K von Figura focuses on Biochemistry, Mannose 6-phosphate receptor, Cell biology, Mannose and Cathepsin D. Biochemistry is closely attributed to Molecular biology in his work. The study incorporates disciplines such as Receptor and Mannose 6-phosphate in addition to Mannose 6-phosphate receptor.
His research integrates issues of Osteopetrosis, Transmembrane protein, Transmembrane domain, Immunoelectron microscopy and Clathrin adaptor proteins in his study of Cell biology. His work deals with themes such as Secretion, Transferrin and Enzyme, which intersect with Mannose. His study looks at the relationship between Cathepsin D and topics such as Cathepsin, which overlap with Glycosylation.
His primary scientific interests are in Biochemistry, Mannose, Molecular biology, Mannose 6-phosphate receptor and Receptor. His study connects Cell biology and Biochemistry. In his study, Site-directed mutagenesis is strongly linked to Glycosylation, which falls under the umbrella field of Mannose.
The Molecular biology study combines topics in areas such as Gene expression, Mucopolysaccharidosis type VI, Mutation, Peptide sequence and Arylsulfatase B. His Mannose 6-phosphate receptor study contributes to a more complete understanding of Lysosome. His Lysosome study combines topics from a wide range of disciplines, such as Lysosomal acid phosphatase and Acid phosphatase.
The scientist’s investigation covers issues in Biochemistry, Mannose, Arylsulfatase A, Receptor and Formylglycine-generating enzyme. His study ties his expertise on Molecular biology together with the subject of Biochemistry. His research investigates the link between Molecular biology and topics such as Tartrate-resistant acid phosphatase that cross with problems in Bone resorption.
His study in Mannose is interdisciplinary in nature, drawing from both Endosome, Glycoprotein and Enzyme. The concepts of his Arylsulfatase A study are interwoven with issues in Cysteine, Mutant and Active site. His studies in Formylglycine-generating enzyme integrate themes in fields like Arylsulfatases, Hydrolase, Sulfation, Aldehyde and Stereochemistry.
His primary areas of study are Biochemistry, Cell biology, Mannose, Stereochemistry and Transferrin. Biochemistry is often connected to Molecular biology in his work. His Cell biology study incorporates themes from Monomeric Clathrin Assembly Proteins, Vesicular transport protein and Clathrin.
K von Figura combines subjects such as Cathepsin D, Cathepsin, Mannose 6-phosphate receptor, Receptor and Intracellular with his study of Mannose. His research on Stereochemistry also deals with topics like
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Lysosomal Enzymes and their Receptors
K von Figura;A Hasilik.
Annual Review of Biochemistry (1986)
Mice deficient for the lysosomal proteinase cathepsin D exhibit progressive atrophy of the intestinal mucosa and profound destruction of lymphoid cells.
P. Saftig;M. Hetman;W. Schmahl;K. Weber.
The EMBO Journal (1995)
Carbohydrate-deficient glycoprotein syndrome type Ib. Phosphomannose isomerase deficiency and mannose therapy.
R. Niehues;M. Hasilik;G. Alton;C. Korner.
Journal of Clinical Investigation (1998)
A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3
S Höning;I V Sandoval;K von Figura.
The EMBO Journal (1998)
Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis.
G Lukatela;N Krauss;K Theis;T Selmer.
Molecular Basis of Different Forms of Metachromatic Leukodystrophy
A Polten;A L Fluharty;C B Fluharty;J Kappler.
The New England Journal of Medicine (1991)
Biosynthesis and transport of cathepsin D in cultured human fibroblasts.
V Gieselmann;R Pohlmann;A Hasilik;K Von Figura.
Journal of Cell Biology (1983)
Possible pathways for lysosomal enzyme delivery
H. J. Geuze;J. W. Slot;G. J. A. M. Strous;A. Hasilik.
Journal of Cell Biology (1985)
Arylsulfatase A pseudodeficiency: loss of a polyadenylylation signal and N-glycosylation site
V Gieselmann;A Polten;J Kreysing;K von Figura.
Proceedings of the National Academy of Sciences of the United States of America (1989)
Targeting of a lysosomal membrane protein: a tyrosine-containing endocytosis signal in the cytoplasmic tail of lysosomal acid phosphatase is necessary and sufficient for targeting to lysosomes.
C Peters;M Braun;B Weber;M Wendland.
The EMBO Journal (1990)
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