INT298868

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Context Info
Confidence 0.07
First Reported 2010
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 4
Disease Relevance 1.64
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.

Golgi apparatus (RAB7A, GOPC) plasma membrane (GOPC) GTPase activity (RAB7A)
cytoplasm (GOPC) lysosome (RAB7A)
RAB7A (Homo sapiens)
GOPC (Homo sapiens)
Pain Link Frequency Relevance Heat
imagery 20 5.84 Low Low
Pain 12 5.00 Very Low Very Low Very Low
Congenital analgesia 4 5.00 Very Low Very Low Very Low
Demyelination 4 5.00 Very Low Very Low Very Low
Nerve growth factor 4 5.00 Very Low Very Low Very Low
Peripheral nervous system 4 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Disease 304 100.00 Very High Very High Very High
Charcot Marie Tooth Disease 24 5.00 Very Low Very Low Very Low
Neurodegenerative Disease 16 5.00 Very Low Very Low Very Low
Pain 16 5.00 Very Low Very Low Very Low
Neurological Disease 8 5.00 Very Low Very Low Very Low
Syndrome 8 5.00 Very Low Very Low Very Low
Mouth Disease 8 5.00 Very Low Very Low Very Low
Ulcers 4 5.00 Very Low Very Low Very Low
Demyelinating Disease 4 5.00 Very Low Very Low Very Low
Muscle Weakness 4 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
The L129F substitution does not alter the overall structure of the molecule as compared to the published structure of wild-type Rab7 bound to GppNHp (PDB 1VG8) (Fig. 1A–C, Supplementary Material, Fig.
Rab7 Binding (bound) of Fig
1) Confidence 0.07 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2830827 Disease Relevance 0.21 Pain Relevance 0
Using LC-MS/MS, we demonstrate that disease-causing mutations do not qualitatively alter the complement of Rab7 interactors but cause quantitative changes in specific interactions (Fig. 4).
Rab7 Binding (interactions) of Fig associated with disease
2) Confidence 0.07 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2830827 Disease Relevance 0.67 Pain Relevance 0
Surprisingly, despite evidence of unregulated activation, Rab7 disease mutants have normal subcellular localization and associate normally with LAMP2 (Fig. 5B) and LysoTracker Red (data not shown).
Rab7 Binding (associate) of Fig associated with disease
3) Confidence 0.07 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2830827 Disease Relevance 0.56 Pain Relevance 0
The L129F substitution does not alter the overall structure of the molecule as compared to the published structure of wild-type Rab7 bound to GppNHp (PDB 1VG8) (Fig. 1A–C, Supplementary Material, Fig.
Rab7 Binding (bound) of Fig
4) Confidence 0.07 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2830827 Disease Relevance 0.21 Pain Relevance 0

General Comments

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