INT283550

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Context Info
Confidence 0.33
First Reported 2008
Last Reported 2009
Negated 0
Speculated 0
Reported most in Body
Documents 2
Total Number 3
Disease Relevance 0.11
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.

endosome (Cav1) mitochondrion (Cav1) Golgi apparatus (Cav1)
endoplasmic reticulum (Cav1) intracellular (Cav1) protein complex (Cav1)
Anatomy Link Frequency
HeLa 2
Cav1 (Mus musculus)
Pain Link Frequency Relevance Heat
potassium channel 4 5.00 Very Low Very Low Very Low
anesthesia 3 5.00 Very Low Very Low Very Low
addiction 1 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Disorder Of Lipid Metabolism 2 59.00 Quite High
Targeted Disruption 7 52.04 Quite High
Stress 2 42.08 Quite Low
Syndrome 2 28.20 Quite Low
Congenital Anomalies 4 27.80 Quite Low
Apoptosis 3 5.00 Very Low Very Low Very Low
Vibrio Infection 3 5.00 Very Low Very Low Very Low
Infection 2 5.00 Very Low Very Low Very Low
Metabolic Disorder 1 5.00 Very Low Very Low Very Low
Cognitive Disorder 1 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
The maxi-K channel contains a consensus caveolin-binding motif (1007YNMLCFGIY1015) in its C-terminus [26], and mutation of phenylalanine within the caveolin-binding motif had previously been shown to disrupt the association between the ganglioside-specific sialidase Neu3 and cav-1 [27].
Negative_regulation (disrupt) of cav-1 Binding (association) of
1) Confidence 0.33 Published 2009 Journal Reprod Biol Endocrinol Section Body Doc Link PMC2785819 Disease Relevance 0 Pain Relevance 0
A recent study investigating similar maxi-K channel mutants in HEK 293 cells found that single, double and triple substitutions of these aromatic amino acids fail to disrupt the interaction between the maxi-K channel and cav-1, but that complete deletion of the consensus site abolishes almost all (80-85%) interaction with cav-1 [8].
Negative_regulation (abolishes) of cav-1 Binding (interaction) of
2) Confidence 0.33 Published 2009 Journal Reprod Biol Endocrinol Section Body Doc Link PMC2785819 Disease Relevance 0 Pain Relevance 0
However, it was shown that desmosterol in model membranes promotes the formation and stability of ordered domains somewhat less efficiently than cholesterol [53, 55], and recent data show that inhibition of 24-dehydrocholesterol reductase in HeLa cells increases the structural heterogeneity of caveolae due to a decreased affinity of caveolin-1 for sterol and a reduced stability of caveolin oligomers [19].
Negative_regulation (decreased) of caveolin-1 Binding (affinity) of in HeLa
3) Confidence 0.14 Published 2008 Journal Neurochem Res Section Body Doc Link PMC2758381 Disease Relevance 0.11 Pain Relevance 0

General Comments

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