INT282995

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Context Info
Confidence 0.03
First Reported 2009
Last Reported 2010
Negated 2
Speculated 0
Reported most in Body
Documents 21
Total Number 21
Disease Relevance 9.80
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.

cytoplasm (Bcl2, Becn1) mitochondrion (Bcl2) growth (Bcl2)
cell death (Bcl2) nucleus (Bcl2) cell division (Becn1)
Anatomy Link Frequency
groove 3
tail 1
Bcl2 (Mus musculus)
Becn1 (Mus musculus)
Pain Link Frequency Relevance Heat
halothane 19 5.00 Very Low Very Low Very Low
anesthesia 18 5.00 Very Low Very Low Very Low
carbamazepine 2 5.00 Very Low Very Low Very Low
Clonidine 2 5.00 Very Low Very Low Very Low
analgesia 2 5.00 Very Low Very Low Very Low
Substantia nigra 2 5.00 Very Low Very Low Very Low
antagonist 2 5.00 Very Low Very Low Very Low
cerebral cortex 1 5.00 Very Low Very Low Very Low
Inflammation 1 5.00 Very Low Very Low Very Low
Buprenorphine 1 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Apoptosis 1890 100.00 Very High Very High Very High
Starvation 67 99.84 Very High Very High Very High
Sprains And Strains 72 99.36 Very High Very High Very High
Death 65 98.46 Very High Very High Very High
Infection 920 93.20 High High
Viral Infection 234 91.04 High High
Lymphatic System Cancer 18 90.40 High High
Stress 44 89.68 High High
Cold Sores 18 84.56 Quite High
Dna Damage 2 84.52 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
One direct crosstalk between these two pathways is mediated in part by the functional and physical interaction of Beclin1, an essential autophagy activator, with Bcl-2, a prototype apoptosis inhibitor [11],[12].
Bcl-2 Binding (interaction) of Beclin1 associated with apoptosis
1) Confidence 0.03 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2752191 Disease Relevance 0.92 Pain Relevance 0
Beclin1 was originally identified as an interactor of Bcl-2 by a yeast two-hybrid screen [7].
Bcl-2 Binding (interactor) of Beclin1
2) Confidence 0.03 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2752191 Disease Relevance 0.84 Pain Relevance 0
Aside from its ability to interact with and inhibit pro-apoptotic family members like Bax and BH3-only proteins, the hydrophobic pocket of Bcl-2 also binds Beclin1 (the mammalian ortholog of yeast Atg6), which is part of a class III PI3 kinase complex required for the initiation of autophagosome membrane [16],[17].
Bcl-2 Binding (binds) of Beclin1 associated with apoptosis
3) Confidence 0.03 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2752191 Disease Relevance 0.89 Pain Relevance 0
It is also possible that the autophagy induced when Beclin1 is unchecked by vBcl-2 can trigger cell death of latently infected cells, such a scenario is supported by the fact that a Beclin1 mutant unable to bind to Bcl-2 induces caspase-independent autophagic cell death [12].
Bcl-2 Neg (unable) Binding (bind) of Beclin1 associated with death
4) Confidence 0.03 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2752191 Disease Relevance 0.45 Pain Relevance 0
The interaction of Bcl-2 with Beclin1 largely correlates to its anti-autophagic activity [15].
Bcl-2 Binding (interaction) of Beclin1
5) Confidence 0.03 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2752191 Disease Relevance 0 Pain Relevance 0
In fact, the anti-autophagic action of Bcl-2 closely mirrors its capacity to bind and inhibit Beclin1 [12].
Bcl-2 Binding (bind) of Beclin1
6) Confidence 0.03 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2752191 Disease Relevance 0.73 Pain Relevance 0
Wild-type (WT) vBcl-2 readily interacted with Beclin1 BH3-like domain in the yeast two-hybrid assay.
vBcl-2 Binding (interacted) of Beclin1
7) Confidence 0.02 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2752191 Disease Relevance 0.21 Pain Relevance 0
1 helix leads to the loss of both Beclin1 binding and autophagy suppressing activity, reflecting a striking correlation between the ability of vBcl-2 to bind Beclin1 and its protection from Beclin1-mediated autophagy.
vBcl-2 Binding (ability) of Beclin1
8) Confidence 0.02 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2752191 Disease Relevance 0 Pain Relevance 0
However, the Beclin1 peptide (KD 40 nM) binds to vBcl-2 with a much higher affinity than is observed for the Bak (KD 76 nM) and Bax peptides (KD 690 nM) [28], raising the possibility that Beclin1 may not necessarily share binding sites with the pro-apoptotic Bcl-2 family members for the hydrophobic groove of vBcl-2.
vBcl-2 Binding (binds) of Beclin1 in groove associated with apoptosis
9) Confidence 0.02 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2752191 Disease Relevance 0.57 Pain Relevance 0
