Poolman, Bert (Berend), 1959-
Poolman, Berend
Poolman, B.
Bert Poolman
Poolman, Bert
VIAF ID: 217149106185068491434 ( Personal )
Permalink: http://viaf.org/viaf/217149106185068491434
Preferred Forms
- 100 0 _ ‡a Bert Poolman
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- 100 1 _ ‡a Poolman, Berend
- 100 1 _ ‡a Poolman, Berend
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4xx's: Alternate Name Forms (5)
Works
Title | Sources |
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Bacterial mechanosensitive ion channels : taking advantage of homologues | |
binding specificity of OppA determines the selectivity of the oligopeptide ATP-binding cassette transporter | |
Cellular homeostasis of Escherichia coli probed by super-resolution microscopy | |
Control over translocation across the lipid bilayer via an engineered channel protein | |
Energy transducing processes in growing and starving lactic acid Streptococci | |
How do spores wake up? Proteins involved in the first stages of spore germination | |
Import to the inner nuclear membrane : a structural perspective | |
Initiation rites in molecular biology | |
Kinetics, dynamics and localization of basic amino acid transporters in Saccharomyces cerevisiae | |
Mechanosensation at the molecular level : a study of a bacterial channel | |
Membrane protein targeting to the ouskirts of the endoplasmic reticulum | |
On the mechanism of proton-coupled transport by the maltose permease of Saccharomyces cerevisiae | |
On the mechanism of transport of inner nuclear membrame proteins | |
On the regulation of the metabolic shift and protein synthesis in Lactococcus Lactis | |
Papers presented at the Third Symposium on Lactic Acid Bacteria - Genetics, Metabolism and Applications, Wageningen, The Netherlands, 17-21 September 1990 | |
Quantification of macromolecular crowding and ionic strenght in living cells | |
Selectivity of the yeast Nuclear Pore Complex - Probing transport in vivo | |
Structural and functional diversity of substrate-binding domains in ABC importers | |
Synthetische biologie : de mens als schepper? | |
Translocation across biological membranes: activity, structure and regulation of transporters | |
Tuning the lipid bilayer : the influence of small molecules on domain formation and membrane fusion |