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Frank Baas

Researcher at Leiden University Medical Center

Publications -  446
Citations -  33815

Frank Baas is an academic researcher from Leiden University Medical Center. The author has contributed to research in topics: Gene & Complement system. The author has an hindex of 93, co-authored 434 publications receiving 31187 citations. Previous affiliations of Frank Baas include Flanders Institute for Biotechnology & Academic Medical Center.

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Journal Article

Analysis of expression of cMOAT (MRP2), MRP3, MRP4, and MRP5, homologues of the multidrug resistance-associated protein gene (MRP1), in human cancer cell lines.

TL;DR: In this paper, the authors identified three new homologues of MRP1, the gene encoding the multidrug resistanceassociated protein, and cMOAT (or MRP2 ), the canalicular multispecific organic anion transporter gene.
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Exome sequencing in amyotrophic lateral sclerosis identifies risk genes and pathways

Elizabeth T. Cirulli, +70 more
- 27 Mar 2015 - 
TL;DR: A moderate-scale sequencing study aimed at increasing the number of genes known to contribute to predisposition for ALS found several known ALS genes were found to be associated, and TBK1 (the gene encoding TANK-binding kinase 1) was identified as an ALS gene.
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The Human Transcriptome Map: Clustering of Highly Expressed Genes in Chromosomal Domains

TL;DR: The Human Transcriptome Map (HPM) as mentioned in this paper is a tool to search for genes that are overexpressed or silenced in cancer using the SAGE serial analysis of gene expression.
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The human multidrug resistance-associated protein MRP is a plasma membrane drug-efflux pump.

TL;DR: It is concluded that MRP is a plasma membrane drug-efflux pump that confers drug resistance in human lung carcinoma cells by generating a subline stably transfected with an expression vector containing MRP cDNA.
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Drug export activity of the human canalicular multispecific organic anion transporter in polarized kidney MDCK cells expressing cMOAT (MRP2) cDNA.

TL;DR: It is shown that cMOAT causes transport of the organic anions S-(2,4-dinitrophenyl)-glutathione, the glutathione conjugate of ethacrynic acid, and S-(PGA1)-gluten, a substrate not shown to be transported by organic anion transporters previously.