Werner Machleidt spends much of his time researching Biochemistry, Peptide sequence, Cyanogen bromide, Molecular biology and Cystatin. His study looks at the intersection of Biochemistry and topics like Cystatin B with Cystatin A. His biological study spans a wide range of topics, including Amino acid and Neurospora crassa.
His studies in Cyanogen bromide integrate themes in fields like Edman degradation, Saccharomyces cerevisiae, Residue, Protein subunit and N,N-Dicyclohexylcarbodiimide. His research in Molecular biology intersects with topics in Plasmid, Coding region, Complementary DNA, Molecular cloning and Protein sequencing. In his work, Docking, E-64 and Fast protein liquid chromatography is strongly intertwined with Isoelectric point, which is a subfield of Papain.
The scientist’s investigation covers issues in Biochemistry, Molecular biology, Cathepsin B, Peptide sequence and Cystatin. Amino acid, Cathepsin L, Edman degradation, Papain and Cysteine are the core of his Biochemistry study. His Molecular biology research includes themes of Complementary DNA, Sequence analysis, Recombinant DNA and DNA sequencing.
The concepts of his Cathepsin B study are interwoven with issues in Cathepsin and Peptide. Werner Machleidt focuses mostly in the field of Peptide sequence, narrowing it down to matters related to Protein subunit and, in some cases, Neurospora crassa. His research on Cystatin frequently connects to adjacent areas such as Cyanogen bromide.
Biochemistry, Calpain, Cell biology, Cathepsin B and Proteases are his primary areas of study. His work is connected to Peptide, Cathepsin L, Active site, Cathepsin O and Papain, as a part of Biochemistry. His research combines Peptide sequence and Cathepsin L.
His study in Papain is interdisciplinary in nature, drawing from both Cysteine and Cystatin. His Calpain study combines topics from a wide range of disciplines, such as Apoptosis, Protein subunit and Recombinant DNA. His study looks at the intersection of Cathepsin B and topics like Cathepsin with Extracellular matrix and HaCaT.
Werner Machleidt focuses on Cell biology, Cathepsin, Cathepsin S, Cathepsin D and Cathepsin B. His Cell biology research incorporates themes from Proteases, Secretion, Calpain and Recombinant DNA. The study incorporates disciplines such as Apoptosis, Cytochrome c, Caspase, Bcl-2 family and Programmed cell death in addition to Calpain.
Werner Machleidt works mostly in the field of Cathepsin, limiting it down to concerns involving Extracellular matrix and, occasionally, Plasma protein binding, Integrin, Cell adhesion and RGD motif. His Cathepsin S research includes elements of Molecular biology and Cell culture. He interconnects Cell fractionation, Cytoplasm, Subcellular localization and Protein subunit in the investigation of issues within Ionomycin.
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Nomenclature and classification of the proteins homologous with the cysteine-proteinase inhibitor chicken cystatin.
A J Barrett;H Fritz;A Grubb;S Isemura.
Biochemical Journal (1986)
SopE and SopE2 from Salmonella typhimurium Activate Different Sets of RhoGTPases of the Host Cell
Andrea Friebel;Heiko Ilchmann;Martin Aepfelbacher;Kristin Ehrbar.
Journal of Biological Chemistry (2001)
Surface cathepsin B protects cytotoxic lymphocytes from self- destruction after degranulation
Kithiganahalli N. Balaji;Norbert Schaschke;Werner Machleidt;Marta Catalfamo.
Journal of Experimental Medicine (2002)
Identification of the probable inhibitory reactive sites of the cysteine proteinase inhibitors human cystatin C and chicken cystatin.
Magnus Abrahamson;Anka Ritonja;Molly A Brown;Anders Grubb.
Journal of Biological Chemistry (1987)
Products of mitochondrial protein synthesis in Neurospora crassa. Determination of equimolar amounts of three products in cytochrome oxidase on the basis of amino-acid analysis.
Walter Sebald;Werner Machleidt;Joachim Otto.
FEBS Journal (1973)
Ionomycin-activated calpain triggers apoptosis. A probable role for Bcl-2 family members.
Shirley Gil-Parrado;Amaury Fernández-Montalván;Irmgard Assfalg-Machleidt;Oliver Popp.
Journal of Biological Chemistry (2002)
The acid-stable proteinase inhibitor of human mucous secretions (HUSI-I, antileukoprotease): Complete amino acid sequence as revealed by protein and cDNA sequencing and structural homology to whey proteins and Red Sea turtle proteinase inhibitor
Ursula Seemüller;Marianne Arnhold;Hans Fritz;Karin Wiedenmann.
FEBS Letters (1986)
Human cystatin, a new protein inhibitor of cysteine proteinases.
Jože Brzin;Tatjana Popovič;Vito Turk;Ursula Borchart.
Biochemical and Biophysical Research Communications (1984)
Mechanism of inhibition of papain by chicken egg white cystatin. Inhibition constants of N-terminally truncated forms and cyanogen bromide fragments of the inhibitor.
Werner Machleidt;Werner Machleidt;Ulrich Thiele;Ulrich Thiele;Bernd Laber;Bernd Laber;Irmgard Assfalg-Machleidt;Irmgard Assfalg-Machleidt.
FEBS Letters (1989)
Aminopropyl glass and its p-phenylene diisothiocyanate derivative, a new support in solid-phase Edman degradation of peptides and proteins
Elmar Wachter;Werner Machleidt;Helmut Hofner;Joachim Otto.
FEBS Letters (1973)
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