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Context Info
Confidence 0.36
First Reported 1998
Last Reported 2010
Negated 0
Speculated 0
Reported most in Abstract
Documents 2
Total Number 2
Disease Relevance 1.44
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.

extracellular space (CLEC3B) extracellular region (CLEC3B) cytoplasm (CLEC3B)
CLEC3B (Homo sapiens)
Pain Link Frequency Relevance Heat
palliative 1 25.00 Low Low
tolerance 1 5.00 Very Low Very Low Very Low
Pain 1 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Metastasis 24 96.16 Very High Very High Very High
Cancer 28 95.24 Very High Very High Very High
Malignant Neoplastic Disease 2 88.08 High High
Solid Tumor 1 87.88 High High
Colon Cancer 2 84.48 Quite High
Skin Cancer 47 83.20 Quite High
Advanced Or Metastatic Breast Cancer 2 81.20 Quite High
Ovarian Cancer 7 71.60 Quite High
Infection 1 69.44 Quite High
Residual Neoplasm 2 25.00 Low Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
By binding to plasminogen, tetranectin may enhance activation of plasminogen to plasmin, which plays a role in the degradation of extracellular proteins and cancer progression.
tetranectin Binding (binding) of associated with cancer
1) Confidence 0.36 Published 2010 Journal International Journal of Molecular Sciences Section Body Doc Link PMC2956083 Disease Relevance 1.21 Pain Relevance 0
From its discovery in 1986 tetranectin (TN) has been suggested to participate in proteolytic processes through its binding to plasminogen, which enhances the activation of plasminogen to plasmin.
tetranectin Binding (binding) of
2) Confidence 0.30 Published 1998 Journal APMIS Suppl. Section Abstract Doc Link 9868384 Disease Relevance 0.23 Pain Relevance 0

General Comments

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