The scientist’s investigation covers issues in ADAM17 Protein, Molecular biology, Biochemistry, Metalloproteinase and ADAM Proteins. Roy A. Black has researched ADAM17 Protein in several fields, including Tumor necrosis factor alpha, ADAM15, ADAM9 and Cell biology. His Tumor necrosis factor alpha research integrates issues from Sheddase and Ectodomain.
His Molecular biology research is multidisciplinary, incorporating perspectives in Receptor, Protease and Cytokine. Many of his studies on Biochemistry apply to Interleukin as well. In his study, Cell activation and Kinase is inextricably linked to Transmembrane protein, which falls within the broad field of ADAM Proteins.
His primary scientific interests are in Biochemistry, Molecular biology, Metalloproteinase, Tumor necrosis factor alpha and Cell biology. The Molecular biology study combines topics in areas such as Receptor, Transmembrane protein, ADAM17 Protein and Proteolysis. His research in ADAM17 Protein tackles topics such as ADAM9 which are related to areas like ADAM10.
His primary area of study in Metalloproteinase is in the field of Disintegrin. The study incorporates disciplines such as Metalloprotease inhibitor, Cell, Sheddase and Cytokine in addition to Tumor necrosis factor alpha. His Cell biology course of study focuses on Ectodomain and Amphiregulin.
Roy A. Black spends much of his time researching Fatty acid, Biochemistry, Membrane, Amino acid and Vesicle. His Fatty acid study combines topics in areas such as Yield, Cellular life, Flocculation and Peptide. RNA and Decanoic acid are the primary areas of interest in his Biochemistry study.
His RNA research focuses on Protocell and how it relates to Prebiotic, Salt, Divalent, Biophysics and Oligonucleotide. His studies in Vesicle integrate themes in fields like Glycine and Alanine. The various areas that Roy A. Black examines in his Glycine study include Leucine, Isoleucine and Dipeptide.
His primary areas of study are Membrane, Protocell, Biochemistry, RNA and Internal medicine. His work deals with themes such as Amino acid and Fatty acid, which intersect with Membrane. His Amino acid research incorporates elements of Prebiotic, Vesicle, Biophysics, Salt and Divalent.
Roy A. Black regularly ties together related areas like Oligonucleotide in his Fatty acid studies. The concepts of his Internal medicine study are interwoven with issues in Lesion, Endocrinology, Knee Joint and Bone tissue. Micelle, Decanoic acid, Ribose and Amphiphile are fields of study that intersect with his Nucleobase research.
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A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cells
Roy A. Black;Charles T. Rauch;Carl J. Kozlosky;Jacques J. Peschon.
An Essential Role for Ectodomain Shedding in Mammalian Development
Jacques J. Peschon;Jennifer L. Slack;Pranitha Reddy;Kim L. Stocking.
A Novel Proteolytic Cleavage Involved in Notch Signaling: The Role of the Disintegrin-Metalloprotease TACE
Christel Brou;Frédérique Logeat;Neetu Gupta;Christine Bessia.
Molecular Cell (2000)
Evidence That Tumor Necrosis Factor α Converting Enzyme Is Involved in Regulated α-Secretase Cleavage of the Alzheimer Amyloid Protein Precursor
Joseph D. Buxbaum;Kang-Nian Liu;Yuxia Luo;Jennifer L. Slack.
Journal of Biological Chemistry (1998)
Viral inhibition of inflammation. Cowpox virus encodes an inhibitor of the interleukin 1β converting enzyme.
Caroline A. Ray;Roy A. Black;Shirley R. Kronheim;Teresa A. Greenstreet.
Functional Analysis of the Domain Structure of Tumor Necrosis Factor-α Converting Enzyme
Pranhitha Reddy;Jennifer L. Slack;Raymond Davis;Douglas Pat Cerretti.
Journal of Biological Chemistry (2000)
ADAMs: focus on the protease domain
Roy A Black;Judith M White.
Current Opinion in Cell Biology (1998)
Tumor Necrosis Factor-α Converting Enzyme (TACE) Regulates Epidermal Growth Factor Receptor Ligand Availability
Susan Wohler Sunnarborg;C. Leann Hinkle;Mary Stevenson;William E. Russell.
Journal of Biological Chemistry (2002)
Tumor necrosis factor-α converting enzyme
Roy A Black.
The International Journal of Biochemistry & Cell Biology (2002)
Generation of biologically active interleukin-1 beta by proteolytic cleavage of the inactive precursor.
R A Black;S R Kronheim;M Cantrell;M C Deeley.
Journal of Biological Chemistry (1988)
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