W. Schliebs

Publications84
h-index37
Citations3,427
Highly Influential Citations235
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Yarrowia lipolytica Pex20p, Saccharomyces cerevisiae Pex18p/Pex21p and mammalian Pex5pL fulfil a common function in the early steps of the peroxisomal PTS2 import pathway
TLDR
It is shown here that the early steps of protein import into peroxisomes exhibit a greater similarity than was thought previously to be the case.
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Recombinant Human Peroxisomal Targeting Signal Receptor PEX5
TLDR
Surface plasmon resonance analysis indicates that PEX5 binds to the N-terminal fragment of PEX14-(1–78) with a very high affinity in the low nanomolar range, and a pentapeptide motif that is reiterated seven times in Pex5 is proposed as a determinant for the interaction with PEX 14.
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MINOS1 is a conserved component of mitofilin complexes and required for mitochondrial function and cristae organization
TLDR
MINOS1/Mio10 is a novel constituent of the mitofilin/Fcj1 complex of the inner membrane, linking the morphology phenotype of the mutant to the activity of the mitochondrial inner membrane organizing complex.
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The peroxisomal importomer constitutes a large and highly dynamic pore
TLDR
It is demonstrated that the membrane-associated import receptor Pex5p together with its docking partner Pex14p forms a gated ion-conducting channel which can be opened to a diameter of about 9 nm by the cytosolic receptor–cargo complex.
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Recognition of a functional peroxisome type 1 target by the dynamic import receptor pex5p.
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Proteomics Characterization of Mouse Kidney Peroxisomes by Tandem Mass Spectrometry and Protein Correlation Profiling*S
TLDR
This work uses classical subcellular fractionation in combination with MS-based proteomics methodologies to characterize the proteome of mouse kidney peroxisomes and believes to have compiled the so far most comprehensive protein catalogue of mammalian per oxisomes.
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Peroxisomal matrix protein import: the transient pore model
TLDR
A mechanistic model is proposed that conceptually divides the import process into three consecutive steps: the formation of a translocation pore by the import receptor, the ubiquitylation of the import receptors, and pore disassembly/receptor recycling.
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The Di-aromatic Pentapeptide Repeats of the Human Peroxisome Import Receptor PEX5 Are Separate High Affinity Binding Sites for the Peroxisomal Membrane Protein PEX14*
TLDR
It is demonstrated that the evolutionarily conserved pentapeptide repeat motifs, WX(E/D/Q/A/S)(E/ D/Q)(F/Y), in PEX5 bind to PEX14 with high affinity, and proposed that the side chains of the aromatic amino acids are in close proximity as part of an amphipathic α-helix and together form hydrophobic anchors for binding P EX5 to individual PEX 14 molecules.
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Pex14p, more than just a docking protein.
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A double mutation at the tip of the dimer interface loop of triosephosphate isomerase generates active monomers with reduced stability.
TLDR
A monomeric double-mutation variant of TIM, expressed in Escherichia coli, purified to homogeneity, and biochemically characterized shows that RE-TIM is a monomer in solution and implies that wild type monomersic subunits have some stability and are catalytically active.
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