INT265512

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Context Info
Confidence 0.40
First Reported 2009
Last Reported 2010
Negated 1
Speculated 0
Reported most in Body
Documents 4
Total Number 5
Disease Relevance 1.43
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.

cell proliferation (ERBB2) signal transduction (ERBB2) plasma membrane (ERBB2)
nucleus (ERBB2) cytoplasm (ERBB2)
Anatomy Link Frequency
2C4 2
arm 2
ERBB2 (Homo sapiens)
Pain Link Frequency Relevance Heat
palliative 1 32.16 Quite Low
abdominal pain 2 14.24 Low Low
Pain 4 11.68 Low Low
cva 2 8.16 Low Low
imagery 3 5.00 Very Low Very Low Very Low
Inflammation 2 5.00 Very Low Very Low Very Low
headache 2 5.00 Very Low Very Low Very Low
alcohol 1 5.00 Very Low Very Low Very Low
antagonist 1 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Solid Tumor 17 98.92 Very High Very High Very High
Toxicity 32 94.72 High High
Hyperplasia 4 92.08 High High
Cancer 99 91.84 High High
Apoptosis 9 89.72 High High
Adhesions 3 88.64 High High
Breast Cancer 156 79.88 Quite High
Disease 46 59.36 Quite High
Recurrence 19 39.04 Quite Low
Prostate Cancer 2 34.00 Quite Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Pertuzumab has been shown to bind to the dimerization arm of HER2, blocking HER2/HER3 heterodimerization and attenuating growth of solid tumors in model systems [133].
Negative_regulation (blocking) of HER2 Binding (heterodimerization) of in arm associated with solid tumor
1) Confidence 0.40 Published 2010 Journal Current Genomics Section Body Doc Link PMC2878980 Disease Relevance 0.58 Pain Relevance 0
rhuMAb 2C4 (pertuzumab, RO4368451), a human epidermal growth factor receptor-2 (HER2) targeted antibody that binds to an epitope distinct from trastuzumab, blocks ligand-associated heterodimerization of HER2 with other HER receptor family members.
Negative_regulation (blocks) of HER2 Binding (heterodimerization) of in 2C4
2) Confidence 0.38 Published 2009 Journal Japanese Journal of Clinical Oncology Section Abstract Doc Link PMC2661001 Disease Relevance 0.51 Pain Relevance 0
Unlike HER1, HER3 and HER4, HER2 is considered to be an orphan receptor: no direct ligand for HER2 has been discovered.
Negative_regulation (discovered) of HER2 Neg (no) Binding (ligand) of
3) Confidence 0.37 Published 2009 Journal Japanese Journal of Clinical Oncology Section Body Doc Link PMC2661001 Disease Relevance 0.35 Pain Relevance 0
For instance, it is not uncommon that one protein is annotated with various synonyms in different models (e.g. both HER2 and ERBB2 correspond to the same protein); one generic name used in different models may actually refer to different proteins (e.g.
Negative_regulation (e.g.) of HER2 Binding (correspond) of
4) Confidence 0.35 Published 2010 Journal Nucleic Acids Research Section Body Doc Link PMC2896112 Disease Relevance 0 Pain Relevance 0
For instance, it is not uncommon that one protein is annotated with various synonyms in different models (e.g. both HER2 and ERBB2 correspond to the same protein); one generic name used in different models may actually refer to different proteins (e.g.
Negative_regulation (e.g.) of ERBB2 Binding (correspond) of
5) Confidence 0.35 Published 2010 Journal Nucleic Acids Research Section Body Doc Link PMC2896112 Disease Relevance 0 Pain Relevance 0

General Comments

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