmacontransporter en chloridekanaal in de nier, Niflumic acid, Niflumic Acid, Gezondheid, Geneeskunde: algemeen, Water-Electrolyte Balance, Cystic fibrosis transmembrane conductance regulator, Recombinant Proteins, Financial Economics, Cell biology, Biochemistry, Regulatie water en zouttransport in de verzamelbuis van de nier, Liver, Organ Specificity, Chloride channel, Female, Kidney Diseases, Rabbits, medicine.drug, Research Article, Logic, Cells, Molecular Sequence Data, Urogenital System, Biology, Medical sciences, Cell Physiology (Non MeSH), Chloride Channels, medicine, Animals, Humans, ATP Binding Cassette Transporter, Subfamily B, Member 1, Amino Acid Sequence, Ion transporter, Ion Transport, Role and putative double function of P-glycoprotein as multidrug transporter and chloride channel in the kidney, Sequence Homology, Amino Acid, Cell Membrane, Colforsin, Apical membrane, Blotting, Northern, Hormones, Models, Structural, biology.protein, Oocytes, ATP-Binding Cassette Transporters

وصف الملف: application/pdf

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3af54e234cfdedc5f64178a603aedf6e
https://hdl.handle.net/2066/22512

3

Molecular pharmacology of renal organic anion transporters

المؤلفون: Rosalinde Masereeuw, Rémon A. M. H. Van Aubel, Frans G. M. Russel

المصدر: ResearcherID
American Journal of Physiology : Renal Physiology, 279, pp. F216-F232
American Journal of Physiology : Renal Physiology, 279, F216-F232
Scopus-Elsevier

URL الوصول: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c71bce8eb864121ad8facf9590de10b
https://pubmed.ncbi.nlm.nih.gov/10919840

4

Multidrug resistance protein Mrp2 mediates ATP-dependent transport of classic renal organic anion p-aminohippurate

المؤلفون: Carel H. van Os, Frans G. M. Russel, Rosalinde Masereeuw, Rémon A. M. H. Van Aubel, Janny G. P. Peters

المصدر: American Journal of Physiology : Renal Physiology, 279, pp. F713-F717
ResearcherID
Scopus-Elsevier
American Journal of Physiology : Renal Physiology, 279, F713-F717

مصطلحات موضوعية: Anions, ATP Binding Cassette Transporter, Subfamily B, Time Factors, Moleculaire en funktionele karakterisering van Ca2+-kanalen in enterocyten, Physiology, ATP-binding cassette transporter, Spodoptera, Kidney, Cell Line, Adenosine Triphosphate, Animals, Epithelial polarity, biology, Role and putative double function of P-glycoprotein as multidrug transporter and chloride channel in the kidney, Membrane transport protein, Rol en vermeende dubbelfunctie van P-glycoproteïne als multifarmacontransporter en chloridekanaal in de nier, Multidrug resistance-associated protein 2, Kidney metabolism, Membrane Transport Proteins, Transporter, Biological Transport, Multidrug Resistance-Associated Protein 2, Recombinant Proteins, Molecular and functional characterization of Ca2+ channels in enterocytes, Kinetics, Biochemistry, biology.protein, Organic anion transport, p-Aminohippuric Acid, Rabbits, Multidrug Resistance-Associated Proteins, Carrier Proteins