INT174104

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Context Info
Confidence 0.16
First Reported 2003
Last Reported 2003
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 2
Disease Relevance 0.98
Pain Relevance 0.09

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

extracellular space (HSPG2, Ache) extracellular region (HSPG2, Ache) plasma membrane (HSPG2, Ache)
nuclear envelope (Ache) small molecule metabolic process (HSPG2) Golgi apparatus (Ache)
Anatomy Link Frequency
synapse 2
HSPG2 (Homo sapiens)
Ache (Mus musculus)
Pain Link Frequency Relevance Heat
Neurotransmitter 2 95.00 High High
carbamazepine 10 19.28 Low Low
anesthesia 8 16.00 Low Low
Disease Link Frequency Relevance Heat
Syndrome 44 88.16 High High
Exencephaly /

Neural Tube Defects

2 78.84 Quite High
Cleidocranial Dysplasia 10 78.16 Quite High
Contracture 14 58.08 Quite High
Congenital Anomalies 6 56.56 Quite High
Hypopituitarism 26 50.00 Quite Low
Ocular Toxicity (including Many Sub-types) 4 43.84 Quite Low
Myopia 6 43.20 Quite Low
Cataract 2 41.52 Quite Low
Bone Cancer 4 38.12 Quite Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Peng et al. (1999) demonstrated that perlecan in vitro binds to acetylcholinesterase, and postulated that the perlecan-dystroglycan complex may function as an acceptor molecule for acetylcholinesterase at the neuromuscular junction. [9] Arikawa-Hirasawa et al. (2002) have shown that in perlecan-null mice, agrin and acetylcholine molecules were present at the neuromuscular junction but acetylcholinesterase was totally absent, indicating that perlecan binds acetylcholinesterase and localizes it at the synapse. [10]
perlecan Binding (binds) of acetylcholinesterase in synapse
1) Confidence 0.16 Published 2003 Journal BMC Neurol Section Body Doc Link PMC166146 Disease Relevance 0.44 Pain Relevance 0.04
Peng et al. (1999) demonstrated that perlecan in vitro binds to acetylcholinesterase, and postulated that the perlecan-dystroglycan complex may function as an acceptor molecule for acetylcholinesterase at the neuromuscular junction. [9] Arikawa-Hirasawa et al. (2002) have shown that in perlecan-null mice, agrin and acetylcholine molecules were present at the neuromuscular junction but acetylcholinesterase was totally absent, indicating that perlecan binds acetylcholinesterase and localizes it at the synapse. [10]
perlecan Binding (binds) of acetylcholinesterase in synapse
2) Confidence 0.10 Published 2003 Journal BMC Neurol Section Body Doc Link PMC166146 Disease Relevance 0.39 Pain Relevance 0.05

General Comments

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