Furthermore, the binding of purified vBcl-2 protein to the Beclin1-derived peptide appears to be the tightest when compared to peptides from the pro-apoptotic proteins, including BAX, BAK, BIM, PUMA, BID, and Noxa [28].
vBcl-2 Binding (binding) of Beclin1 associated with apoptosis
10) Confidence 0.02 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2752191 Disease Relevance 0.32 Pain Relevance 0
Nonetheless, due to the engagement of the hydrophobic surface groove of vBcl-2 by both the pro-autophagic BH3 domain of Beclin1 and the pro-apoptotic BH3 domain [28], mutations of vBcl-2 identified so far that disrupt Beclin1 binding and inhibition of autophagy also abolish its capacity to interact with BH3 peptides and inhibit apoptosis, adding to the complexity of genetically dissecting the in vivo role of vBcl-2-mediated autophagy inhibition and the vBcl-2-mediated antagonism of apoptosis in ?
vBcl-2 Binding (binding) of Beclin1 in groove associated with apoptosis
11) Confidence 0.02 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2752191 Disease Relevance 0.73 Pain Relevance 0
Moreover, our study indicates that despite their structural overlap, Beclin1 and pro-apoptotic Bcl-2 proteins interact with vBcl-2 through two discrete modes of binding that are dependent on a distinct region of vBcl-2.
vBcl-2 Binding (interact) of Beclin1 associated with apoptosis
12) Confidence 0.02 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2752191 Disease Relevance 0.83 Pain Relevance 0
We show that removing the BH2 domain from vBcl-2 does not affect vBcl-2's capacity to bind and suppress Beclin1, but it significantly dampens its anti-apoptotic activity.
vBcl-2 Binding (bind) of Beclin1 associated with apoptosis
13) Confidence 0.02 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2752191 Disease Relevance 0.71 Pain Relevance 0
Given the pivotal role of vBcl-2 in apoptosis inhibition, it is important to know if the regions of vBcl-2, which is required for binding and inhibiting Beclin1, are equally or differentially required for blocking apoptosis.
vBcl-2 Binding (binding) of Beclin1 associated with apoptosis
14) Confidence 0.02 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2752191 Disease Relevance 0.63 Pain Relevance 0
7 or BH2, one of the central components of the vBcl-2 hydrophobic cleft, had no significant effect on the interaction between vBcl-2 and Beclin1, as was seen with the deletion mutation of the C-terminal hydrophobic ‘tail’ (?
vBcl-2 Neg (no) Binding (interaction) of Beclin1 in tail
15) Confidence 0.02 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2752191 Disease Relevance 0 Pain Relevance 0
We then assessed the effects of the vBcl-2 mutants binding to Beclin1, in particular that of ??
vBcl-2 Binding (binding) of Beclin1
16) Confidence 0.02 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2752191 Disease Relevance 0 Pain Relevance 0
To analyze the interactions between the Beclin1 and vBcl-2 mutants, yeast strain AH109, expressing the BH3-like domain of Beclin1 fused to the Gal4 activation domain in the pGADT7 plasmid, was used to transform pGBKT7 plasmids containing the mutants of vBcl-2, and the transformants then assayed for ?
vBcl-2 Binding (interactions) of Beclin1 associated with sprains and strains
17) Confidence 0.02 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2752191 Disease Relevance 0.30 Pain Relevance 0
In contrast, a vBcl-2 mutant with a triple alanine substitution at the conserved residues of Ser85, Gly86, and Arg87 (hereafter termed as vBcl-2 AAA) within the BH3 binding groove that has been shown to abrogate BH3 peptide binding of vBcl-2, lost the ability to interact with Beclin1 (Figure 1).
vBcl-2 Binding (interact) of Beclin1 in groove
18) Confidence 0.02 Published 2009 Journal PLoS Pathogens Section Body Doc Link PMC2752191 Disease Relevance 0.15 Pain Relevance 0
Autophagy can be inhibited by the binding of the apoptosis-related proteins Bcl-2 or Bcl-XL to Beclin 1.
Bcl-2 Binding (binding) of Beclin 1 associated with apoptosis
19) Confidence 0.01 Published 2010 Journal Seminars in Cell & Developmental Biology Section Body Doc Link PMC2938570 Disease Relevance 0.76 Pain Relevance 0
Starvation induces Jun N-terminal kinase 1 (Jnk1) activity, which phosphorylates Bcl-2, thereby disrupting the interaction between Beclin 1 and Bcl-2 to induce autophagy [21].
Bcl-2 Binding (interaction) of Beclin 1 associated with starvation
20) Confidence 0.01 Published 2010 Journal Seminars in Cell & Developmental Biology Section Body Doc Link PMC2938570 Disease Relevance 0.76 Pain Relevance 0

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