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Arthur Landy
Researcher at Brown University
Publications - 124
Citations - 9581
Arthur Landy is an academic researcher from Brown University. The author has contributed to research in topics: Site-specific recombination & DNA. The author has an hindex of 52, co-authored 124 publications receiving 9460 citations. Previous affiliations of Arthur Landy include Laboratory of Molecular Biology.
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Journal ArticleDOI
Dynamic, structural, and regulatory aspects of lambda site-specific recombination.
Journal ArticleDOI
Empirical estimation of protein-induced DNA bending angles: applications to λ site-specific recombination complexes
John F. Thompson,Arthur Landy +1 more
TL;DR: An empirical relation between the degree of bending and the altered electrophoretic mobility in polyacrylamide gels that allows estimation of protein-induced bends is generated.
Journal ArticleDOI
The integrase family of site-specific recombinases: regional similarities and global diversity.
P. Argos,Arthur Landy,K. Abremski,J.B. Egan,E. Haggard-Ljungquist,R.H. Hoess,Michael L. Kahn,Bill Kalionis,S.V. Narayana,L.S. Pierson rd +9 more
TL;DR: A combination of two methods for detecting distant relationships in protein primary sequences was used to compare the site‐specific recombination proteins encoded by bacteriophage lambda, phi 80, P22, P2, 186, P4 and P1, and it is suggested that tyrosine‐433 forms a transient covalent linkage to DNA during strand cleavage and rejoining.
Journal ArticleDOI
Similarities and differences among 105 members of the Int family of site-specific recombinases
TL;DR: Alignments of 105 site-specific recombinases belonging to the Int family of proteins identified extended areas of similarity and three types of structural differences, including charged amino acids that are highly conserved and a specific pattern of buried residues contributing to the overall protein fold.
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Amber suppression: a nucleotide change in the anticodon of a tyrosine transfer RNA.
TL;DR: In certain mutants a single base change alters the meaning of a messenger codon in such a way that, instead of spelling out an amino-acid, it spells out chain termination.