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Lesley H. Greene

Researcher at Old Dominion University

Publications -  31
Citations -  1460

Lesley H. Greene is an academic researcher from Old Dominion University. The author has contributed to research in topics: Protein folding & Protein structure. The author has an hindex of 13, co-authored 29 publications receiving 1381 citations. Previous affiliations of Lesley H. Greene include University of Oxford & University of Miami.

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The CATH domain structure database: new protocols and classification levels give a more comprehensive resource for exploring evolution.

TL;DR: There has been a 20% increase in the number of structural domains classified in CATH, up to 86 151 domains, and an update of the CATH Dictionary of homologous structures (CATH-DHS) which now contains multiple structural alignments, consensus information and functional annotations for 1459 well populated superfamilies in Cath.
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Uncovering network systems within protein structures.

TL;DR: Recognising that proteins are networks provides a means of rationalising the robustness in the overall three-dimensional fold of a protein against random mutations and suggests an alternative avenue to investigate the determinants of protein structure, function and folding.
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Structural analysis of the nurse shark (new) antigen receptor (NAR): molecular convergence of NAR and unusual mammalian immunoglobulins.

TL;DR: It is shown by electron microscopy that NAR V regions, unlike those of conventional Ig and TCR, do not form dimers but rather are independent, flexible domains, which are the result of convergent evolution at the molecular level.
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Sequence and structural analysis of the chitinase insertion domain reveals two conserved motifs involved in chitin-binding.

TL;DR: Sequence and structural studies of the chitinase insertion domains conducted within the framework of evolution identified four conserved residues which clearly interact with the substrates.
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Screening transthyretin amyloid fibril inhibitors: characterization of novel multiprotein, multiligand complexes by mass spectrometry.

TL;DR: The observation of a novel ten-component complex containing six protein subunits, two vitamin molecules, and two synthetic ligands allows us to conclude that ligand binding does not inhibit association of transthyretin with holo retinol binding protein.