What is he best known for?
The fields of study he is best known for:
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.
His most cited work include:
- Nomenclature and classification of the proteins homologous with the cysteine-proteinase inhibitor chicken cystatin. (281 citations)
- SopE and SopE2 from Salmonella typhimurium Activate Different Sets of RhoGTPases of the Host Cell (188 citations)
- Ionomycin-activated calpain triggers apoptosis. A probable role for Bcl-2 family members. (182 citations)
What are the main themes of his work throughout his whole career to date?
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.
He most often published in these fields:
- Biochemistry (63.85%)
- Molecular biology (23.85%)
- Cathepsin B (23.08%)
What were the highlights of his more recent work (between 2000-2019)?
- Biochemistry (63.85%)
- Calpain (7.69%)
- Cell biology (4.62%)
In recent papers he was focusing on the following fields of study:
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.
Between 2000 and 2019, his most popular works were:
- SopE and SopE2 from Salmonella typhimurium Activate Different Sets of RhoGTPases of the Host Cell (188 citations)
- Ionomycin-activated calpain triggers apoptosis. A probable role for Bcl-2 family members. (182 citations)
- Surface cathepsin B protects cytotoxic lymphocytes from self- destruction after degranulation (182 citations)
In his most recent research, the most cited papers focused on:
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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