INT187133

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Context Info
Confidence 0.73
First Reported 2005
Last Reported 2011
Negated 0
Speculated 0
Reported most in Body
Documents 19
Total Number 19
Disease Relevance 11.30
Pain Relevance 5.51

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

aging (TIMP1) extracellular region (TIMP1)
Anatomy Link Frequency
cleavage 4
ECM 3
cartilage 2
chondrocytes 1
blood vessels 1
TIMP1 (Homo sapiens)
Pain Link Frequency Relevance Heat
metalloproteinase 200 100.00 Very High Very High Very High
rheumatoid arthritis 123 100.00 Very High Very High Very High
Pain 131 99.64 Very High Very High Very High
Inflammatory response 21 99.58 Very High Very High Very High
Osteoarthritis 470 98.92 Very High Very High Very High
Inflammation 257 98.80 Very High Very High Very High
imagery 134 96.44 Very High Very High Very High
Inflammatory stimuli 4 95.92 Very High Very High Very High
cytokine 119 95.04 Very High Very High Very High
Infliximab 22 73.52 Quite High
Disease Link Frequency Relevance Heat
Rheumatoid Arthritis 164 100.00 Very High Very High Very High
Pain 137 99.64 Very High Very High Very High
INFLAMMATION 292 99.40 Very High Very High Very High
Cancer 275 99.28 Very High Very High Very High
Rupture 18 99.20 Very High Very High Very High
Osteoarthritis 221 98.92 Very High Very High Very High
Obesity 129 98.32 Very High Very High Very High
Apoptosis 77 96.72 Very High Very High Very High
Autoimmune Disease 5 96.32 Very High Very High Very High
Metastasis 26 95.00 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Matrix metalloproteinases (MMPs) belong to the group of ECM degradation enzymes.
Protein_catabolism (degradation) of metalloproteinases in ECM associated with metalloproteinase
1) Confidence 0.73 Published 2006 Journal BMC Urol Section Body Doc Link PMC1560390 Disease Relevance 1.13 Pain Relevance 0.31
This hypothesis seems to conflict with the present view of MMP-mediated proteolytic degradation of cartilage in RA and with the fact that TIMP-3-transfected synovial fibroblasts are deprived of their invasive capacity [14], while TIMP-1-transduced chondrocytes resist catabolism [15].
Protein_catabolism (degradation) of TIMP in chondrocytes associated with rheumatoid arthritis
2) Confidence 0.48 Published 2005 Journal Arthritis Res Ther Section Body Doc Link PMC1257425 Disease Relevance 0.83 Pain Relevance 0.36
Loss of collagen and structural strength leading to rupture of the membranes is mediated by matrix metalloproteinases (MMPs), a large family of enzymes that act to degrade collagen and remodel tissue.
Protein_catabolism (degrade) of metalloproteinases associated with rupture and metalloproteinase
3) Confidence 0.17 Published 2010 Journal BMC Pregnancy Childbirth Section Body Doc Link PMC2841774 Disease Relevance 1.05 Pain Relevance 0.30
Such a HCI approach can also include the ability to “degrade gracefully” as the inputs become increasingly noisy (Williamson, 2006).
Protein_catabolism (degrade) of HCI
4) Confidence 0.17 Published 2010 Journal Frontiers in Neuroscience Section Body Doc Link PMC2944670 Disease Relevance 0 Pain Relevance 0
grams of EPA and DHA per day either by an increased consumption of fatty fish or supplementation with fish oil supplements rich in EPA.
Protein_catabolism (grams) of EPA
5) Confidence 0.14 Published 2011 Journal Journal of Obesity Section Body Doc Link PMC2952901 Disease Relevance 0.39 Pain Relevance 0.08
Tissue inhibitor of metalloproteinases-3 (TIMP-3) is one of four TIMP proteins that are natural inhibitors of matrix metalloproteinases (MMP), a group of peptidases that regulate the degradation, composition and turnover of basement membranes and extracellular matrix.
Protein_catabolism (degradation) of metalloproteinases in extracellular matrix associated with metalloproteinase
6) Confidence 0.07 Published 2006 Journal Respir Res Section Body Doc Link PMC1351173 Disease Relevance 0.39 Pain Relevance 0.15
Billinghurst and Poole were the first to report on the use of antibodies to detect neoepitopes of collagen generated by collagenase cleavage (Billinghurst et al. 1997).
Protein_catabolism (cleavage) of collagenase in cleavage
7) Confidence 0.03 Published 2006 Journal Biomark Insights Section Body Doc Link PMC2716783 Disease Relevance 0.14 Pain Relevance 0.07
Collagenase mediated cleavage results in two fragments: a ¾ length fragment (also referred to as TCA) and a ¼ length fragment (TCB).
Protein_catabolism (cleavage) of Collagenase in cleavage
8) Confidence 0.03 Published 2006 Journal Biomark Insights Section Body Doc Link PMC2716783 Disease Relevance 0.07 Pain Relevance 0.09
Tissue inhibitor of metalloproteinases-3 (TIMP-3) is one of four TIMP proteins that are natural inhibitors of matrix metalloproteinases (MMP), a group of peptidases that regulate the degradation, composition and turnover of basement membranes and extracellular matrix.
Protein_catabolism (degradation) of metalloproteinases in basement membranes associated with metalloproteinase
9) Confidence 0.02 Published 2006 Journal Respir Res Section Body Doc Link PMC1351173 Disease Relevance 0.39 Pain Relevance 0.15
Activated CD4+ T cells contribute to stimulation of osteoclastogenesis and activation of metalloproteinases responsible for the degradation of connective tissue, resulting in joint damage.
Protein_catabolism (degradation) of metalloproteinases in connective tissue associated with metalloproteinase
10) Confidence 0.02 Published 2005 Journal Arthritis Res Ther Section Body Doc Link PMC2833970 Disease Relevance 0.61 Pain Relevance 0.72
The neoepitope resulting from collagenase cleavage of triple-helical type II collagen (Col2:3/4Clong, also known as C2C) was measured by means of an enzyme-linked immunosorbent assay (ELISA) [14].
Protein_catabolism (cleavage) of collagenase in cleavage
11) Confidence 0.02 Published 2007 Journal Arthritis Res Ther Section Body Doc Link PMC2212578 Disease Relevance 0.20 Pain Relevance 0.05
BMI = body mass index; BOKS = Boston Osteoarthritis of the Knee Study; C2C (also called Col2:3/4Clong) = collagenase cleavage of triple-helical type II collagen; CI = confidence interval; Col2CTx = crosslinked peptides from the C-telopeptide domain of type II collagen; COMP = cartilage oligomeric matrix protein; CPII = C-propeptide of type II collagen; ELISA = enzyme-linked immunosorbent assay; FOV = field of view; K&L = Kellgren & Lawrence; MRI = magnetic resonance imaging; OA = osteoarthritis; TE = time to echo; TR = repetition time; WORMS = Whole Organ Magnetic Resonance Imaging Score.


