What is he best known for?
The fields of study he is best known for:
His main research concerns Biochemistry, Mannose 6-phosphate receptor, Enzyme, Cell biology and Mannose.
He frequently studies issues relating to Molecular biology and Biochemistry.
His Mannose 6-phosphate receptor research focuses on Golgi apparatus and how it relates to Galactosyltransferase, Immunoelectron microscopy and Vesicle.
The study incorporates disciplines such as Enzyme Precursors, Intracellular and Phosphorylation in addition to Enzyme.
His Cell biology research is multidisciplinary, incorporating perspectives in Transforming growth factor beta and Cell division.
His Mannose study deals with Receptor intersecting with Antibody.
His most cited work include:
- Lysosomal Enzymes and their Receptors (797 citations)
- BIOSYNTHESIS OF LYSOSOMAL ENZYMES IN FIBROBLASTS. SYNTHESIS AS PRECURSORS OF HIGHER MOLECULAR WEIGHT (652 citations)
- Biosynthesis of lysosomal enzymes in fibroblasts. Phosphorylation of mannose residues. (337 citations)
What are the main themes of his work throughout his whole career to date?
Andrej Hasilik mostly deals with Biochemistry, Enzyme, Cathepsin D, Molecular biology and Mannose 6-phosphate receptor.
His study in Biochemistry concentrates on Mannose, Biosynthesis, Lysosome, Golgi apparatus and Secretion.
Andrej Hasilik interconnects Enzyme Precursors, Oligosaccharide and Intracellular in the investigation of issues within Enzyme.
His Cathepsin D research also works with subjects such as
- Cell biology together with Immunoelectron microscopy,
- Immunology which intersects with area such as Crevicular fluid.
His Molecular biology study incorporates themes from Immunoprecipitation, Lysozyme, Cathepsin O, Cathepsin A and Cathepsin H.
His research integrates issues of Alkaline phosphatase, Phosphodiester bond, Endocytosis, Phosphorylation and Membrane protein in his study of Mannose 6-phosphate receptor.
He most often published in these fields:
- Biochemistry (73.46%)
- Enzyme (38.89%)
- Cathepsin D (36.42%)
What were the highlights of his more recent work (between 2000-2015)?
- Biochemistry (73.46%)
- Cathepsin D (36.42%)
- Cell biology (16.67%)
In recent papers he was focusing on the following fields of study:
Andrej Hasilik mainly focuses on Biochemistry, Cathepsin D, Cell biology, Enzyme and Membrane protein.
His study in Biochemistry focuses on Lysosome, Membrane, Serglycin, Chondroitin sulfate and U937 cell.
The various areas that he examines in his Cathepsin D study include Protease, Pepstatin, Immunology, Molecular biology and Myeloperoxidase.
The concepts of his Cell biology study are interwoven with issues in Cathepsin, Peptide transport, Major histocompatibility complex and Transporter associated with antigen processing.
His biological study spans a wide range of topics, including Cancer research, Disease and Glycosphingolipid.
His Membrane protein study integrates concerns from other disciplines, such as Proteome, Mannose 6-phosphate receptor, Proteomics and Organelle.
Between 2000 and 2015, his most popular works were:
- Integral and Associated Lysosomal Membrane Proteins (142 citations)
- The proteome of lysosomes (138 citations)
- Purified recombinant human prosaposin forms oligomers that bind procathepsin D and affect its autoactivation. (76 citations)
In his most recent research, the most cited papers focused on:
His primary areas of investigation include Cathepsin D, Cell biology, Biochemistry, Cathepsin and Immunology.
Andrej Hasilik interconnects Molecular biology and Pepstatin in the investigation of issues within Cathepsin D.
A large part of his Cell biology studies is devoted to Endoplasmic reticulum.
His Membrane protein, Biotinylation and Binding site study are his primary interests in Biochemistry.
His work focuses on many connections between Biotinylation and other disciplines, such as Immunocytochemistry, that overlap with his field of interest in Enzyme.
The study incorporates disciplines such as Mannose 6-phosphate receptor and Mitochondrial membrane transport protein in addition to Integral membrane protein.
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