His primary areas of investigation include Biochemistry, CRISPR, Genetics, Folding and Computational biology. His work in Biochemistry is not limited to one particular discipline; it also encompasses Cell biology. His CRISPR research includes themes of Pseudomonas aeruginosa, Function and Mobile genetic elements.
His Folding research incorporates themes from Crystallography and Sequence. His research integrates issues of Proteome, Ligand Binding Protein and Sequence in his study of Computational biology. His biological study deals with issues like Energy landscape, which deal with fields such as Biophysics.
Alan R. Davidson mainly investigates Genetics, Biochemistry, Crystallography, CRISPR and SH3 domain. His Crystallography research is multidisciplinary, relying on both Sequence alignment, Biophysics, Protein folding, Folding and Nuclear magnetic resonance spectroscopy. His Protein folding study which covers Protein structure that intersects with Conserved sequence and Computational biology.
His CRISPR study combines topics from a wide range of disciplines, such as Genome, Mobile genetic elements and DNA. In his research, Cyclic nucleotide-binding domain is intimately related to Stereochemistry, which falls under the overarching field of SH3 domain. As a part of the same scientific family, Alan R. Davidson mostly works in the field of Gene, focusing on Pseudomonas aeruginosa and, on occasion, Microbiology and Mutation.
Alan R. Davidson mainly focuses on CRISPR, DNA, Bacteria, Cell biology and Mobile genetic elements. His studies in CRISPR integrate themes in fields like RNA, Computational biology and Function. Alan R. Davidson has included themes like Psychological repression, Genome, Binding site and Mutagenesis in his DNA study.
The concepts of his Bacteria study are interwoven with issues in Type VI secretion system, Biochemistry, Escherichia coli Proteins and Pyocyanin. Within one scientific family, Alan R. Davidson focuses on topics pertaining to In vitro under Mobile genetic elements, and may sometimes address concerns connected to Mutant. His study with Pseudomonas aeruginosa involves better knowledge in Genetics.
Alan R. Davidson spends much of his time researching CRISPR, Gene, Mobile genetic elements, DNA and Computational biology. The study of CRISPR is intertwined with the study of Library science in a number of ways. His Gene research is multidisciplinary, relying on both Pseudomonas aeruginosa, Bacteria, Glycosylation and Microbiology.
His Mobile genetic elements research entails a greater understanding of Genetics. In his study, Promoter, Repressor, Cell biology and Transcription is inextricably linked to Genome, which falls within the broad field of DNA. Alan R. Davidson has researched Computational biology in several fields, including Biological evolution, Horizontal gene transfer and Function.
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Bacteriophage genes that inactivate the CRISPR/Cas bacterial immune system
Joe Bondy-Denomy;April Pawluk;Karen L. Maxwell;Alan R. Davidson.
Nature (2013)
Low-populated folding intermediates of Fyn SH3 characterized by relaxation dispersion NMR
Dmitry M Korzhnev;Xavier Salvatella;Michele Vendruscolo;Ariel A Di Nardo.
Nature (2004)
Structural proteomics of an archaeon.
Dinesh Christendat;Adelinda Yee;Akil Dharamsi;Yuval Kluger.
Nature Structural & Molecular Biology (2000)
Naturally Occurring Off-Switches for CRISPR-Cas9
April Pawluk;Nadia Amrani;Yan Zhang;Bianca Garcia.
Cell (2016)
Multiple mechanisms for CRISPR–Cas inhibition by anti-CRISPR proteins
Joseph Bondy-Denomy;Bianca Garcia;Scott Strum;Mingjian Du.
Nature (2015)
The phage λ major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system
Lisa G. Pell;Voula Kanelis;Logan W. Donaldson;P. Lynne Howell.
Proceedings of the National Academy of Sciences of the United States of America (2009)
A New Group of Phage Anti-CRISPR Genes Inhibits the Type I-E CRISPR-Cas System of Pseudomonas aeruginosa
April Pawluk;Joseph Bondy-Denomy;Vivian H. W. Cheung;Karen L. Maxwell.
Mbio (2014)
An unusual eukaryotic protein phosphatase required for transcription by RNA polymerase II and CTD dephosphorylation in S. cerevisiae.
Michael S Kobor;Jacques Archambault;William Lester;Frank C.P Holstege.
Molecular Cell (1999)
Folded proteins occur frequently in libraries of random amino acid sequences.
Alan R. Davidson;Robert T. Sauer.
Proceedings of the National Academy of Sciences of the United States of America (1994)
Protein folding: defining a "standard" set of experimental conditions and a preliminary kinetic data set of two-state proteins.
Karen L. Maxwell;David Wildes;Arash Zarrine-Afsar;Miguel A. De Los Rios.
Protein Science (2005)
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