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I. G. L. Pauli

Researcher at Katholieke Universiteit Leuven

Publications -  8
Citations -  736

I. G. L. Pauli is an academic researcher from Katholieke Universiteit Leuven. The author has contributed to research in topics: Furin & Proprotein convertase. The author has an hindex of 8, co-authored 8 publications receiving 710 citations.

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Failure of ventral closure and axial rotation in embryos lacking the proprotein convertase furin

TL;DR: The present data identify Furin as an important activator of signals responsible for ventral closure and embryonic turning as well as cardiac and endodermal marker genes that are compromised.
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Limited Redundancy of the Proprotein Convertase Furin in Mouse Liver

TL;DR: The generation and characterization of an interferon inducible Mx-Cre/loxP furin knock-out mouse model is reported and the absence of a severe phenotype raises the possibility of using furin as a local therapeutic target in the treatment of pathologies like cancer and viral infections.
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Cloning and functional expression of Dfurin2, a subtilisin-like proprotein processing enzyme of Drosophila melanogaster with multiple repeats of a cysteine motif.

TL;DR: It is shown that Dfur2 encodes an endoproteolytic enzyme with specificity for paired basic amino acid residues as, in cotransfection experiments, correct cleavage was demonstrated of the precursor of the von Willebrand factor but not of a cleavage mutant.
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cDNA sequence of a Drosophila melanogaster gene, Dfur1, encoding a protein structurally related to the subtilisin-like proprotein processing enzyme furin

TL;DR: From overlapping Dfur1 cDNA clones, a composite cDNA could be constructed and analysis of its nucleotide sequence revealed the coding sequence for a protein of 899 amino acid residues that exhibited striking sequence homology to human furin and contained the same protein domains except for the cysteine‐rich region.
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Generation of structural and functional diversity in furin-like proteins in Drosophila melanogaster by alternative splicing of the Dfur1 gene.

TL;DR: The studies indicate that the Dfur1 gene encodes structurally different subtilisin‐like proprotein processing enzymes with distinct physiological functions in Drosophila.