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Anton O. Muijsers

Researcher at University of Amsterdam

Publications -  73
Citations -  4728

Anton O. Muijsers is an academic researcher from University of Amsterdam. The author has contributed to research in topics: Cytochrome c oxidase & Cytochrome c. The author has an hindex of 37, co-authored 73 publications receiving 4602 citations. Previous affiliations of Anton O. Muijsers include Netherlands Cancer Institute.

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Prohibitins act as a membrane‐bound chaperone for the stabilization of mitochondrial proteins

TL;DR: The fact that Phb1/2 is a large multimeric complex, which provides protection of native peptides against proteolysis, suggests a functional homology with protein chaperones with respect to their ability to hold and prevent misfolding of newly synthesized proteins.
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Chitotriosidase, a chitinase, and the 39‐kDa human cartilage glycoprotein, a chitin‐binding lectin, are homologues of family 18 glycosyl hydrolases secreted by human macrophages

TL;DR: In this article, it was shown that a single amino acid substitution in the catalytic center of the 39-kDa isoform of chitotriosidase, which generates a similar sequence to that in HC gp-39, results in a loss of hydrolytic activity and creates the capacity to bind to chitin.
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Purification and characterization of human chitotriosidase, a novel member of the chitinase family of proteins.

TL;DR: The human chitotriosidase described here showed chitinolytic activity toward artificial substrates as well as chitin and may therefore be considered to be a chit inase.
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Refsum disease is caused by mutations in the phytanoyl-CoA hydroxylase gene

TL;DR: Biochemically, the finding that Refsum disease is caused by a deficiency of phytanoyl-CoA hydroxylase (PhyH), a peroxisomal protein catalyzing the first step in the α-oxidation ofphytanic acid is confirmed.
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Chemical cross-linking and mass spectrometry for protein structural modeling.

TL;DR: Efforts towards rapid and sensitive methods for protein structural characterization are described, complementing existing technologies and thought to contribute valuable tools towards future high throughput protein structure elucidation.