Graeme B. Cox

What is he best known for?

The fields of study he is best known for:

• Enzyme
• Gene
• Amino acid

Graeme B. Cox focuses on Biochemistry, Escherichia coli, Protein subunit, Mutant and Molecular biology. Graeme B. Cox merges Biochemistry with ATP-binding cassette transporter in his study. Graeme B. Cox has researched Escherichia coli in several fields, including Cytochrome, Enzyme and Metabolism.

His Protein subunit study incorporates themes from ATPase and ATP synthase. His Mutant study integrates concerns from other disciplines, such as Oxidase test, Oxidative phosphorylation and Magnesium ion. His Molecular biology research is multidisciplinary, relying on both Protein primary structure, Peptide sequence, Calcium, Affinity chromatography and Peptide.

His most cited work include:

• The Vpu protein of human immunodeficiency virus type 1 forms cation-selective ion channels. (223 citations)
• Oxidative phosphorylation in Escherichia coli K 12. Mutations affecting magnesium ion- or calcium ion-stimulated adenosine triphosphatase (201 citations)
• Phosphate-specific transport system of Escherichia coli: nucleotide sequence and gene-polypeptide relationships. (176 citations)

What are the main themes of his work throughout his whole career to date?

Biochemistry, Escherichia coli, Mutant, Molecular biology and Protein subunit are his primary areas of study. His study in Membrane, ATPase, Amino acid, Alanine and Site-directed mutagenesis are all subfields of Biochemistry. His Escherichia coli study combines topics from a wide range of disciplines, such as Mutation, Oxidative phosphorylation and Biosynthesis, Enzyme.

The concepts of his Mutant study are interwoven with issues in Allele and Cell membrane. His Molecular biology research is multidisciplinary, incorporating perspectives in Plasmid, Peptide sequence, Gene, Magnesium ion and Operon. Graeme B. Cox combines subjects such as Crystallography, Receptor, GABAA receptor, Enterobacteriaceae and ATP synthase with his study of Protein subunit.

He most often published in these fields:

• Biochemistry (78.50%)
• Escherichia coli (61.68%)
• Mutant (43.93%)

What were the highlights of his more recent work (between 1994-2004)?

• Biochemistry (78.50%)
• Ion channel (10.28%)
• Protein subunit (28.04%)

In recent papers he was focusing on the following fields of study:

His main research concerns Biochemistry, Ion channel, Protein subunit, Biophysics and GABAA receptor. His work in Biochemistry tackles topics such as Molecular biology which are related to areas like Peptide sequence. His Ion channel research incorporates themes from Human Immunodeficiency Virus Proteins, Membrane, Lipid bilayer, Cell biology and Peptide.

His biological study spans a wide range of topics, including Crystallography, Alanine and ATP synthase. The various areas that Graeme B. Cox examines in his Biophysics study include Integral membrane protein, Virus and Phospholipid. His Escherichia coli research includes elements of Mutation, ATP hydrolysis, Complementation and Aspartic acid.

Between 1994 and 2004, his most popular works were:

• The Vpu protein of human immunodeficiency virus type 1 forms cation-selective ion channels. (223 citations)
• Crystal structure of the ϵ subunit of the proton-translocating ATP synthase from Escherichia coli (152 citations)
• Mutations in the white gene of Drosophila melanogaster affecting ABC transporters that determine eye colouration. (124 citations)

In his most recent research, the most cited papers focused on:

• Enzyme
• Gene
• Amino acid

Graeme B. Cox mostly deals with Biochemistry, Ion channel, Lipid bilayer, ATP-binding cassette transporter and Molecular biology. His study involves Transmembrane domain, Protein subunit, Alanine and ATP synthase, a branch of Biochemistry. His research in Lipid bilayer intersects with topics in Biophysics, Affinity chromatography and Peptide.

His Molecular biology research is multidisciplinary, incorporating perspectives in ATP hydrolysis, Escherichia coli, Complementation, Peptide sequence and Arginine. His research in Escherichia coli intersects with topics in Protein structure, Threonine and Aspartic acid. His White study integrates concerns from other disciplines, such as Tryptophan, Nucleic acid sequence, Membrane and Guanine.