INT176242

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Context Info
Confidence 0.42
First Reported 2004
Last Reported 2010
Negated 1
Speculated 0
Reported most in Body
Documents 10
Total Number 17
Disease Relevance 10.18
Pain Relevance 0.52

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

mitochondrion (Bax) endoplasmic reticulum (Bax) intracellular (Bax)
cytoplasm (Bax) cytosol (Bax) cell proliferation (Bax)
Anatomy Link Frequency
pore 1
Bax (Mus musculus)
Pain Link Frequency Relevance Heat
Neuropeptide 28 98.16 Very High Very High Very High
Central nervous system 21 91.32 High High
cINOD 10 88.44 High High
Hippocampus 10 86.84 High High
addiction 25 81.84 Quite High
cerebral cortex 15 74.16 Quite High
Spinal cord 81 72.52 Quite High
medulla 1 68.76 Quite High
Inflammation 75 50.00 Quite Low
antagonist 12 31.00 Quite Low
Disease Link Frequency Relevance Heat
Apoptosis 794 99.64 Very High Very High Very High
Adhesions 8 98.60 Very High Very High Very High
Neurodegenerative Disease 48 98.08 Very High Very High Very High
Spinal Cord Injury 122 97.20 Very High Very High Very High
Dementia 13 96.80 Very High Very High Very High
Urological Neuroanatomy 9 94.96 High High
Cancer 139 94.08 High High
Prostate Cancer 27 93.60 High High
Autoimmune Disease 9 93.20 High High
INFLAMMATION 103 88.20 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
First, the interaction of BAX with a binding partner could be affected by low levels of BAX protein, especially if the binding partner had a reduced affinity for BAX in its globular conformation.
BAX Binding (interaction) of
1) Confidence 0.42 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2964639 Disease Relevance 0.59 Pain Relevance 0.04
These proteins generally exist in or at the surface of the MOM, and may interact directly with BAK and BAX to prevent an accidental insertion event at the membrane surface.
BAX Binding (interact) of
2) Confidence 0.42 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2964639 Disease Relevance 0.91 Pain Relevance 0
Under these conditions, aggregation by cooperative binding may rely on passive diffusion of cytosolic BAX, which are only captured at the MOM when they randomly collide with MOM-bound BAX proteins.
BAX Binding (bound) of
3) Confidence 0.37 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2964639 Disease Relevance 0.28 Pain Relevance 0
immunoreactivity of Bax, a proapoptotic protein regulated in part by VNs in
Bax Binding (immunoreactivity) of associated with neuropeptide
4) Confidence 0.36 Published 2008 Journal Mediators of Inflammation Section Body Doc Link PMC2643053 Disease Relevance 1.22 Pain Relevance 0.20
GFP-BAX aggregation is impaired at sub-lethal levels of expression
GFP-BAX Binding (aggregation) of
5) Confidence 0.32 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2964639 Disease Relevance 0.64 Pain Relevance 0
Under these conditions, aggregation by cooperative binding may rely on passive diffusion of cytosolic BAX, which are only captured at the MOM when they randomly collide with MOM-bound BAX proteins.
BAX Binding (bound) of
6) Confidence 0.32 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2964639 Disease Relevance 0.28 Pain Relevance 0
In particular, Bax can homodimerize with itself and heterodimerize with Bcl-2 or Bcl-xL.
Bax Binding (homodimerize) of
7) Confidence 0.31 Published 2007 Journal BMC Cancer Section Body Doc Link PMC2222640 Disease Relevance 0.64 Pain Relevance 0
Furthermore, experiments using a GFP-BAX fusion protein, indicate that normal aggregation of BAX is impaired at non-lethal levels, suggesting that the level of BAX is critical for the successful activation of this proapoptotic protein, and not related to overcoming a defined number of anti-apoptotic proteins.


BAX Binding (aggregation) of associated with apoptosis
8) Confidence 0.31 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2964639 Disease Relevance 0.88 Pain Relevance 0.09
The activation of BAX during apoptosis is simplistically divided into four basic steps, including initial activation (conformational change) of cytosolic monomers, translocation to the MOM and insertion into this membrane, secondary recruitment of inactivate BAX monomers by MOM-bound BAX molecules, and aggregation of bound and recruited BAX molecules into oligomers that enable the release of cytochrome c.
BAX Binding (bound) of associated with apoptosis
9) Confidence 0.31 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2964639 Disease Relevance 0.53 Pain Relevance 0
First, the interaction of BAX with a binding partner could be affected by low levels of BAX protein, especially if the binding partner had a reduced affinity for BAX in its globular conformation.
BAX Binding (affinity) of
10) Confidence 0.31 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2964639 Disease Relevance 0.41 Pain Relevance 0.04
, nitrotyrosine, S-100, PAR, Fas Ligand (FasL), Bax and Bcl-2
Bax Binding (nitrotyrosine) of
11) Confidence 0.26 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2935363 Disease Relevance 0.64 Pain Relevance 0.07
These latter studies also provide a rational explanation for the presence of the protein in the cytoplasmic compartment where it has been shown to influence TGFbeta-mediated signaling and inhibit apoptosis through a direct interaction with activated Bax [43].
Bax Neg (inhibit) Binding (interaction) of associated with apoptosis
12) Confidence 0.25 Published 2010 Journal BMC Cancer Section Body Doc Link PMC2856549 Disease Relevance 0.34 Pain Relevance 0
Although the function(s) of clusterin remains somewhat enigmatic, recent studies indicate that antiapoptotic effects are mediated in part through direct interactions with activated Bax [22].
Bax Binding (interactions) of
13) Confidence 0.20 Published 2007 Journal Genome Biol Section Body Doc Link PMC2394769 Disease Relevance 0.74 Pain Relevance 0
Acetylation of Ku70 seems to inhibit the interaction with Bax and promote apoptosis (Cohen et al., 2004).
Bax Binding (interaction) of associated with apoptosis
14) Confidence 0.18 Published 2010 Journal The Journal of Cell Biology Section Body Doc Link PMC2867301 Disease Relevance 0.25 Pain Relevance 0
For example, we found that estrogen promotes p53 phosphorylation [37], but uncouples p53 from its regulation of Bax, a mitochondrial-associated pro-apoptotic factor.
Bax Binding (regulation) of associated with apoptosis
15) Confidence 0.09 Published 2004 Journal BMC Neurosci Section Body Doc Link PMC395829 Disease Relevance 0.67 Pain Relevance 0.08
Whether this complex leads to association with the VDAC/ANT ion channel formation, or activated BAX complex solely causes pore formation and subsequent cytochrome c release, is currently not understood.
BAX Binding (complex) of in pore
16) Confidence 0.09 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2908617 Disease Relevance 0.88 Pain Relevance 0
In viable cells, Bcl-XL binds Bax and Bak, thus keeping them in an inactive form.
Bax Binding (binds) of
17) Confidence 0.04 Published 2006 Journal BMC Neurosci Section Body Doc Link PMC1775042 Disease Relevance 0.28 Pain Relevance 0

General Comments

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