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Sulfation of Tyr1680 of human blood coagulation factor VIII is essential for the interaction of factor VIII with von Willebrand factor.
- A. Leyte, H. V. van Schijndel, +4 authors J. V. van Mourik
- Chemistry, Medicine
- The Journal of biological chemistry
- 15 January 1991
The acidic region of the Factor VIII light chain was studied with regard to structural requirements for the formation of a functional von Willebrand factor (vWF)-binding site. Factor VIII mutants… Expand
Recombinant human acid alpha-glucosidase: high level production in mouse milk, biochemical characteristics, correction of enzyme deficiency in GSDII KO mice.
Glycogen storage disease type II (GSDII) is caused by lysosomal acid alpha-glucosidase deficiency. Patients have a rapidly fatal or slowly progressive impairment of muscle function. Enzyme… Expand
Spectinomycin interacts specifically with the residues G1064 and C1192 in 16S rRNA, thereby potentially freezing this molecule into an inactive conformation.
- M. Brink, G. Brink, M. Verbeet, H. D. de Boer
- Biology, Medicine
- Nucleic acids research
- 11 February 1994
The upper stem of helix 34, consisting of the base-paired sequences C1063G1064U1065 and A1191C1192G1193, is suggested to be involved in the binding of spectinomycin. In E. coli 16S rRNA, each of the… Expand
Generalized glycogen storage and cardiomegaly in a knockout mouse model of Pompe disease.
- A. Bijvoet, E. V. D. van de Kamp, +8 authors A. T. van der Ploeg
- Medicine, Biology
- Human molecular genetics
Glycogen storage disease type II (GSDII; Pompe disease), caused by inherited deficiency of acid alpha-glucosidase, is a lysosomal disorder affecting heart and skeletal muscles. A mouse model of this… Expand
The interaction between human blood-coagulation factor VIII and von Willebrand factor. Characterization of a high-affinity binding site on factor VIII.
- A. Leyte, M. Verbeet, T. Brodniewicz-Proba, J. V. van Mourik, K. Mertens
- Chemistry, Medicine
- The Biochemical journal
- 1 February 1989
The interaction between human Factor VIII and immobilized multimeric von Willebrand Factor (vWF) was characterized. Equilibrium binding studies indicated the presence of multiple classes of Factor… Expand
Inhibition of human coagulation factor VIII by monoclonal antibodies. Mapping of functional epitopes with the use of recombinant factor VIII fragments.
The epitopes of four monoclonal antibodies against coagulation Factor VIII were mapped with the use of recombinant DNA techniques. Full-length Factor VIII cDNA and parts thereof were inserted into… Expand
Role of the Surface-Exposed and Copper-Coordinating Histidine in Blue Copper Proteins: The Electron-Transfer and Redox-Coupled Ligand Binding Properties of His117Gly Azurin
In many reduced blue copper proteins the C-terminal surface-exposed active-site histidine protonates at low pH and dissociates from the Cu atom. In this state, the proteins exhibit high reduction… Expand
Molecular cloning of the rDNA of Saccharomyces rosei and comparison of its transcription initiation region with that of Saccharomyces carlsbergensis.
- M. Verbeet, J. Klootwijk, H. van Heerikhuizen, R. Fontijn, E. Vreugdenhil, R. J. Planta
- Biology, Medicine
- 1 July 1983
We have cloned one complete repeating unit of rDNA from Saccharomyces rosei and determined its physical and genetic organization. Heteroduplex analysis of the rDNA units from S. rosei and S.… Expand
Specialized ribosomes: highly specific translation in vivo of a single targetted mRNA species.
In previous studies [Hui and de Boer, Proc. Natl. Acad. Sci. USA 84 (1987) (1987) 4762-4766; Hui et al., Methods Enzymol. 153 (1987) 432-452], it was shown that efficient translation of the human… Expand
The organization of gene in yeast mitochondrial DNA
- J. P. M. Sanders, C. Heyting, M. Verbeet, F. Meijlink, P. Borst
- Molecular and General Genetics MGG
Summary1)We have constructed independent physical maps of the mtDNAs from three different wild-type Saccharomyces strains by double-digestion analysis and hybridization analysis, using restriction… Expand