Member of the European Molecular Biology Organization (EMBO)
His primary areas of study are Protein structure, Biochemistry, RNA, Cell biology and Stereochemistry. The Protein structure study which covers Biophysics that intersects with Fiber diffraction, Heat shock protein and In vitro. His RNA study improves the overall literature in Genetics.
His study in Cell biology is interdisciplinary in nature, drawing from both Periplasmic space, Efflux, Membrane transport protein and Histone H1. The concepts of his Stereochemistry study are interwoven with issues in Hemoglobin, Crystal structure, DNA and Hydrogen bond. His DNA research is multidisciplinary, incorporating perspectives in Crystallography, Stacking and Guanine.
Biochemistry, RNA, RNase P, Cell biology and Stereochemistry are his primary areas of study. Many of his studies involve connections with topics such as Biophysics and Biochemistry. As a part of the same scientific study, he usually deals with the Biophysics, concentrating on Crystallography and frequently concerns with Molecule.
In his work, Exoribonuclease is strongly intertwined with Polynucleotide phosphorylase, which is a subfield of RNA. His Stereochemistry research is multidisciplinary, relying on both Ligand, DNA, Crystal structure, Hydrogen bond and Hemeprotein. His work in Genetics tackles topics such as Computational biology which are related to areas like Regulation of gene expression.
Ben F. Luisi mostly deals with RNA, Efflux, Cell biology, Biophysics and RNase P. Biochemistry covers Ben F. Luisi research in RNA. His studies in Efflux integrate themes in fields like Periplasmic space, Escherichia coli, Transporter, Bacteria and Allosteric regulation.
His Cell biology study combines topics in areas such as Bacteriophage, Helicase, Polynucleotide phosphorylase, Regulation of gene expression and Drug resistance. Ben F. Luisi interconnects Molecular biology and Bacteriophage phiKZ in the investigation of issues within RNase P. Within one scientific family, Ben F. Luisi focuses on topics pertaining to Multiple drug resistance under Transport protein, and may sometimes address concerns connected to Protein structure.
Ben F. Luisi focuses on RNA, Efflux, Biochemistry, Cell biology and Biophysics. Ben F. Luisi has included themes like Polynucleotide phosphorylase and Bioinformatics in his RNA study. His Efflux study combines topics from a wide range of disciplines, such as Cell envelope, Escherichia coli and Antibiotic resistance.
His research integrates issues of Metabolome and Metabolomics in his study of Biochemistry. His Biophysics research integrates issues from Transport protein, Periplasmic space, Transmembrane protein and Membrane, Inner membrane. His Multiple drug resistance study integrates concerns from other disciplines, such as Protein structure and Structural biology.
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A Molecular Switch and Proton Wire Synchronize the Active Sites in Thiamine Enzymes
René A. W. Frank;Christopher M. Titman;J. Venkatesh Pratap;Ben F. Luisi.
Science (2004)
Crystal structure of the bacterial membrane protein TolC central to multidrug efflux and protein export
Vassilis Koronakis;Andrew Sharff;Eva Koronakis;Ben Luisi.
Nature (2000)
Crystal structure of trp repressor/operator complex at atomic resolution.
Z. Otwinowski;R. W. Schevitz;R. G. Zhang;C. L. Lawson.
Nature (1988)
Hfq and its constellation of RNA
Jörg Vogel;Ben F. Luisi.
Nature Reviews Microbiology (2011)
The high-resolution crystal structure of a parallel-stranded guanine tetraplex
Gerard Laughlan;Alastair I. H. Murchie;David G. Norman;Madeleine H. Moore.
web science (1994)
Stereochemistry of cooperative mechanisms in hemoglobin
M.F. Perutz;G. Fermi;B. Luisi;B. Shaanan.
Accounts of Chemical Research (1987)
The crystal structure of a parallel-stranded guanine tetraplex at 0.95 A resolution.
Kathryn Phillips;Zbyszek Dauter;Alastair I.H. Murchie;David M.J. Lilley.
Journal of Molecular Biology (1997)
Structure of the AcrAB–TolC multidrug efflux pump
Dijun Du;Zhao Wang;Nathan R. James;Jarrod E. Voss.
Nature (2014)
Multidrug efflux pumps: structure, function and regulation
Dijun Du;Xuan Wang-Kan;Arthur Neuberger;Hendrik W. van Veen.
Nature Reviews Microbiology (2018)
A duplicated fold is the structural basis for polynucleotide phosphorylase catalytic activity, processivity, and regulation.
Martyn F. Symmons;George H. Jones;Ben F. Luisi.
Structure (2000)
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