2020 - Fellow of the Royal Society, United Kingdom
His work often combines Biochemistry and Biophysics studies. He conducts interdisciplinary study in the fields of Biophysics and Biochemistry through his research. His study deals with a combination of Gene and Mutant. His study deals with a combination of Mutant and Gene. He frequently studies issues relating to Operon and Escherichia coli. His research combines Escherichia coli and Operon. Many of his studies on Cell biology involve topics that are commonly interrelated, such as Transport protein. His Transport protein study frequently draws connections between adjacent fields such as Cell biology. Ben C. Berks conducts interdisciplinary study in the fields of Twin-arginine translocation pathway and Signal peptide through his works.
Biochemistry and Biophysics are two areas of study in which Ben C. Berks engages in interdisciplinary research. While working on this project, he studies both Gene and Mutant. In his papers, Ben C. Berks integrates diverse fields, such as Mutant and Gene. His Escherichia coli study frequently links to adjacent areas such as Periplasmic space. His research is interdisciplinary, bridging the disciplines of Escherichia coli and Periplasmic space. His Enzyme study frequently draws connections to other fields, such as Nitrite reductase. By researching both Nitrite reductase and Nitrate reductase, he produces research that crosses academic boundaries. He performs multidisciplinary studies into Nitrate reductase and Enzyme in his work. His Organic chemistry study typically links adjacent topics like Sulfur.
His work blends Gene and Protein subunit studies together. Ben C. Berks regularly ties together related areas like Genetics in his Protein subunit studies. Ben C. Berks combines Genetics and Transformation (genetics) in his studies. He applies his multidisciplinary studies on Transformation (genetics) and DNA in his research. He performs multidisciplinary study in DNA and Nuclease in his work. In his works, he conducts interdisciplinary research on Nuclease and Gene. He brings together Biochemistry and Biological system to produce work in his papers. Ben C. Berks incorporates Biological system and Biochemistry in his studies. His research brings together the fields of Transport protein and Cell biology.
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A common export pathway for proteins binding complex redox cofactors
Ben C. Berks.
Molecular Microbiology (1996)
The Tat protein export pathway
Ben C. Berks;Frank Sargent;Tracy Palmer;Tracy Palmer.
Molecular Microbiology (2000)
ENZYMES AND ASSOCIATED ELECTRON TRANSPORT SYSTEMS THAT CATALYSE THE RESPIRATORY REDUCTION OF NITROGEN OXIDES AND OXYANIONS
Ben C. Berks;Stuart J. Ferguson;James W.B. Moir;James W.B. Moir;David J. Richardson.
Biochimica et Biophysica Acta (1995)
Overlapping functions of components of a bacterial Sec-independent protein export pathway.
Frank Sargent;Frank Sargent;Erik G. Bogsch;Nicola R. Stanley;Nicola R. Stanley;Margaret Wexler;Margaret Wexler.
The EMBO Journal (1998)
Functional, biochemical and genetic diversity of prokaryotic nitrate reductases
David Richardson;B. C. Berks;D. A. Russell;S. Spiro.
Cellular and Molecular Life Sciences (2001)
AN ESSENTIAL COMPONENT OF A NOVEL BACTERIAL PROTEIN EXPORT SYSTEM WITH HOMOLOGUES IN PLASTIDS AND MITOCHONDRIA
Erik G. Bogsch;Frank Sargent;Frank Sargent;Nicola R. Stanley;Nicola R. Stanley;Ben C. Berks.
Journal of Biological Chemistry (1998)
The twin-arginine translocation (Tat) protein export pathway
Tracy Palmer;Ben C. Berks.
Nature Reviews Microbiology (2012)
Sec-independent Protein Translocation in Escherichia coli: A DISTINCT AND PIVOTAL ROLE FOR THE TatB PROTEIN *
Frank Sargent;Frank Sargent;Nicola R. Stanley;Nicola R. Stanley;Ben C. Berks;Tracy Palmer;Tracy Palmer.
Journal of Biological Chemistry (1999)
The twin arginine consensus motif of Tat signal peptides is involved in Sec-independent protein targeting in Escherichia coli.
Nicola R. Stanley;Nicola R. Stanley;Tracy Palmer;Tracy Palmer;Ben C. Berks.
Journal of Biological Chemistry (2000)
A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system.
Simon C. Andrews;Ben C. Berks;Joseph McClay;Andrew Ambler.
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