What is he best known for?
The fields of study he is best known for:
Daniel D. Billadeau mainly focuses on Cell biology, Signal transduction, Cancer research, Receptor and T cell.
His Cell biology study frequently links to other fields, such as Immunological synapse.
His Cancer research research integrates issues from Gene silencing, Epigenetics, GSK-3 and Pancreatic cancer.
His research in Pancreatic cancer intersects with topics in Carcinogenesis and Cancer cell.
His work focuses on many connections between Receptor and other disciplines, such as Immune recognition, that overlap with his field of interest in Microtubule, Signalling, VAV2 and Function.
Daniel D. Billadeau has researched Actin in several fields, including Biophysics, Plasma protein binding and Cytoskeleton.
His most cited work include:
- A FAM21-Containing WASH Complex Regulates Retromer-Dependent Sorting (346 citations)
- Structure and control of the actin regulatory WAVE complex (317 citations)
- NKG2D-DAP10 triggers human NK cell–mediated killing via a Syk-independent regulatory pathway (301 citations)
What are the main themes of his work throughout his whole career to date?
His main research concerns Cell biology, Cancer research, Signal transduction, Pancreatic cancer and GSK-3.
The Cell biology study combines topics in areas such as T cell, Immunological synapse and T-cell receptor.
His T cell research includes themes of Cytotoxic T cell and Phosphorylation.
In his research on the topic of Cancer research, Cell culture is strongly related with Cell growth.
His studies deal with areas such as Carcinogenesis, SOX2, Transcription factor, Pancreas and Gemcitabine as well as Pancreatic cancer.
His work on GSK3B as part of general GSK-3 research is frequently linked to XIAP, thereby connecting diverse disciplines of science.
He most often published in these fields:
- Cell biology (53.68%)
- Cancer research (29.44%)
- Signal transduction (16.02%)
What were the highlights of his more recent work (between 2018-2021)?
- Cell biology (53.68%)
- Endosome (12.12%)
- Cancer research (29.44%)
In recent papers he was focusing on the following fields of study:
His primary scientific interests are in Cell biology, Endosome, Cancer research, Pancreatic cancer and Phosphorylation.
His Cell biology research incorporates themes from Chromatin and Endocytic recycling.
His Endosome research incorporates elements of Phenotype, Phosphatase, Membrane protein and Zebrafish.
His work deals with themes such as Protein kinase B, GSK-3, SOX2, KRAS and Fibroblast growth factor receptor, which intersect with Cancer research.
His biological study deals with issues like Gemcitabine, which deal with fields such as Oncology and Phases of clinical research.
His study in Phosphorylation is interdisciplinary in nature, drawing from both Kinase and Actin nucleation.
Between 2018 and 2021, his most popular works were:
- Endosomal PI(3)P regulation by the COMMD/CCDC22/CCDC93 (CCC) complex controls membrane protein recycling (20 citations)
- Targeting glycogen synthase kinase 3 for therapeutic benefit in lymphoma (17 citations)
- Glypican-1 and glycoprotein 2 bearing extracellular vesicles do not discern pancreatic cancer from benign pancreatic diseases (15 citations)
In his most recent research, the most cited papers focused on:
Daniel D. Billadeau spends much of his time researching Cell biology, Endosome, Cancer research, WASH complex and Membrane protein.
His work carried out in the field of Cell biology brings together such families of science as Nectin, Cell adhesion and Virus receptor.
His Endosome research is multidisciplinary, incorporating perspectives in Mutation, Pontocerebellar hypoplasia, Mutant and Zebrafish.
The various areas that Daniel D. Billadeau examines in his Cancer research study include Pancreatic cancer, Kinase, GSK-3, Pancreatic disease and Tissue microarray.
His WASH complex study incorporates themes from Vesicle, Cellular homeostasis, Organelle and Receptor recycling.
His studies in Membrane protein integrate themes in fields like Signal transducing adaptor protein, Protein tyrosine phosphatase, Phosphatase, Protein subunit and Retromer.
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