INT178548

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Context Info
Confidence 0.70
First Reported 2004
Last Reported 2004
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 2
Disease Relevance 1.52
Pain Relevance 0.07

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

nuclear envelope (AAAS) small molecule metabolic process (AAAS) carbohydrate metabolic process (AAAS)
transmembrane transport (AAAS) cytoplasm (AAAS) nucleocytoplasmic transport (AAAS)
Anatomy Link Frequency
pore 2
AAAS (Homo sapiens)
Pain Link Frequency Relevance Heat
imagery 6 68.76 Quite High
anesthesia 2 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Syndrome 44 96.44 Very High Very High Very High
Hypersensitivity 8 74.32 Quite High
Disorders Of The Lacrimal System 24 71.12 Quite High
Congenital Anomalies 8 65.28 Quite High
Miosis 2 60.56 Quite High
Amblyopia 6 53.40 Quite High
Optic Atrophy 4 29.16 Quite Low
Neurodegenerative Disease 2 17.44 Low Low
Reprotox - General 1 2 6.36 Low Low
Pressure Volume 2 Under Development 4 5.64 Low Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
WD proteins are a functionally diverse family whose members are involved in processes such as cell division, cell-fate determination, transcription, transmembrane signaling and intracellular trafficking. [23] Proteomic analysis of the mammalian nuclear pore complex (NPC) has shown that ALADIN is part of this structure, which is critical for communication between the nucleus and the cytoplasm of cells. [24] When mutated, ALADIN localizes to the cytoplasm, rather than the NPC. [25] However, cells from a subject with triple-A syndrome showed morphologically normal NPCs.
Localization (localizes) of ALADIN in pore associated with syndrome
1) Confidence 0.70 Published 2004 Journal BMC Ophthalmol Section Body Doc Link PMC459227 Disease Relevance 0.71 Pain Relevance 0.03
WD proteins are a functionally diverse family whose members are involved in processes such as cell division, cell-fate determination, transcription, transmembrane signaling and intracellular trafficking. [23] Proteomic analysis of the mammalian nuclear pore complex (NPC) has shown that ALADIN is part of this structure, which is critical for communication between the nucleus and the cytoplasm of cells. [24] When mutated, ALADIN localizes to the cytoplasm, rather than the NPC. [25] However, cells from a subject with triple-A syndrome showed morphologically normal NPCs.
Localization (localizes) of ALADIN in pore associated with syndrome
2) Confidence 0.61 Published 2004 Journal BMC Ophthalmol Section Body Doc Link PMC459227 Disease Relevance 0.81 Pain Relevance 0.03

General Comments

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