What is he best known for?
The fields of study he is best known for:
His primary scientific interests are in Ubiquitin, Biochemistry, Proteasome, Ubiquitin ligase and Ubiquitin-conjugating enzyme.
His study in Ubiquitin is interdisciplinary in nature, drawing from both Ribosomal RNA, Ribosomal protein and Protein degradation, Cell biology.
His work in the fields of Chaperone overlaps with other areas such as DNAJA3.
His work in Biochemistry addresses subjects such as Biophysics, which are connected to disciplines such as Substrate.
The study incorporates disciplines such as Deubiquitinating enzyme, ADRM1, Protein subunit, Proteasome assembly and Protein structure in addition to Proteasome.
His Ubiquitin-conjugating enzyme research includes themes of ERAD pathway, Endoplasmic-reticulum-associated protein degradation, Lysine, Protein ubiquitination and Signal transduction.
His most cited work include:
- In Vivo Half-Life of a Protein is a Function of its Amino-Terminal Residue (1580 citations)
- A proteomics approach to understanding protein ubiquitination (1324 citations)
- Recognition and Processing of Ubiquitin-Protein Conjugates by the Proteasome (1243 citations)
What are the main themes of his work throughout his whole career to date?
Daniel Finley spends much of his time researching Proteasome, Cell biology, Ubiquitin, Biochemistry and Ubiquitin-conjugating enzyme.
His Proteasome research is multidisciplinary, incorporating perspectives in Protein degradation, Biophysics, Deubiquitinating enzyme, Protein subunit and Proteolysis.
Daniel Finley has researched Cell biology in several fields, including F-box protein and Enzyme.
His Ubiquitin study incorporates themes from Molecular biology, In vitro and Function.
His research in Mutant, Saccharomyces cerevisiae, Proteasome assembly, ATPase and Protein structure are components of Biochemistry.
Daniel Finley combines subjects such as Proteomics and Lysine with his study of Ubiquitin ligase.
He most often published in these fields:
- Proteasome (64.50%)
- Cell biology (50.89%)
- Ubiquitin (49.70%)
What were the highlights of his more recent work (between 2017-2021)?
- Cell biology (50.89%)
- Proteasome (64.50%)
- Ubiquitin (49.70%)
In recent papers he was focusing on the following fields of study:
His main research concerns Cell biology, Proteasome, Ubiquitin, Biophysics and Protein degradation.
His Cell biology research includes themes of Proteome, Protein subunit and UBQLN2.
His Proteasome study integrates concerns from other disciplines, such as Proteolysis and Function.
His biological study focuses on Deubiquitinating enzyme.
The study incorporates disciplines such as ATP hydrolysis, ATPase, In vitro and Protein aggregation in addition to Biophysics.
His Protein degradation research incorporates themes from Cell, Saccharomyces cerevisiae, Nucleus, Cytosol and Microtubule.
Between 2017 and 2021, his most popular works were:
- Cryo-EM structures and dynamics of substrate-engaged human 26S proteasome. (113 citations)
- The proteasome 19S cap and its ubiquitin receptors provide a versatile recognition platform for substrates (30 citations)
- The Proteasome and Its Network: Engineering for Adaptability. (26 citations)
In his most recent research, the most cited papers focused on:
His primary areas of investigation include Cell biology, Proteasome, Ubiquitin, Function and Biophysics.
His Cell biology study combines topics in areas such as Ribosomal protein, Mutation, Point mutation, Protein domain and Protein biosynthesis.
His Proteasome research incorporates elements of Substrate specificity, Protein subunit, Allosteric regulation and Proteolysis.
His study in the fields of Deubiquitinating enzyme under the domain of Ubiquitin overlaps with other disciplines such as Ciliopathies.
His work deals with themes such as Fibril and Proteases, which intersect with Function.
His work carried out in the field of Biophysics brings together such families of science as ATP hydrolysis, ATPase, Protein degradation, Hydrolase and Protein structure.
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