The roles of substrate thermal stability and P2 and P1' subsite identity on matrix metalloproteinase triple-helical peptidase activity and collagen specificity.
about
Matrix metalloproteinase interactions with collagen and elastinCollagenolytic Matrix Metalloproteinase Activities toward Peptomeric Triple-Helical SubstratesUltrasound enhanced matrix metalloproteinase-9 triggered release of contents from echogenic liposomes.Remote exosites of the catalytic domain of matrix metalloproteinase-12 enhance elastin degradation.High throughput screening of potentially selective MMP-13 exosite inhibitors utilizing a triple-helical FRET substrate.Matrix metalloproteinase 13-deficient mice are resistant to osteoarthritic cartilage erosion but not chondrocyte hypertrophy or osteophyte development.NMR and bioinformatics discovery of exosites that tune metalloelastase specificity for solubilized elastin and collagen triple helices.Discovery of novel inhibitors of a disintegrin and metalloprotease 17 (ADAM17) using glycosylated and non-glycosylated substrates.Basis for substrate recognition and distinction by matrix metalloproteinasesCharacterization of selective exosite-binding inhibitors of matrix metalloproteinase 13 that prevent articular cartilage degradation in vitro.Development of a Förster resonance energy transfer assay for monitoring bacterial collagenase triple-helical peptidase activity.Using fluorogenic peptide substrates to assay matrix metalloproteinases.Exosite interactions impact matrix metalloproteinase collagen specificities.Rapid lead discovery through iterative screening of one bead one compound libraries.Matrix metalloproteinase inhibition by heterotrimeric triple-helical Peptide transition state analoguesRelease of liposomal contents by cell-secreted matrix metalloproteinase-9Comparison of metalloproteinase protein and activity profiling.Mechanical load induces a 100-fold increase in the rate of collagen proteolysis by MMP-1.Single-molecule tracking of collagenase on native type I collagen fibrils reveals degradation mechanism.Matrix metalloprotease-1a promotes tumorigenesis and metastasis.Characterization of an exosite binding inhibitor of matrix metalloproteinase 13.Identification of collagen binding domain residues that govern catalytic activities of matrix metalloproteinase-2 (MMP-2).Interstitial collagen catabolism.Molecular dissection of the structural machinery underlying the tissue-invasive activity of membrane type-1 matrix metalloproteinase.Differentiation of secreted and membrane-type matrix metalloproteinase activities based on substitutions and interruptions of triple-helical sequences.Genetic inhibition of fibroblast growth factor receptor 1 in knee cartilage attenuates the degeneration of articular cartilage in adult mice.Mast cell-restricted, tetramer-forming tryptases induce aggrecanolysis in articular cartilage by activating matrix metalloproteinase-3 and -13 zymogensBilayer Membrane Modulation of Membrane Type 1 Matrix Metalloproteinase (MT1-MMP) Structure and Proteolytic Activity.MicroRNA-381 Regulates Chondrocyte Hypertrophy by Inhibiting Histone Deacetylase 4 Expression.Identification of specific hemopexin-like domain residues that facilitate matrix metalloproteinase collagenolytic activity.Analysis of flavonoid-based pharmacophores that inhibit aggrecanases (ADAMTS-4 and ADAMTS-5) and matrix metalloproteinases through the use of topologically constrained peptide substrates.The role of collagen charge clusters in the modulation of matrix metalloproteinase activity.Chemical biology for understanding matrix metalloproteinase function.Synthesis and biological applications of collagen-model triple-helical peptides.AMPK deficiency in chondrocytes accelerated the progression of instability-induced and ageing-associated osteoarthritis in adult mice.Monitoring and Inhibiting MT1-MMP during Cancer Initiation and Progression.Bacterial collagenases - A review.Matrix metalloproteinase collagenolysis in health and disease.Determining the Substrate Specificity of Matrix Metalloproteases using Fluorogenic Peptide Substrates.Matrix metalloproteinases as reagents for cell isolation.
