INT89791

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Context Info
Confidence 0.33
First Reported 2000
Last Reported 2010
Negated 0
Speculated 2
Reported most in Body
Documents 7
Total Number 9
Disease Relevance 2.28
Pain Relevance 4.64

This is a graph with borders and nodes. Maybe there is an Imagemap used so the nodes may be linking to some Pages.

peptidase activity (Mmp3) extracellular space (Mmp3) extracellular region (Mmp3)
proteinaceous extracellular matrix (Mmp3) nucleus (Mmp3) protein complex (Mmp3)
Anatomy Link Frequency
joints 1
tendon 1
nucleus 1
annulus 1
Mmp3 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
metalloproteinase 252 100.00 Very High Very High Very High
agonist 171 99.22 Very High Very High Very High
cytokine 17 97.36 Very High Very High Very High
Snapping jaw 5 94.00 High High
anesthesia 5 93.12 High High
Inflammation 20 90.68 High High
Pain 5 90.32 High High
Potency 48 88.24 High High
Osteoarthritis 27 86.24 High High
Arthritis 6 84.72 Quite High
Disease Link Frequency Relevance Heat
Temporomandibular Joint Syndrome 4 94.00 High High
INFLAMMATION 23 90.68 High High
Endometriosis (extended) 2 88.92 High High
Cadaver 2 86.96 High High
Osteoarthritis 42 86.24 High High
Arthritis 12 84.72 Quite High
Congenital Anomalies 2 84.28 Quite High
Tendinopathy 5 83.28 Quite High
Pulpitis 1 80.76 Quite High
Sprains And Strains 2 80.60 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Loaded (c8-9) and internal-control discs (c6-7 and c10-11) were dissected and annulus and nucleus tissue were separately analyzed by real-time RT-PCR for levels of anabolic (collagen-1A1, collagen-2A1, aggrecan) and catabolic (MMP-3, MMP-13, ADAMTs-4) mRNA.
Spec (analyzed) Transcription (levels) of MMP-3 in nucleus
1) Confidence 0.33 Published 2004 Journal J. Orthop. Res. Section Abstract Doc Link 15475197 Disease Relevance 0 Pain Relevance 0.09
In their rabbit flexor tendon model, Asundi and Rempel described MMP 3, but not MMP 1 inhibition [25].
Transcription (described) of MMP 3 in tendon associated with metalloproteinase
2) Confidence 0.29 Published 2010 Journal BMC Musculoskelet Disord Section Body Doc Link PMC2998463 Disease Relevance 0.25 Pain Relevance 0.57
The real-time PCR technique was applied to detected the mRNA expressions of MMP-2, MMP-3 and TIMP-2.
Transcription (expressions) of MMP-3
3) Confidence 0.19 Published 2006 Journal Sichuan Da Xue Xue Bao Yi Xue Ban Section Body Doc Link 16468658 Disease Relevance 0.18 Pain Relevance 0
However, the basal MMP activities were decreased significantly by Wy14643 (Figures 4(a) and 4(b)), as well as the basal mRNA levels for MMP-3 and MMP-13 (Table 2).
Transcription (levels) of MMP-3 associated with metalloproteinase
4) Confidence 0.14 Published 2010 Journal PPAR Research Section Body Doc Link PMC2957135 Disease Relevance 0 Pain Relevance 0.84
Loaded (c8-9) and internal-control discs (c6-7 and c10-11) were dissected and annulus and nucleus tissue were separately analyzed by real-time RT-PCR for levels of anabolic (collagen-1A1, collagen-2A1, aggrecan) and catabolic (MMP-3, MMP-13, ADAMTs-4) mRNA.
Spec (analyzed) Transcription (levels) of MMP-3 in annulus
5) Confidence 0.11 Published 2004 Journal J. Orthop. Res. Section Abstract Doc Link 15475197 Disease Relevance 0 Pain Relevance 0.09
Consistently, the levels of mRNA for MMP-3 and -13 were reduced by 50% and by 10%, respectively, whereas those for TIMP-1 were upregulated by 65% (Table 2).
Transcription (levels) of MMP-3 associated with metalloproteinase
6) Confidence 0.11 Published 2010 Journal PPAR Research Section Body Doc Link PMC2957135 Disease Relevance 0 Pain Relevance 0.68
In the present work, we demonstrated that PPAR agonists (Wy14643) are capable to inhibit mRNA expression or activity of MMP-3 & 13 and global MMP activity through a PPAR-independent mechanism pathway.
Transcription (expression) of MMP-3 associated with metalloproteinase and agonist
7) Confidence 0.09 Published 2010 Journal PPAR Research Section Body Doc Link PMC2957135 Disease Relevance 0.95 Pain Relevance 0.85
MMP-1 and TIMP-1 were not recordable in most joints, and the serum concentrations of MMP-1, MMP-3, and TIMP-1 were similar to those in controls in all groups.
Transcription (concentrations) of MMP-3 in joints associated with metalloproteinase
8) Confidence 0.05 Published 2000 Journal Br J Oral Maxillofac Surg Section Abstract Doc Link 10922168 Disease Relevance 0.62 Pain Relevance 1.06
TNF-alpha, IL-1beta, and IL-6 increased the mRNA and/or protein expression of MMP-1, MMP-2, and MMP-3.
Transcription (expression) of MMP-3
9) Confidence 0.02 Published 2006 Journal J Endod Section Abstract Doc Link 16934628 Disease Relevance 0.23 Pain Relevance 0.46

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