Richard L. Stevens mainly investigates Molecular biology, Mast cell, Biochemistry, Immunology and Proteases. His work deals with themes such as Interleukin 3, Cell culture, Gene, Recombinant DNA and Histamine, which intersect with Molecular biology. The various areas that Richard L. Stevens examines in his Mast cell study include Cellular differentiation, Protease, Connective tissue, Interleukin 33 and Degranulation.
His Biochemistry study frequently intersects with other fields, such as Immunoglobulin E. His work in the fields of Immunology, such as Inflammation, Eosinophil and Tryptase, overlaps with other areas such as Population. Richard L. Stevens interconnects Serine, Receptor, Serglycin, Cell biology and Granule in the investigation of issues within Proteases.
His scientific interests lie mostly in Molecular biology, Mast cell, Biochemistry, Cell biology and Immunology. His studies examine the connections between Molecular biology and genetics, as well as such issues in Histamine, with regards to Prostaglandin D2 and Fibroblast. His Mast cell research is multidisciplinary, relying on both Proteases, Protease, Connective tissue, Interleukin 33 and Degranulation.
His study in Biochemistry focuses on Chondroitin sulfate, Glycosaminoglycan, Proteoglycan, Enzyme and Arylsulfatase A. His biological study spans a wide range of topics, including Sulfation and Heparin. As a part of the same scientific study, Richard L. Stevens usually deals with the Cell biology, concentrating on Immune system and frequently concerns with Natural killer cell.
His primary areas of study are Immunology, Mast cell, Cell biology, Tryptase and Molecular biology. The concepts of his Immunology study are interwoven with issues in COPD and Lung. His Mast cell research is mostly focused on the topic Chymase.
Richard L. Stevens has included themes like Interleukin 33, Innate immune system, Biochemistry and Cytokine in his Cell biology study. The study incorporates disciplines such as Serine protease, Colitis, Proteases, Proteoglycan and Matrix metalloproteinase in addition to Tryptase. The Molecular biology study combines topics in areas such as Protease, Guanine nucleotide exchange factor, Signal transduction, Serglycin and Gene.
The scientist’s investigation covers issues in Immunology, Tryptase, Mast cell, Inflammation and Proteases. His Tryptase study integrates concerns from other disciplines, such as Serine protease, Colitis, Pathogenesis, Lung and Proinflammatory cytokine. His Mast cell research includes themes of Molecular biology, Elastase, Protease and Cell biology.
Richard L. Stevens interconnects Gene and TMPRSS6 in the investigation of issues within Molecular biology. He combines subjects such as Biochemistry and Cytokine with his study of Cell biology. His Proteases study deals with TRANSMEMBRANE TRYPTASE intersecting with Immunoglobulin E, Cathepsin G, Serglycin, Granzyme B and Proteoglycan.
This overview was generated by a machine learning system which analysed the scientist’s body of work. If you have any feedback, you can contact us here.
The Importance of Diagnostic Cytogenetics on Outcome in AML: Analysis of 1,612 Patients Entered Into the MRC AML 10 Trial
David Grimwade;Helen Walker;Fiona Oliver;Keith Wheatley.
Blood (1998)
Human eosinophils have prolonged survival, enhanced functional properties, and become hypodense when exposed to human interleukin 3.
M E Rothenberg;W F Owen;D S Silberstein;J Woods.
Journal of Clinical Investigation (1988)
Heparin is essential for the storage of specific granule proteases in mast cells
Donald E. Humphries;Guang W. Wong;Daniel S. Friend;Michael F. Gurish.
Nature (1999)
Recent advances in the cellular and molecular biology of mast cells
Richard L. Stevens;K. Frank Austen.
Immunology Today (1989)
Interleukin 3: A differentiation and growth factor for the mouse mast cell that contains chondroitin sulfate E proteoglycan.
E Razin;J N Ihle;D Seldin;J M Mencia-Huerta.
Journal of Immunology (1984)
Regulation of human eosinophil viability, density, and function by granulocyte/macrophage colony-stimulating factor in the presence of 3T3 fibroblasts.
W F Owen;M E Rothenberg;D S Silberstein;J C Gasson.
Journal of Experimental Medicine (1987)
Coculture of interleukin 3-dependent mouse mast cells with fibroblasts results in a phenotypic change of the mast cells.
F Levi-Schaffer;K F Austen;P M Gravallese;R L Stevens.
Proceedings of the National Academy of Sciences of the United States of America (1986)
IL-5-dependent conversion of normodense human eosinophils to the hypodense phenotype uses 3T3 fibroblasts for enhanced viability, accelerated hypodensity, and sustained antibody-dependent cytotoxicity.
M E Rothenberg;J Petersen;R L Stevens;D S Silberstein.
Journal of Immunology (1989)
Culture from mouse bone marrow of a subclass of mast cells possessing a distinct chondroitin sulfate proteoglycan with glycosaminoglycans rich in N-acetylgalactosamine-4,6-disulfate.
E Razin;R L Stevens;F Akiyama;K Schmid.
Journal of Biological Chemistry (1982)
Human ecalectin, a variant of human galectin-9, is a novel eosinophil chemoattractant produced by T lymphocytes
Ryoji Matsumoto;Hiroyuki Matsumoto;Masako Seki;Mitsumi Hata.
Journal of Biological Chemistry (1998)
If you think any of the details on this page are incorrect, let us know.
We appreciate your kind effort to assist us to improve this page, it would be helpful providing us with as much detail as possible in the text box below:
Harvard Medical School
University of New South Wales
Brigham and Women's Hospital
Brigham and Women's Hospital
Hebrew University of Jerusalem
Cincinnati Children's Hospital Medical Center
University of California, San Francisco
Boston University
University of California, Los Angeles
University of Technology Sydney
Carnegie Mellon University
University of Missouri
University of Amsterdam
The University of Texas at Austin
IBM (United States)
University of Helsinki
Norwegian University of Science and Technology
University of Oxford
Australian National University
KU Leuven
Nagoya City University
University of Arizona
University of Bremen
Technical University of Madrid
University of Vienna
IMT Institute for Advanced Studies Lucca