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Fibrin-clot Formation by Extracts of Rabbit-skin Homografts
National licenceNature Publishing Group | 1964| -
Tripartite Chimeras Comprising Functional Domains Derived from the Cytosolic NADPH Oxidase Components p47^p^h^o^x, p67^p^h^o^x, and Rac1 Elicit Activator-independent Superoxide Production by Phagocyte Membranes. AN ESSENTIAL ROLE FOR ANIONIC MEMBRANE PHOSPHOLIPIDS
British Library Online Contents | 2007| -
Targeting of Rac1 to the phagocyte membrane is sufficient for the induction of NADPH oxidase assembly
British Library Online Contents | 2000| -
Yeast ARF GTPase-activating proteins with overlapping function
British Library Conference Proceedings | 1997| -
Activation of the Superoxide-Generating NADPH Oxidase by Chimeric Proteins Consisting of Segments of the Cytosolic Component p67^p^h^o^x and the Small GTPase Rac1
British Library Online Contents | 2001| -
Vitamin A-induced Rejection of Autografts and Homografts
National licenceNature Publishing Group | 1965| -
Targeting of Rac1 to the phagocyte membrane is sufficient for the induction of NADPH oxidase assembly
British Library Online Contents | 2000| -
Energy and Environmental Analysis of Wind Energy Systems
British Library Conference Proceedings | 2000| -
Mapping of Functional Domains in p47^p^h^o^x Involved in the Activation of NADPH Oxidase by "Peptide Walking"
British Library Online Contents | 1998| -
Mutational Analysis of Novel Effector Domains in Rac1 Involved in the Activation of Nicotinamide Adenine Dinucleotide Phosphate (Reduced) Oxidase
British Library Online Contents | 1998| -
Inhibition of NADPH oxidase activation by 4-(2-aminoethyl)-benzenesulfonyl fluoride and related compounds
British Library Online Contents | 1997| -
The COP9 signalosome-like complex in S. cerevisiae and links to other PCI complexes
British Library Online Contents | 2003| -
Mapping of functional domains in the p22^p^h^o^x subunit of flavocytochrome b~5~5~9 participating in the assembly of the NADPH oxidase complex by "peptide walking"
British Library Online Contents | 2002|
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