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Yves J. M. Bollen
Researcher at VU University Amsterdam
Publications - 19
Citations - 930
Yves J. M. Bollen is an academic researcher from VU University Amsterdam. The author has contributed to research in topics: Flavodoxin & Membrane protein. The author has an hindex of 13, co-authored 19 publications receiving 857 citations. Previous affiliations of Yves J. M. Bollen include Wageningen University and Research Centre.
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Journal ArticleDOI
Lost in Transition: Start-Up of Glycolysis Yields Subpopulations of Nongrowing Cells
Johan H. van Heerden,Johan H. van Heerden,Johan H. van Heerden,Meike T. Wortel,Meike T. Wortel,Meike T. Wortel,Frank J. Bruggeman,Frank J. Bruggeman,Joseph J. Heijnen,Yves J. M. Bollen,Robert Planqué,Josephus Hulshof,Tom O'Toole,S. Aljoscha Wahl,Bas Teusink,Bas Teusink,Bas Teusink +16 more
TL;DR: How cell fate can be determined by glycolytic dynamics combined with cell heterogeneity purely at the metabolic level is revealed, extending fundamental knowledge of this central pathway that is dysfunctional in diseases such as diabetes and cancer.
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Last in, first out: the role of cofactor binding in flavodoxin folding.
TL;DR: The influence of the flavin mononucleotide (FMN) cofactor on the global stability and folding kinetics of Azotobacter vinelandii holoflavodoxin is reported.
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Formation of on- and off-pathway intermediates in the folding kinetics of Azotobacter vinelandii apoflavodoxin.
TL;DR: The folding kinetics of the 179-residue Azotobacter vinelandii apoflavodoxin, which has an alpha-beta parallel topology, have been followed by stopped-flow experiments monitored by fluorescence intensity and anisotropy and it is shown that the intermediate that populates during refolding is off-pathway.
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MreB-Dependent Organization of the E. coli Cytoplasmic Membrane Controls Membrane Protein Diffusion
TL;DR: This work uses single-molecule fluorescence microscopy and three-dimensional quantitative analyses in live Escherichia coli to demonstrate that its cytoplasmic membrane contains microdomains with distinct physical properties that depend on the integrity of the MreB cytoskeleton network underneath the membrane.
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The folding energy landscape of apoflavodoxin is rugged: Hydrogen exchange reveals nonproductive misfolded intermediates
TL;DR: Four PUFs of the relatively large apoflavodoxin are identified, and at least three of them are partially misfolded conformations, which suggest that they are on a dead-end folding route that starts from unfolded apof Lavodoxin and does not continue all of the way to native protein.