MMP-20 is predominately a tooth-specific enzyme with a deep catalytic pocket that hydrolyzes type V collagen
about
Reduced amelogenin-MMP20 interactions in amelogenesis imperfectaPseudogenization of the tooth gene enamelysin (MMP20) in the common ancestor of extant baleen whalesCatalytic domain of MMP20 (Enamelysin) - the NMR structure of a new matrix metalloproteinaseHypomaturation enamel defects in Klk4 knockout/LacZ knockin miceDental enamel development: proteinases and their enamel matrix substratesDeterminants of Macromolecular Specificity from Proteomics-Derived Peptide Substrate Data.Emerging principles in protease-based drug discovery.Evidence for a single loss of mineralized teeth in the common avian ancestor.JNK/c-Jun signaling pathway mediates the fluoride-induced down-regulation of MMP-20 in vitroDrug delivery strategies for common orofacial diseases.Murine matrix metalloproteinase-20 overexpression stimulates cell invasion into the enamel layer via enhanced Wnt signalingDPPI may activate KLK4 during enamel formation.Matrix metalloproteinase-20 over-expression is detrimental to enamel development: a Mus musculus modelMatrix metalloproteinase 20-dentin sialophosphoprotein interaction in oral cancer.Matrix Metalloproteinase 20 Co-expression With Dentin Sialophosphoprotein in Human and Monkey Kidneys.Expression of Matrix Metalloproteinase (MMP)-20 and Potential Interaction with Dentin Sialophosphoprotein (DSPP) in Human Major Salivary Glands.Matrix metalloproteinase 20 promotes a smooth enamel surface, a strong dentino-enamel junction, and a decussating enamel rod patternAssessment of dental fluorosis in Mmp20 +/- miceActivation profiles of human kallikrein-related peptidases by matrix metalloproteinases.Extracts of irradiated mature human tooth crowns contain MMP-20 protein and activity.Molecular evolution of matrix metalloproteinase 20.Postradiation Matrix Metalloproteinase-20 Expression and Its Impact on Dental Micromorphology and Radiation-Related Caries.Claudin-16 Deficiency Impairs Tight Junction Function in Ameloblasts, Leading to Abnormal Enamel Formation.
P2860
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P2860
MMP-20 is predominately a tooth-specific enzyme with a deep catalytic pocket that hydrolyzes type V collagen
description
2006 nî lūn-bûn
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2006 թուականի Մարտին հրատարակուած գիտական յօդուած
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2006 թվականի մարտին հրատարակված գիտական հոդված
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2006年の論文
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2006年論文
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2006年論文
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2006年論文
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2006年論文
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2006年論文
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2006年论文
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name
MMP-20 is predominately a toot ...... hat hydrolyzes type V collagen
@ast
MMP-20 is predominately a toot ...... hat hydrolyzes type V collagen
@en
type
label
MMP-20 is predominately a toot ...... hat hydrolyzes type V collagen
@ast
MMP-20 is predominately a toot ...... hat hydrolyzes type V collagen
@en
prefLabel
MMP-20 is predominately a toot ...... hat hydrolyzes type V collagen
@ast
MMP-20 is predominately a toot ...... hat hydrolyzes type V collagen
@en
P2093
P2860
P356
P1433
P1476
MMP-20 is predominately a toot ...... hat hydrolyzes type V collagen
@en
P2093
Andreas Klingenhoff
Benjamin E Turk
Daniel H Lee
Ernst Reichenberger
J Timothy Wright
James P Simmer
Justin A Komisarof
Lewis C Cantley
Yasuo Yamakoshi
P2860
P304
P356
10.1021/BI052252O
P407
P577
2006-03-01T00:00:00Z