J
Jean-François Collet
Researcher at Université catholique de Louvain
Publications - 123
Citations - 6329
Jean-François Collet is an academic researcher from Université catholique de Louvain. The author has contributed to research in topics: Periplasmic space & Bacterial outer membrane. The author has an hindex of 42, co-authored 111 publications receiving 5344 citations. Previous affiliations of Jean-François Collet include University of Michigan & Katholieke Universiteit Leuven.
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Oxidative stress, protein damage and repair in bacteria
TL;DR: This Review discusses the current understanding of the reducing systems that enable bacteria to repair oxidatively damaged cysteine and methionine residues in the cytoplasm and in the bacterial cell envelope, and highlights the importance of these repair systems in bacterial physiology and virulence.
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Structure, function and mechanism of thioredoxin proteins
TL;DR: The most significant results that have contributed to the authors' knowledge regarding the structure, the function, and the mechanism of these crucial enzymes are reviewed.
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A new class of phosphotransferases phosphorylated on an aspartate residue in an amino-terminal DXDX(T/V) motif.
Jean-François Collet,Vincent Stroobant,Michel Pirard,Ghislain Delpierre,Emile Van Schaftingen +4 more
TL;DR: Phosphomannomutase and l-3-phosphoserine phosphatase belong to a new phosphotransferase family with an amino-terminal DXDX(T/V) motif that serves as an intermediate phosphoryl acceptor.
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Oxidative protein folding in bacteria
TL;DR: This work has shown that disulphide bond formation in prokaryotes is actually driven by electron transport, and two isomerases exist in Escherichia coli, DsbC and DsbG, where the membrane protein DsbD maintains these disul PHIs in their reduced and thereby active form.
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Sequence of a putative glucose 6‐phosphate translocase, mutated in glycogen storage disease type Ib
Isabelle Gerin,Maria Veiga-da-Cunha,Younes Achouri,Jean-François Collet,Emile Van Schaftingen +4 more
TL;DR: In two patients with glycogen storage disease type Ib, mutations were observed that either replaced a conserved Gly to Cys or introduced a premature stop codon, and the encoded protein is therefore most likely the glucose 6‐phosphate translocase that is functionally associated with glucose‐6-phosphatase.