Journal ArticleDOI
Merging the binding sites of aldose and aldehyde reductase for detection of inhibitor selectivity-determining features.
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TLDR
The study revealed induced-fit adaptations within the mutated binding site as an essential prerequisite for ligand accommodation related to the selectivity discrimination of the ligands and highlights the limits of the present understanding of protein-ligand interactions.About:
This article is published in Journal of Molecular Biology.The article was published on 2008-06-20. It has received 44 citations till now. The article focuses on the topics: Ligand (biochemistry) & Binding site.read more
Citations
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Journal ArticleDOI
The aldo-keto reductase superfamily and its role in drug metabolism and detoxification.
TL;DR: The aldo-keto reductase (AKR) superfamily comprises enzymes that catalyze redox transformations involved in biosynthesis, intermediary metabolism, and detoxification that play an important role in the phase II detoxification of a large number of pharmaceuticals, drugs, and xenobiotics.
Journal ArticleDOI
Targeting aldose reductase for the treatment of diabetes complications and inflammatory diseases: new insights and future directions.
Rosanna Maccari,Rosaria Ottanà +1 more
TL;DR: In this review, recent advances in the field and promising future directions for developing ARIs are discussed.
Journal ArticleDOI
Accurate Estimation of Ligand Binding Affinity Changes upon Protein Mutation.
TL;DR: It is shown that both the free energy calculations and Rosetta are able to quantitatively predict changes in ligand binding affinity upon protein mutations, yet the best predictions are the result of combining the estimates of both methods.
Journal ArticleDOI
Survey of the year 2008: applications of isothermal titration calorimetry
TL;DR: This review highlights some of the particularly interesting reports from 2008 employing ITC, with a particular focus on protein interactions with other proteins, nucleic acids, lipids and drugs.
Journal ArticleDOI
A diverse series of substituted benzenesulfonamides as aldose reductase inhibitors with antioxidant activity: design, synthesis, and in vitro activity.
TL;DR: Additional 2,6-difluorophenol and tetrazole, methylsulfonylamide, and isoxazolidin-3-one phenylsulfonamide derivatives were synthesized and tested in vitro in protocols primarily related to the long-term diabetic complications.
References
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Book ChapterDOI
Processing of X-ray diffraction data collected in oscillation mode
Zbyszek Otwinowski,Wladek Minor +1 more
TL;DR: The methods presented in the chapter have been applied to solve a large variety of problems, from inorganic molecules with 5 A unit cell to rotavirus of 700 A diameters crystallized in 700 × 1000 × 1400 A cell.
Journal ArticleDOI
Coot: model-building tools for molecular graphics.
Paul Emsley,Kevin Cowtan +1 more
TL;DR: CCP4mg is a project that aims to provide a general-purpose tool for structural biologists, providing tools for X-ray structure solution, structure comparison and analysis, and publication-quality graphics.
Journal ArticleDOI
PROCHECK: a program to check the stereochemical quality of protein structures
TL;DR: The PROCHECK suite of programs as mentioned in this paper provides a detailed check on the stereochemistry of a protein structure and provides an assessment of the overall quality of the structure as compared with well refined structures of the same resolution.
Journal ArticleDOI
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Axel T. Brunger,Axel T. Brunger,Paul D. Adams,G M Clore,W. L. DeLano,Piet Gros,R.W. Grosse-Kunstleve,R.W. Grosse-Kunstleve,Jiansheng Jiang,J. Kuszewski,Michael Nilges,Navraj S. Pannu,Randy J. Read,Luke M. Rice,Thomas Simonson,Gregory L. Warren +15 more
TL;DR: The Crystallography & NMR System (CNS) as mentioned in this paper is a software suite for macromolecular structure determination by X-ray crystallography or solution nuclear magnetic resonance (NMR) spectroscopy.
Journal ArticleDOI
Improved methods for building protein models in electron density maps and the location of errors in these models.
TL;DR: In this paper, the authors describe strategies and tools that help to alleviate this problem and simplify the model-building process, quantify the goodness of fit of the model on a per-residue basis and locate possible errors in peptide and side-chain conformations.