Protein_catabolism (cleavage) of collagenase in cleavage associated with helminth infection, obesity, imagery and osteoarthritis
12) Confidence 0.02 Published 2007 Journal Arthritis Res Ther Section Body Doc Link PMC2212578 Disease Relevance 0.79 Pain Relevance 0.53
, which induces a cascade of inflammatory and catabolic events including the expression of cartilage degrading matrix metalloproteinases (MMP) [3], nitric oxygen (NO) production and prostaglandin E2 (PGE2) release [4], while inhibiting proteoglycan and collagen synthesis [5,6].
Protein_catabolism (degrading) of metalloproteinases in cartilage associated with inflammation and metalloproteinase
13) Confidence 0.01 Published 2010 Journal Arthritis Res Ther Section Body Doc Link PMC2911907 Disease Relevance 0.79 Pain Relevance 0.65
While degradation of ECM with enzymes, such as collagenase and MMPs, may improve viral penetration and distribution, on the other hand may also increase tumour spread.
Protein_catabolism (degradation) of collagenase associated with cancer
14) Confidence 0.01 Published 2010 Journal The Open Virology Journal Section Body Doc Link PMC2936037 Disease Relevance 1.37 Pain Relevance 0.04
Experiments have demonstrated that NO plays a catabolic role in the development of OA and mediates the inflammatory response, is involved in the degradation of matrix metalloproteinases, inhibits the synthesis of both collagen and proteoglycans, and helps to mediate apoptosis.
Protein_catabolism (degradation) of metalloproteinases associated with inflammatory response, metalloproteinase, apoptosis and osteoarthritis
15) Confidence 0.01 Published 2008 Journal Arthritis Res Ther Section Abstract Doc Link PMC2582805 Disease Relevance 0.99 Pain Relevance 0.50
Several factors affect degradability of collagen, for example, structure contraction caused by cell penetration, collagenase, gelatinase and other non-specific proteinases can digest collagen [50].
Protein_catabolism (degradability) of collagenase
16) Confidence 0.01 Published 2010 Journal International Journal of Molecular Sciences Section Body Doc Link PMC2956096 Disease Relevance 0.26 Pain Relevance 0.09
Matrix metalloproteinases (MMPs) are known to degrade the cartilage9 and therefore they may have a role in the ingrowth of blood vessels and nerves during the initiation of OA.
Protein_catabolism (degrade) of metalloproteinases in nerves associated with metalloproteinase and osteoarthritis
17) Confidence 0.01 Published 2010 Journal Osteoarthritis and Cartilage Section Body Doc Link PMC2853084 Disease Relevance 0.80 Pain Relevance 0.63
and upregulates the transcription of a number of genes involved in cartilage degradation including iNOS, matrix metalloproteinases and COX-2, as well as IL-1?
Protein_catabolism (degradation) of metalloproteinases in cartilage associated with metalloproteinase
18) Confidence 0.01 Published 2008 Journal Arthritis Res Ther Section Body Doc Link PMC2582805 Disease Relevance 0.29 Pain Relevance 0.16
Matrix metalloproteinases (MMPs) are known to degrade the cartilage9 and therefore they may have a role in the ingrowth of blood vessels and nerves during the initiation of OA.
Protein_catabolism (degrade) of metalloproteinases in blood vessels associated with metalloproteinase and osteoarthritis
19) Confidence 0.00 Published 2010 Journal Osteoarthritis and Cartilage Section Body Doc Link PMC2853084 Disease Relevance 0.80 Pain Relevance 0.63

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