P2860
Q26996437-BB091FFD-05C4-4F73-A3EC-D1F4F2878558Q27301783-A7777D57-C186-46FD-B935-E7870CC03B0BQ30449753-4AC2240A-9277-4030-8768-1FE8EE1AC654Q30504556-1A1FC23D-96C5-4156-B6C4-9628953C6729Q33325058-CA044AD8-3DBC-4E94-B584-8B73FC606DC7Q33706862-C6845825-085F-4025-9F47-06F77C20526FQ34155412-04E55D4C-2018-44C8-A5FB-DFA3262914C2Q34395100-8A98F298-C6B4-4D23-ABFE-52752848DF2EQ34407655-F2185084-0A5F-44D1-BE79-2B4C7A841C8BQ34631606-FFE9AC2D-F780-4316-AF81-938ED5B1FF8CQ34663383-491DE8BB-D5F7-41F3-8692-6B4EA947025BQ35162671-D3D0BD28-185E-4AD5-AE0B-C9E1BA20CA4BQ35423858-37C89BB8-5317-4B2C-844D-89B2AF6C57E1Q35461662-2E0A59A3-884C-4121-AF5D-CF5839ACDFA4Q35557168-F1C33E81-A7B9-4604-A198-B3FF2C4104E7Q35636788-04800D7A-356F-49F8-8FFB-40C312945590Q35819663-53FEA01F-7B15-41B1-8AD4-6CB88C9B0AFBQ35873741-1E83B031-5A3B-4062-AF47-EC910F26EC96Q36055116-9C747333-465A-4332-BA7D-E8F0B9831D0DQ36097959-9D21FBDE-6532-4A4F-A4E2-34FD7324D28CQ36281981-CC0A4741-9725-4A62-B9ED-FD58872ABB8BQ36442625-3A3B77E2-81E8-49CD-9B1B-93AA473A258BQ36724874-EA3AE1F1-3ED6-409F-8990-5CB6076DC729Q36796844-0D71889A-89AF-44A3-A948-424E8DBA6863Q36942459-C819B872-0F13-4FD1-A9B9-16E117A9301DQ36948397-C1CCE2B4-B898-48F9-9189-2FEEC6AB927CQ37055039-92291BB0-2239-4AAA-BDEF-D127F5C68E35Q37089575-DCF43E78-D20F-41A6-89E3-2AB06BE78F6FQ37286201-EC13F279-7953-40C9-8581-0942092C8CADQ37433262-883CDE32-CABB-4F84-8DEB-940443DD5EB0Q37435339-77A0CF65-97B5-44CA-8473-A69E096C546CQ37511686-A9F5757C-2B4A-4B92-8600-EDD891DCA3B3Q37632925-F623A56C-CF89-4427-916F-794C42C678D2Q37632930-189CA86A-7270-4E45-B91D-03BD1E377087Q37657974-5B57FBBE-9E6C-4D8F-AB83-F2317D95AC55Q37693503-A8485AF8-F37D-40E2-9563-A649AD8E94A9Q38206220-BE8780B0-FFF6-4B03-A9CF-952C0CE1EF07Q38431602-D8E8A8F1-7F1C-432C-80CF-63B5BECE0B51Q38432629-BDE3FFE2-99E9-48E7-895B-380FB77779E1Q38435741-C080A8B8-FC50-4B58-A209-DB9AD7C86830
P2860
The roles of substrate thermal stability and P2 and P1' subsite identity on matrix metalloproteinase triple-helical peptidase activity and collagen specificity.
description
2006 nî lūn-bûn
@nan
2006 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
The roles of substrate thermal ...... vity and collagen specificity.
@ast
The roles of substrate thermal ...... vity and collagen specificity.
@en
The roles of substrate thermal ...... vity and collagen specificity.
@nl
type
label
The roles of substrate thermal ...... vity and collagen specificity.
@ast
The roles of substrate thermal ...... vity and collagen specificity.
@en
The roles of substrate thermal ...... vity and collagen specificity.
@nl
prefLabel
The roles of substrate thermal ...... vity and collagen specificity.
@ast
The roles of substrate thermal ...... vity and collagen specificity.
@en
The roles of substrate thermal ...... vity and collagen specificity.
@nl
P2093
P2860
P356
P1476
The roles of substrate thermal ...... vity and collagen specificity.
@en
P2093
Duanqing Pei
Gregg B Fields
Hideaki Nagase
Janelle L Lauer-Fields
Keith Brew
Mare Cudic
Robert Visse
P2860
P304
38302-38313
P356
10.1074/JBC.M606004200
P407
P577
2006-10-25T00:00:00Z