INT192044

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Context Info
Confidence 0.24
First Reported 2006
Last Reported 2008
Negated 0
Speculated 0
Reported most in Body
Documents 2
Total Number 6
Disease Relevance 2.39
Pain Relevance 0

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

cytoplasm (DSP, Jup) structural molecule activity (DSP, Jup) plasma membrane (DSP, Jup)
mitochondrion (DSP) cell morphogenesis (Jup) protein binding, bridging (DSP)
Anatomy Link Frequency
tail 1
filaments 1
plaque 1
DSP (Homo sapiens)
Jup (Mus musculus)
Pain Link Frequency Relevance Heat
Catecholamine 1 16.32 Low Low
Kinase C 65 5.00 Very Low Very Low Very Low
metalloproteinase 30 5.00 Very Low Very Low Very Low
agonist 25 5.00 Very Low Very Low Very Low
corticosteroid 10 5.00 Very Low Very Low Very Low
addiction 10 5.00 Very Low Very Low Very Low
imagery 10 5.00 Very Low Very Low Very Low
Pain 5 5.00 Very Low Very Low Very Low
Inflammatory mediators 5 5.00 Very Low Very Low Very Low
antagonist 5 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Adhesions 260 99.66 Very High Very High Very High
Cataract 1 97.40 Very High Very High Very High
Arrhythmogenic Right Ventricular Dysplasia 60 96.24 Very High Very High Very High
Disease 109 95.52 Very High Very High Very High
Embryonic Lethality 15 80.16 Quite High
Acantholysis 325 71.20 Quite High
Sudden Death 2 71.00 Quite High
Heart Rate Under Development 7 69.80 Quite High
Bullous Skin Disease 1520 66.60 Quite High
Apoptosis 100 63.20 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
To date five candidate genes have been identified, i.e., ryanodine receptor (RyR2 on 1q42), plakoglobin (JUP on 17q21), desmoplakin (DSM on 6p24), plakophilin-2 (PKP2 on 12p11), and transforming growth factor ?
desmoplakin Binding (ryanodine receptor) of JUP
1) Confidence 0.24 Published 2006 Journal BMC Med Genet Section Body Doc Link PMC1444927 Disease Relevance 1.10 Pain Relevance 0
Plakoglobin has been demonstrated to interact with other desmosomal plaque components such as desmoplakin, plakophilins and also with cytokeratin filaments (Bonne et al. 2003; Chen et al. 2002; Kowalczyk et al. 1997; Smith and Fuchs 1998).
desmoplakin Binding (interact) of Plakoglobin in filaments
2) Confidence 0.12 Published 2008 Journal Histochem Cell Biol Section Body Doc Link PMC2413110 Disease Relevance 0.19 Pain Relevance 0
It is believed that the cytoplasmic tail of Dsgs and Dscs interact with plakoglobin which in turn binds to desmoplakin (Fig. 1).
desmoplakin Binding (binds) of plakoglobin in tail
3) Confidence 0.12 Published 2008 Journal Histochem Cell Biol Section Body Doc Link PMC2413110 Disease Relevance 0.20 Pain Relevance 0
Desmoplakin consists of an aminoterminal plakin domain, which can interact with all other desmosomal plaque proteins such as plakoglobin and plakophilins but also with Dsc 1a (Kowalczyk et al. 1997; Smith and Fuchs 1998; Troyanovsky et al. 1994b).
Desmoplakin Binding (interact) of plakoglobin in plaque
4) Confidence 0.12 Published 2008 Journal Histochem Cell Biol Section Body Doc Link PMC2413110 Disease Relevance 0.07 Pain Relevance 0
Moreover, plakoglobin phosphorylation was shown to be required for EGFR-induced loss of cell adhesion and to regulate binding of plakoglobin to desmoplakin (Miravet et al. 2003; Yin et al. 2005).
desmoplakin Binding (binding) of plakoglobin associated with adhesions
5) Confidence 0.12 Published 2008 Journal Histochem Cell Biol Section Body Doc Link PMC2413110 Disease Relevance 0.48 Pain Relevance 0
The linker function of plakoglobin seems to be regulated by tyrosine phosphorylation of plakoglobin because following EGFR activation, phosphorylated plakoglobin remained associated with Dsg 2 but not with desmoplakin (Gaudry et al. 2001).
desmoplakin Binding (associated) of plakoglobin
6) Confidence 0.12 Published 2008 Journal Histochem Cell Biol Section Body Doc Link PMC2413110 Disease Relevance 0.36 Pain Relevance 0

General Comments

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