L
Leo G.J. Nijtmans
Researcher at University of Amsterdam
Publications - 21
Citations - 2367
Leo G.J. Nijtmans is an academic researcher from University of Amsterdam. The author has contributed to research in topics: Cytochrome c oxidase & Respiratory chain. The author has an hindex of 17, co-authored 21 publications receiving 2286 citations. Previous affiliations of Leo G.J. Nijtmans include University College London.
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Journal ArticleDOI
Prohibitins act as a membrane‐bound chaperone for the stabilization of mitochondrial proteins
Leo G.J. Nijtmans,Liesbeth de Jong,Marta Artal Sanz,Philip J. Coates,Jan A. Berden,Jaap Willem Back,Anton O. Muijsers,Hans van der Spek,Les A. Grivell +8 more
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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Defective Remodeling of Cardiolipin and Phosphatidylglycerol in Barth Syndrome
Peter Vreken,Fredoen Valianpour,Leo G.J. Nijtmans,Les A. Grivell,Barbara Plecko,Ronald J.A. Wanders,Peter G. Barth +6 more
TL;DR: Evidence is presented that patients with the rare disorder X-linked cardioskeletal myopathy and neutropenia (Barth syndrome, MIM 302060) have a primary defect in CL and PG remodeling, and an essential factor in this important cellular process is identified for the first time.
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The mitochondrial PHB complex: roles in mitochondrial respiratory complex assembly, ageing and degenerative disease.
TL;DR: It is suggested that the original name for these proteins, the prohibitins, should be amended to reflect their roles as proteins that hold badly formed subunits, thereby keeping the nomenclature already in use but altering its meaning to reflect the proteins' true function more accurately.
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Assembly of cytochrome‐c oxidase in cultured human cells
TL;DR: The assembly of cy tochrome-c oxidase was studied in human cells cultured in the presence of inhibitors of mitochondrial or cytosolic protein synthesis and subsequent western blots were developed with monoclonal antibodies against specific subunits of cytochrome- c oxidase.
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A structure for the yeast prohibitin complex: Structure prediction and evidence from chemical crosslinking and mass spectrometry.
Jaap Willem Back,Marta Artal Sanz,Luitzen de Jong,Leo J. de Koning,Leo G.J. Nijtmans,Chris G. de Koster,Les A. Grivell,Hans van der Spek,Anton O. Muijsers +8 more
TL;DR: A chaperone‐like function in holding and assembling newly synthesized mitochondrial polypeptide chains has been proposed, and a circular palisade‐like arrangement of the building blocks projecting into the intermembrane space is postulated.