Jan P. Kraus focuses on Cystathionine beta synthase, Biochemistry, Homocystinuria, Molecular biology and Genetics. The Cystathionine beta synthase study combines topics in areas such as Internal medicine, Homocysteine and Endocrinology. His research in Enzyme, Pyridoxal, Heme, cDNA library and Enzyme activator are components of Biochemistry.
The various areas that Jan P. Kraus examines in his Homocystinuria study include Mutation, Missense mutation, Mutant, Mutation and Cysteine. His study in Cysteine is interdisciplinary in nature, drawing from both Conformational change and Methionine. His Molecular biology study combines topics from a wide range of disciplines, such as Nucleic acid sequence, Pyruvate carboxylase, Complementary DNA, Peptide sequence and ATP synthase.
Jan P. Kraus spends much of his time researching Cystathionine beta synthase, Biochemistry, Homocystinuria, Molecular biology and Genetics. His Cystathionine beta synthase study incorporates themes from Serine, Homocysteine and ATP synthase. His Homocysteine research integrates issues from Cystathionine gamma-lyase and Methionine.
His is doing research in Mutant, CBS domain, Heme, Amino acid and Transsulfuration pathway, both of which are found in Biochemistry. His Homocystinuria research includes themes of Missense mutation, Endocrinology, Internal medicine, Pyridoxine and Enzyme replacement therapy. His work carried out in the field of Molecular biology brings together such families of science as Propionyl-CoA carboxylase and Complementary DNA, Molecular cloning, Gene, Peptide sequence.
Cystathionine beta synthase, Biochemistry, Homocystinuria, Enzyme and Cysteine are his primary areas of study. The concepts of his Cystathionine beta synthase study are interwoven with issues in Homocysteine, Serine, Heme, Stereochemistry and ATP synthase. His work in Transsulfuration pathway, Mutant, CBS domain, Allosteric regulation and Transgene is related to Biochemistry.
He has researched Mutant in several fields, including Molecular biology, Protein folding and Proteasome. His Homocystinuria research incorporates elements of Endocrinology, Enzyme replacement therapy, Peptide sequence, Internal medicine and Sulfur metabolism. As a part of the same scientific family, Jan P. Kraus mostly works in the field of Enzyme, focusing on Metabolism and, on occasion, Low affinity, Hochdurchsatz screening and High-throughput screening.
His scientific interests lie mostly in Biochemistry, Cystathionine beta synthase, Enzyme, Homocystinuria and CBS domain. Jan P. Kraus interconnects Molecular biology and Hippocampus in the investigation of issues within Biochemistry. His study on Cystathionine beta synthase is covered under Cysteine.
When carried out as part of a general Enzyme research project, his work on Transsulfuration pathway is frequently linked to work in Hydrogen sulfide, therefore connecting diverse disciplines of study. Jan P. Kraus has included themes like Sulfur metabolism and Serine in his Homocystinuria study. His work in CBS domain addresses subjects such as Transsulfuration, which are connected to disciplines such as Conformational change.
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Cystathionine β‐synthase mutations in homocystinuria
Jan P. Kraus;Miroslav Janošík;Viktor Kožich;Roseann Mandell.
Human Mutation (1999)
Isolation of cDNA clones coding for human tissue factor: primary structure of the protein and cDNA.
Eleanor K. Spicer;Renata Horton;Laura Bloem;Ronald Bach.
Proceedings of the National Academy of Sciences of the United States of America (1987)
Structure of human cystathionine β-synthase: a unique pyridoxal 5′-phosphate-dependent heme protein
Markus Meier;Miroslav Janosik;Vladimir Kery;Jan P. Kraus.
The EMBO Journal (2001)
Structure and expression of a complementary DNA for the nuclear coded precursor of human mitochondrial ornithine transcarbamylase.
Arthur L. Horwich;Wayne A. Fenton;Kenneth R. Williams;Frantisek Kalousek.
Science (1984)
Cystathionine β-Synthase: Structure, Function, Regulation, and Location of Homocystinuria-causing Mutations
Edith Wilson Miles;Jan P. Kraus.
Journal of Biological Chemistry (2004)
Transsulfuration depends on heme in addition to pyridoxal 5'-phosphate. Cystathionine beta-synthase is a heme protein.
V Kery;G Bukovska;J P Kraus.
Journal of Biological Chemistry (1994)
The molecular basis of homocystinuria due to cystathionine beta-synthase deficiency in Italian families, and report of four novel mutations.
G Sebastio;M P Sperandeo;M Panico;R de Franchis.
American Journal of Human Genetics (1995)
Molecular cloning and nucleotide sequence of cDNAs encoding the precursors of rat long chain acyl-coenzyme A, short chain acyl-coenzyme A, and isovaleryl-coenzyme A dehydrogenases. Sequence homology of four enzymes of the acyl-CoA dehydrogenase family.
Y Matsubara;Y Indo;E Naito;H Ozasa.
Journal of Biological Chemistry (1989)
Analysis of human chromosome 21: correlation of physical and cytogenetic maps; gene and CpG island distributions.
Katheleen Gardiner;Michel Horisberger;Jan Kraus;Umadevi Tantravahi.
The EMBO Journal (1990)
Regulation of human cystathionine beta-synthase by S-adenosyl-L-methionine: evidence for two catalytically active conformations involving an autoinhibitory domain in the C-terminal region.
Miroslav Janošík;Vladimír Kery;Mette Gaustadnes;Kenneth N. Maclean.
Biochemistry (2001)
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