23 research outputs found
Exact model reduction of combinatorial reaction networks
Receptors and scaffold proteins usually possess a high number of distinct binding domains inducing the formation of large multiprotein signaling complexes. Due to combinatorial reasons the number of distinguishable species grows exponentially with the number of binding domains and can easily reach several millions. Even by including only a limited number of components and binding domains the resulting models are very large and hardly manageable. A novel model reduction technique allows the significant reduction and modularization of these models
Neutral lipid alterations in Human Herpesvirus 8-infected HUVEC cells and their possible involvement in neo-angiogenesis
Subcellular distribution of titanium in the liver after treatment with the antitumor agent titanocene dichloride
Structures of small subunit ribosomal RNAsin situ fromEscherichia coli andThermomyces lanuginosus
Ultrastructural localization of Ca2+-binding sites in the spiral limbus, the stria vascularis and Reissner's membrane of the guinea pig
Quaternary structure of the hydroxylamine oxidoreductase from Nitrosomonas europaea
The hydroxylamine oxidoreductase from Nitrosomonas europaea was prepared to apparent electrophoretic homogeneity. Electron microscopy of negatively stained preparations of the sample revealed an overall diameter of about 8.8 nm of the enzyme particle. The native structure was determined as a tetrahedron-like assembly of identical subunits exhibiting four protein masses