What is he best known for?
The fields of study he is best known for:
His primary areas of study are Cell biology, Growth cone, Microtubule, Phosphorylation and GSK-3.
His Cell biology study combines topics in areas such as Amino acid and Neurotransmission.
Phillip R. Gordon-Weeks has included themes like Filopodia, Actin and Arp2/3 complex in his Growth cone study.
His Actin research includes elements of Microtubule polymerization, Biophysics, Anatomy and Microfilament.
Phillip R. Gordon-Weeks is involved in the study of Microtubule that focuses on Tubulin in particular.
His research in Phosphorylation intersects with topics in Axonogenesis, Axon and Kinase.
His most cited work include:
- Inhibition of GSK-3beta leading to the loss of phosphorylated MAP-1B is an early event in axonal remodelling induced by WNT-7a or lithium (286 citations)
- Glycogen synthase kinase 3beta phosphorylation of microtubule-associated protein 1B regulates the stability of microtubules in growth cones. (248 citations)
- The organization of F-actin and microtubules in growth cones exposed to a brain-derived collapsing factor. (247 citations)
What are the main themes of his work throughout his whole career to date?
His primary areas of investigation include Cell biology, Growth cone, Microtubule, Neuroscience and Microtubule-associated protein.
His Cell biology research is multidisciplinary, relying on both Endocrinology, Postsynaptic potential and Glycoprotein.
His studies in Growth cone integrate themes in fields like Molecular biology, Biophysics and Filopodia, Actin.
His work on Tubulin as part of general Microtubule study is frequently linked to Adenomatous polyposis coli, bridging the gap between disciplines.
His Neuroscience study incorporates themes from Synaptic plasticity and Immunoprecipitation.
His Microtubule-associated protein study combines topics from a wide range of disciplines, such as Astral microtubules and Nocodazole.
He most often published in these fields:
- Cell biology (56.36%)
- Growth cone (50.91%)
- Microtubule (28.18%)
What were the highlights of his more recent work (between 2007-2017)?
- Cell biology (56.36%)
- Growth cone (50.91%)
- Filopodia (12.73%)
In recent papers he was focusing on the following fields of study:
Phillip R. Gordon-Weeks mostly deals with Cell biology, Growth cone, Filopodia, Microtubule and Actin.
As part of his studies on Cell biology, Phillip R. Gordon-Weeks frequently links adjacent subjects like Neuron.
His research integrates issues of Axon guidance and Molecular biology in his study of Growth cone.
Phillip R. Gordon-Weeks studied Filopodia and Dendritic spine that intersect with Actin remodeling of neurons and Binding site.
The study incorporates disciplines such as Gene silencing and Cellular differentiation in addition to Microtubule.
His studies deal with areas such as Transient receptor potential channel, TRPC, Actin cytoskeleton and Bioinformatics as well as Actin.
Between 2007 and 2017, his most popular works were:
- Cytoskeletal dynamics in growth-cone steering (205 citations)
- Targeting of the F-actin-binding protein drebrin by the microtubule plus-tip protein EB3 is required for neuritogenesis (191 citations)
- DAPK-1 binding to a linear peptide motif in MAP1B stimulates autophagy and membrane blebbing (112 citations)
In his most recent research, the most cited papers focused on:
Phillip R. Gordon-Weeks spends much of his time researching Cell biology, Filopodia, Growth cone, Actin and Microtubule.
As part of his studies on Cell biology, Phillip R. Gordon-Weeks often connects relevant subjects like Amino acid.
In Filopodia, Phillip R. Gordon-Weeks works on issues like Dendritic spine, which are connected to Actin remodeling of neurons, Treadmilling, Axon guidance and Arp2/3 complex.
His Actin research incorporates elements of Cyclin-dependent kinase 5, Binding site and Motility.
His Cyclin-dependent kinase 5 study is associated with Phosphorylation.
His work deals with themes such as Signal transduction, Cell membrane, Peptide and Small interfering RNA, which intersect with Plasma protein binding.
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