INT189353

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Context Info
Confidence 0.40
First Reported 2006
Last Reported 2009
Negated 0
Speculated 1
Reported most in Body
Documents 11
Total Number 13
Disease Relevance 0.93
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.

nucleoplasm (RAD51) mitochondrion (RAD51) nucleus (RAD51)
cytoplasm (RAD51)
Anatomy Link Frequency
band 1
nucleus 1
RAD51 (Homo sapiens)
Pain Link Frequency Relevance Heat
IPN 9 40.56 Quite Low
imagery 17 5.00 Very Low Very Low Very Low
Pain 5 5.00 Very Low Very Low Very Low
palliative 2 5.00 Very Low Very Low Very Low
COX-2 inhibitor 1 5.00 Very Low Very Low Very Low
metalloproteinase 1 5.00 Very Low Very Low Very Low
anesthesia 1 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Immunization 9 94.48 High High
Breast Cancer 167 89.64 High High
Sprains And Strains 20 83.20 Quite High
Hypersensitivity 11 81.20 Quite High
Disease 38 75.20 Quite High
Cancer 107 71.72 Quite High
Fanconi Anemia 2 50.52 Quite High
Cockayne Syndrome 10 50.00 Quite Low
Noninfiltrating Intraductal Carcinoma 21 5.00 Very Low Very Low Very Low
Targeted Disruption 20 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
These results showed that rEhRAD51 was able to efficiently bind both ssDNA and dsDNA substrates in vitro.


rEhRAD51 Binding (bind) of
1) Confidence 0.40 Published 2008 Journal BMC Mol Biol Section Body Doc Link PMC2324109 Disease Relevance 0 Pain Relevance 0
To prevent that EhRAD51 binds and shifts the pgp200 probe, samples were deproteinized with proteinase K (1 mg/ml) at 37°C for 10 min.
EhRAD51 Binding (binds) of
2) Confidence 0.40 Published 2008 Journal BMC Mol Biol Section Body Doc Link PMC2324109 Disease Relevance 0.08 Pain Relevance 0
Taking in consideration that the EhRAD51 sequence lacks a nuclear localization signal, an alternative possibility might be that EhRAD51 needs to interact with other protein(s) to be transported inside the nucleus.
EhRAD51 Spec (might) Binding (interact) of in nucleus
3) Confidence 0.40 Published 2008 Journal BMC Mol Biol Section Body Doc Link PMC2324109 Disease Relevance 0 Pain Relevance 0
EhRAD51 was able to bind both ssDNA and dsDNA substrates in the presence of ATP and Mg2+.
EhRAD51 Binding (bind) of
4) Confidence 0.40 Published 2008 Journal BMC Mol Biol Section Body Doc Link PMC2324109 Disease Relevance 0 Pain Relevance 0
Since UV-C treatment did not affect trophozoites viability, it is tempting to suggest that DNA repair mechanisms involving EhRAD51 foci formation were activated to restore genome integrity after genotoxic insult.
EhRAD51 Binding (formation) of
5) Confidence 0.31 Published 2008 Journal BMC Mol Biol Section Body Doc Link PMC2324109 Disease Relevance 0 Pain Relevance 0
rEhRAD51 exhibits DNA binding activity in vitro
rEhRAD51 Binding (binding) of
6) Confidence 0.31 Published 2008 Journal BMC Mol Biol Section Body Doc Link PMC2324109 Disease Relevance 0 Pain Relevance 0
These antibodies recognized the 47 kDa rEhRAD51 band (Fig. 5B, lane 4), whereas the preimmune serum, used as negative control, did not detect any signal (Fig. 5B, lane 3).
rEhRAD51 Binding (recognized) of in band
7) Confidence 0.31 Published 2008 Journal BMC Mol Biol Section Body Doc Link PMC2324109 Disease Relevance 0.08 Pain Relevance 0
rEhRAD51 exhibits DNA binding activity in vitro
rEhRAD51 Binding (activity) of
8) Confidence 0.31 Published 2008 Journal BMC Mol Biol Section Body Doc Link PMC2324109 Disease Relevance 0 Pain Relevance 0
IgGs were purified through protein G sepharose chromatography and tested for reactivity against rEhRAD51 protein by Western blot assays.


rEhRAD51 Binding (reactivity) of
9) Confidence 0.30 Published 2008 Journal BMC Mol Biol Section Body Doc Link PMC2324109 Disease Relevance 0.09 Pain Relevance 0
For example, the functional consequences of CtIP ubiquitylation and its implications for RAD51 recruitment are not yet known; furthermore, it is likely that there are other substrates for BRCA1/BARD1.
RAD51 Binding (recruitment) of
10) Confidence 0.13 Published 2008 Journal Breast Cancer Res Section Body Doc Link PMC2397525 Disease Relevance 0.67 Pain Relevance 0
ERCC1-XPF endonuclease is not required for RAD51 foci formation, but essential for completion of mitomycin C-induced HR
RAD51 Binding (formation) of
11) Confidence 0.06 Published 2009 Journal Nucleic Acids Research Section Body Doc Link PMC2770670 Disease Relevance 0 Pain Relevance 0
However, RAD54, which is also a member of this family, forms a complex with RAD51, and the RAD51/RAD54 heterodimer also catalyzes homologous DNA pairing with high efficiency (24).
RAD51 Binding (heterodimer) of
12) Confidence 0.06 Published 2006 Journal Nucleic Acids Research Section Body Doc Link PMC1331990 Disease Relevance 0 Pain Relevance 0
Furthermore, we find that ERCC1-defective UV4DR.7 cells form RAD51 foci equally well as the same cells complemented with wild-type ERCC1 (Figure 7B), suggesting that ERCC1 is not critical for RAD51 loading at DSBs and initiation of HR.
RAD51 Binding (loading) of
13) Confidence 0.05 Published 2009 Journal Nucleic Acids Research Section Body Doc Link PMC2770670 Disease Relevance 0 Pain Relevance 0

General Comments

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