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The FEBS Journal|July 22, 2010
Misfolded endoplasmic reticulum retained subunits cause degradation of wild-type subunits of arylsulfatase A heteromersPeter Poeppel, Mekky Mohamed Abouzied, Christof Völker, et al.
The Journal of Cell Biology|July 1, 1983
Biosynthesis and transport of cathepsin D in cultured human fibroblastsV Gieselmann, R Pohlmann, A Hasilik, et al.
The Journal of Biological Chemistry|July 25, 1985
Synthesis and transport of lysosomal acid phosphatase in normal and I-cell fibroblastsP Lemansky, V Gieselmann, A Hasilik, et al.
The Biochemical Journal|August 15, 2002
N-glycosylation is required for full enzymic activity of the murine galactosylceramide sulphotransferaseMatthias Eckhardt, Simon N Fewou, Ivonne Ackermann, et al.
The Journal of Biological Chemistry|August 25, 1984
Cathepsin D and beta-hexosaminidase synthesized in the presence of 1-deoxynojirimycin accumulate in the endoplasmic reticulumP Lemansky, V Gieselmann, A Hasilik, et al.
Proteomics|June 20, 2019
Investigation of Oligodendrocyte Precursor Cell Differentiation by Quantitative ProteomicsCarmen Schoor, Nahal Brocke-Ahmadinejad, Volkmar Gieselmann, et al.
The Biochemical Journal|May 15, 1979
Recognition of human urine alpha-N-acetylglucosaminidase by rat hepatocytes. Involvement of receptors specific for galactose, mannose 6-phosphate and mannoseK Ullrich, R Basner, V Gieselmann, et al.
Developmental Medicine and Child Neurology|June 29, 2011
The natural course of gross motor deterioration in metachromatic leukodystrophyChristiane Kehrer, Gunnar Blumenstock, Volkmar Gieselmann, et al.
The International Journal of Social Psychiatry|October 30, 2018
Psychiatrists' views on different types of advance statements in mental health care in GermanyAstrid Gieselmann, Alfred Simon, Jochen Vollmann, et al.
The Biochemical Journal|August 15, 1979
Endocytosis of lysosomal enzymes by non-parenchymal rat liver cells. Comparative study of lysosomal-enzyme uptake by hepatocytes and non-parenchymal liver cellsK Ullrich, V Gieselmann, G Mersmann, et al.
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