What is he best known for?
The fields of study he is best known for:
- Enzyme
- Gene
- Organic chemistry
Terrence R. Burke spends much of his time researching Stereochemistry, Integrase, Biochemistry, Peptide and SH2 domain.
His work deals with themes such as Chemical synthesis, Small molecule and Active site, which intersect with Stereochemistry.
His biological study spans a wide range of topics, including Molecular biology and Enzyme inhibitor, Enzyme.
The study incorporates disciplines such as Lead compound, IC50 and Structure–activity relationship in addition to Enzyme inhibitor.
His study in Peptide is interdisciplinary in nature, drawing from both Phosphonate, Phosphatase and Phenylalanine.
Terrence R. Burke interconnects Tumor necrosis factor alpha, Okadaic acid, Transcription factor and Ceramide in the investigation of issues within Protein subunit.
His most cited work include:
- Caffeic acid phenethyl ester is a potent and specific inhibitor of activation of nuclear transcription factor NF-kappa B (1000 citations)
- Folliculin encoded by the BHD gene interacts with a binding protein, FNIP1, and AMPK, and is involved in AMPK and mTOR signaling (365 citations)
- Coumarin-based inhibitors of HIV integrase. (242 citations)
What are the main themes of his work throughout his whole career to date?
Terrence R. Burke mainly investigates Stereochemistry, Biochemistry, Peptide, Integrase and SH2 domain.
In his research on the topic of Stereochemistry, Membrane is strongly related with Binding site.
His work in Peptide addresses issues such as Phenylalanine, which are connected to fields such as Enantioselective synthesis.
Terrence R. Burke usually deals with Integrase and limits it to topics linked to Virology and Mutant.
His SH2 domain study incorporates themes from Cyclic peptide, GRB2 and Ligand.
His Protein tyrosine phosphatase research includes elements of Yersinia pestis and Small molecule.
He most often published in these fields:
- Stereochemistry (46.82%)
- Biochemistry (30.25%)
- Peptide (21.34%)
What were the highlights of his more recent work (between 2012-2021)?
- Integrase (19.11%)
- Stereochemistry (46.82%)
- Biochemistry (30.25%)
In recent papers he was focusing on the following fields of study:
His primary areas of study are Integrase, Stereochemistry, Biochemistry, Peptide and PLK1.
His Integrase research integrates issues from Strand transfer, Mutant and Virology.
His studies in Stereochemistry integrate themes in fields like Residue, Tyrosyl-DNA phosphodiesterase and Histidine.
The Biochemistry study combines topics in areas such as Conjugated system and Drug.
His biological study spans a wide range of topics, including Amino acid, Phosphothreonine, Protein tyrosine phosphatase and Protein–protein interaction.
His PLK1 research is multidisciplinary, incorporating perspectives in Computational biology, Kinase, Bioinformatics and Polo-like kinase.
Between 2012 and 2021, his most popular works were:
- Recent Advances and New Strategies in Targeting Plk1 for Anticancer Therapy. (60 citations)
- Efficacies of Cabotegravir and Bictegravir against drug-resistant HIV-1 integrase mutants. (49 citations)
- Structure of the Rpn13-Rpn2 complex provides insights for Rpn13 and Uch37 as anticancer targets (46 citations)
In his most recent research, the most cited papers focused on:
- Enzyme
- Gene
- Organic chemistry
His scientific interests lie mostly in Integrase, Biochemistry, Virology, Raltegravir and Computational biology.
His work on Integrases as part of general Integrase research is frequently linked to Dolutegravir, thereby connecting diverse disciplines of science.
In his works, Terrence R. Burke performs multidisciplinary study on Biochemistry and Conjugate.
His Virology study combines topics from a wide range of disciplines, such as Structure–activity relationship and Mutant.
Raltegravir is integrated with Potency, Raltegravir Potassium and Stereochemistry in his research.
His Stereochemistry research is multidisciplinary, relying on both Phosphoserine, Pivaloyloxymethyl, Polo kinase, Peptide and Histidine.
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