Conformational variability of matrix metalloproteinases: beyond a single 3D structure. - Wikidata - awgldk - TriplyDB

Conformational variability of matrix metalloproteinases: beyond a single 3D structure.

Conformational variability of matrix metalloproteinases: beyond a single 3D structure.

http://www.wikidata.org/entity/Q33936554

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Biophysical studies of matrix metalloproteinase/triple-helix complexes Catalytic domain of MMP20 (Enamelysin) - the NMR structure of a new matrix metalloproteinase Solution Structure of Inhibitor-Free Human Metalloelastase (MMP-12) Indicates an Internal Conformational Adjustment Paramagnetic shifts in solid-state NMR of proteins to elicit structural information High-Resolution Solid-State NMR Structure of a 17.6 kDa Protein Insights from Selective Non-phosphinic Inhibitors of MMP-12 Tailored to Fit with an S1' Loop Canonical Conformation Antibodies targeting the catalytic zinc complex of activated matrix metalloproteinases show therapeutic potential Matrix Metalloproteinase-10/TIMP-2 Structure and Analyses Define Conserved Core Interactions and Diverse Exosite Interactions in MMP/TIMP Complexes Simple Pseudo-dipeptides with a P2' Glutamate: A NOVEL INHIBITOR FAMILY OF MATRIX METALLOPROTEASES AND OTHER METZINCINS Structure of matrix metalloproteinase-3 with a platinum-based inhibitor Synthesis and in Vitro and in Vivo Evaluation of MMP-12 Selective Optical Probes Path to Collagenolysis: COLLAGEN V TRIPLE-HELIX MODEL BOUND PRODUCTIVELY AND IN ENCOUNTERS BY MATRIX METALLOPROTEINASE-12.Development of selective inhibitors and substrate of matrix metalloproteinase-12.The roles of substrate thermal stability and P2 and P1' subsite identity on matrix metalloproteinase triple-helical peptidase activity and collagen specificity.Zinc-binding groups modulate selective inhibition of MMPs.Matrix metalloproteases in head and neck cancer.Matrix metalloproteinase-induced epithelial-mesenchymal transition in breast cancer.Apparent tradeoff of higher activity in MMP-12 for enhanced stability and flexibility in MMP-3.Probing water-protein contacts in a MMP-12/CGS27023A complex by nuclear magnetic resonance spectroscopy.Ambidextrous binding of cell and membrane bilayers by soluble matrix metalloproteinase-12.Perspectives on NMR in drug discovery: a technique comes of age Matrix metalloproteinases as breast cancer drivers and therapeutic targets.Spinal matrix metalloproteinase 3 mediates inflammatory hyperalgesia via a tumor necrosis factor-dependent mechanism.Metabolic Response of Human Osteoarthritic Cartilage to Biochemically Characterized Collagen Hydrolysates.Towards third generation matrix metalloproteinase inhibitors for cancer therapy Matrix metalloproteases: underutilized targets for drug delivery Stictamides A-C, MMP12 inhibitors containing 4-amino-3-hydroxy-5-phenylpentanoic acid subunits.Looking at the proteases from a simple perspective.An integrated computational and experimental approach to gaining selectivity for MMP-2 within the gelatinase subfamily.Discovery of a New Class of Potent MMP Inhibitors by Structure-Based Optimization of the Arylsulfonamide Scaffold.MMP-12 catalytic domain recognizes triple helical peptide models of collagen V with exosites and high activity.Strategic targeting of multiple water-mediated interactions: a concise and rational structure-based design approach to potent and selective MMP-13 inhibitors Ramachandran analysis of conserved glycyl residues in homologous proteins of known structure Molecular determinants of matrix metalloproteinase-12 covalent modification by a photoaffinity probe: insights into activity-based probe development and conformational variability of matrix metalloproteinases.Rapid determination of enzyme kinetics from fluorescence: overcoming the inner filter effect Interdomain flexibility in full-length matrix metalloproteinase-1 (MMP-1).(1)H-detected solid-state NMR of proteins entrapped in bioinspired silica: a new tool for biomaterials characterization.1H, 13C, and 15N peak assignments and secondary structure of human macrophage metalloelastase (MMP-12) in its inhibitor-free state.Solvent water interactions within the active site of the membrane type I matrix metalloproteinase.Atomic-Level Quality Assessment of Enzymes Encapsulated in Bioinspired Silica.

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Conformational variability of matrix metalloproteinases: beyond a single 3D structure.

http://www.wikidata.org/entity/Q33936554

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2005 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2005 թվականի ապրիլին հրատարակված գիտական հոդված

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2005年の論文

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Conformational variability of matrix metalloproteinases: beyond a single 3D structure.

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Conformational variability of matrix metalloproteinases: beyond a single 3D structure.

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Conformational variability of matrix metalloproteinases: beyond a single 3D structure.

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Conformational variability of matrix metalloproteinases: beyond a single 3D structure.

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PNAS.0407106102

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Proceedings of the National Academy of Sciences of the United States of America

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Conformational variability of matrix metalloproteinases: beyond a single 3D structure.

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Beatrice Terni

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Marta Cosenza

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Stefano Mangani

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Vito Calderone

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Yong-Min Lee

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P2860

PROCHECK: a program to check the stereochemical quality of protein structures

Solution structure of the catalytic domain of human collagenase-3 (MMP-13) complexed to a potent non-peptidic sulfonamide inhibitor: binding comparison with stromelysin-1 and collagenase-1

High-resolution solution structure of the catalytic fragment of human collagenase-3 (MMP-13) complexed with a hydroxamic acid inhibitor

Substrate specificity determinants of human macrophage elastase (MMP-12) based on the 1.1 A crystal structure

Solution structure and backbone dynamics of the catalytic domain of matrix metalloproteinase-2 complexed with a hydroxamic acid inhibitor

X-ray structures of binary and ternary enzyme-product-inhibitor complexes of matrix metalloproteinases

The NMR structure of the inhibited catalytic domain of human stromelysin-1

Dynamics of Fusarium solani cutinase investigated through structural comparison among different crystal forms of its variants

High-resolution solution structure of the inhibitor-free catalytic fragment of human fibroblast collagenase determined by multidimensional NMR

Solution structure of the catalytic domain of human stromelysin-1 complexed to a potent, nonpeptidic inhibitor

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Claudio Luchinat

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7927710

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