What is he best known for?
The fields of study he is best known for:
Carl P. Blobel mostly deals with Cell biology, Disintegrin, Biochemistry, Sheddase and Metalloproteinase.
His work deals with themes such as Cell adhesion, Neural cell adhesion molecule, ADAM17 Protein and ADAM10, which intersect with Cell biology.
His Sheddase research incorporates themes from Epidermal growth factor, Epidermal growth factor receptor and Cancer research.
Carl P. Blobel has researched Epidermal growth factor in several fields, including Molecular biology and Growth factor.
His biological study spans a wide range of topics, including Tumor necrosis factor alpha, Cell culture and Ectodomain.
His study explores the link between Ectodomain and topics such as ADAM9 that cross with problems in ADAM Proteins and Myoblast fusion.
His most cited work include:
- ADAMs: key components in EGFR signalling and development (902 citations)
- Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands (800 citations)
- A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. (614 citations)
What are the main themes of his work throughout his whole career to date?
His primary scientific interests are in Cell biology, Metalloproteinase, Disintegrin, Ectodomain and ADAM10.
Carl P. Blobel interconnects Molecular biology, ADAM17 Protein and Sheddase in the investigation of issues within Cell biology.
His Sheddase research focuses on subjects like Epidermal growth factor receptor, which are linked to Transforming growth factor.
His Metalloproteinase study integrates concerns from other disciplines, such as Tumor necrosis factor alpha, Cancer research and Transmembrane domain.
His work in the fields of Disintegrin, such as ADAM Proteins, intersects with other areas such as Secretory pathway.
His study in Ectodomain is interdisciplinary in nature, drawing from both Betacellulin, Epidermal growth factor, Regulator and ADAM9.
He most often published in these fields:
- Cell biology (72.95%)
- Metalloproteinase (54.11%)
- Disintegrin (41.55%)
What were the highlights of his more recent work (between 2015-2021)?
- Cell biology (72.95%)
- ADAM10 (33.33%)
- Metalloproteinase (54.11%)
In recent papers he was focusing on the following fields of study:
The scientist’s investigation covers issues in Cell biology, ADAM10, Metalloproteinase, Disintegrin and Notch signaling pathway.
Specifically, his work in Cell biology is concerned with the study of Signal transduction.
His research in ADAM10 intersects with topics in Proinflammatory cytokine, Cell signaling, Sheddase and Tumor necrosis factor alpha.
Carl P. Blobel has included themes like Cancer research and Epidermal growth factor receptor in his Metalloproteinase study.
His studies in Disintegrin integrate themes in fields like Transmembrane domain, Epidermal growth factor, Ectodomain and Transmembrane protein.
His work carried out in the field of Ectodomain brings together such families of science as Matrix metalloproteinase and ADAM9.
Between 2015 and 2021, his most popular works were:
- iRhom2 promotes lupus nephritis through TNF-α and EGFR signaling (41 citations)
- A protective Langerhans cell–keratinocyte axis that is dysfunctional in photosensitivity (26 citations)
- Structural modeling defines transmembrane residues in ADAM17 that are crucial for Rhbdf2-ADAM17-dependent proteolysis. (22 citations)
In his most recent research, the most cited papers focused on:
Carl P. Blobel mainly investigates ADAM10, Cell biology, Notch signaling pathway, Angiogenesis and Endothelium.
His ADAM10 research includes themes of Signal transduction and Immunology.
The Angiogenesis study combines topics in areas such as Cell, Downregulation and upregulation, Homeostasis and Kidney development.
His Downregulation and upregulation study which covers Autoimmunity that intersects with Metalloproteinase.
Carl P. Blobel integrates Metalloproteinase with Amyloid precursor protein secretase in his study.
His Endothelium research is multidisciplinary, relying on both Regulator and Transcriptome.
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