The scientist’s investigation covers issues in Biochemistry, Formylglycine-generating enzyme, Cell biology, Cysteine and Peptide sequence. He merges Biochemistry with Fluorescence spectroscopy in his research. Bernhard Schmidt interconnects Multiple sulfatase deficiency, Gene and Active site in the investigation of issues within Formylglycine-generating enzyme.
His work carried out in the field of Cell biology brings together such families of science as Tyrosine, Lysosome, Endocytosis and Lysosomal acid phosphatase, Acid phosphatase. His Peptide sequence study integrates concerns from other disciplines, such as Amino acid and Complementary DNA. His Arylsulfatase study combines topics from a wide range of disciplines, such as Molecular biology and Arylsulfatase A.
His primary areas of investigation include Biochemistry, Molecular biology, Formylglycine-generating enzyme, Cell biology and Sulfatase. Peptide sequence, Multiple sulfatase deficiency, Endoplasmic reticulum, Mannose and Amino acid are the subjects of his Biochemistry studies. His Molecular biology research incorporates elements of RNA, Wild type, Cathepsin H and Arylsulfatase A.
His Formylglycine-generating enzyme research includes elements of Residue, Aldehyde, Arylsulfatase and Active site. His research investigates the connection between Cell biology and topics such as Endocytosis that intersect with issues in Acid phosphatase and Lysosomal acid phosphatase. His research in Cysteine intersects with topics in Conserved sequence and Serine.
Bernhard Schmidt mainly focuses on Biochemistry, Cell biology, Multiple sulfatase deficiency, Formylglycine-generating enzyme and Sulfatase. As part of the same scientific family, Bernhard Schmidt usually focuses on Cell biology, concentrating on Transmembrane protein and intersecting with Integral membrane protein, Vesicle-associated membrane protein 8, Peptide sequence and Membrane protein. Bernhard Schmidt has included themes like Internal medicine, Protein disulfide-isomerase and Endocrinology in his Multiple sulfatase deficiency study.
His Formylglycine-generating enzyme research is multidisciplinary, incorporating perspectives in Secretory protein and Endoplasmic reticulum. His Endoplasmic reticulum research incorporates themes from Secretion, Cysteine and Furin. His study focuses on the intersection of SUMF1 Gene and fields such as Compound heterozygosity with connections in the field of Molecular biology.
Bernhard Schmidt spends much of his time researching Cell biology, Translocase of the inner membrane, Biochemistry, Mitochondrial membrane transport protein and TIM/TOM complex. He has researched Cell biology in several fields, including RNA, RNA Helicase A and Helicase. Bernhard Schmidt has included themes like Saccharomyces cerevisiae and Inner membrane in his Translocase of the inner membrane study.
In his works, he conducts interdisciplinary research on Biochemistry and Niemann–Pick disease, type C. His work in the fields of Mitochondrial membrane transport protein, such as Translocase of the outer membrane, overlaps with other areas such as Intermembrane space. He combines subjects such as Isoelectric point, Phosphatase, Dephosphorylation and Lysosomal acid phosphatase, Acid phosphatase with his study of Mannose 6-phosphate receptor.
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Role of microglia and host prion protein in neurotoxicity of a prion protein fragment
David R. Brown;Bernhard Schmidt;Hans A. Kretzschmar.
Prion protein-deficient cells show altered response to oxidative stress due to decreased SOD-1 activity
David R. Brown;Walter J. Schulz-Schaeffer;Bernhard Schmidt;Hans A. Kretzschmar.
Experimental Neurology (1997)
A Novel Amino Acid Modification in Sulfatases That Is Defective in Multiple Sulfatase Deficiency
Bernhard Schmidt;Thorsten Selmer;Arnd Ingendoh;Kurt von Figurat.
Multiple Sulfatase Deficiency Is Caused by Mutations in the Gene Encoding the Human Cα-Formylglycine Generating Enzyme
Thomas Dierks;Bernhard Schmidt;Ljudmila V. Borissenko;Jianhe Peng.
Phosphorylation of microtubule-associated protein tau: identification of the site for Ca2(+)-calmodulin dependent kinase and relationship with tau phosphorylation in Alzheimer tangles.
B. Steiner;E. M. Mandelkow;J. Biernat;N. Gustke.
The EMBO Journal (1990)
Prion Protein Binds Copper within the Physiological Concentration Range
Michael L. Kramer;Hartmut D. D. Kratzin;Bernhard Schmidt;Alice Römer.
Journal of Biological Chemistry (2001)
The race-specific elicitor, NIP1, from the barley pathogen, Rhynchosporium secalis, determines avirulence on host plants of the Rrs1 resistance genotype.
M Rohe;A Gierlich;H Hermann;M Hahn.
The EMBO Journal (1995)
Highly conserved and disease‐specific patterns of carboxyterminally truncated Aβ peptides 1–37/38/39 in addition to 1–40/42 in Alzheimer's disease and in patients with chronic neuroinflammation
J. Wiltfang;H. Esselmann;M. Bibl;A. Smirnov.
Journal of Neurochemistry (2002)
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)
Guanidinoacetate methyltransferase deficiency: the first inborn error of creatine metabolism in man.
S. Stöckler;D. Isbrandt;F. Hanefeld;B. Schmidt.
American Journal of Human Genetics (1996)
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