INT130194

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Context Info
Confidence 0.65
First Reported 2005
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 9
Total Number 9
Disease Relevance 0.97
Pain Relevance 0.70

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

extracellular region (PROK1)
Anatomy Link Frequency
IL2R 1
decidua 1
corpus luteum 1
kidney 1
PROK1 (Homo sapiens)
Pain Link Frequency Relevance Heat
Potency 1 100.00 Very High Very High Very High
metalloproteinase 10 97.12 Very High Very High Very High
tolerance 1 96.84 Very High Very High Very High
cytokine 28 95.16 Very High Very High Very High
Paracetamol 3 83.28 Quite High
cINOD 4 81.08 Quite High
Pain 9 75.60 Quite High
antagonist 4 61.80 Quite High
Inflammation 4 45.92 Quite Low
Inflammatory response 2 41.32 Quite Low
Disease Link Frequency Relevance Heat
Cancer 20 83.92 Quite High
Fever 2 79.64 Quite High
Peripheral Arterial Disease 5 79.32 Quite High
Adhesions 10 78.56 Quite High
Pain 8 75.60 Quite High
Neurodegenerative Disease 7 74.52 Quite High
Bordatella Infection 2 72.64 Quite High
Hematological Disease 13 71.32 Quite High
Leukemia 9 67.84 Quite High
Hyperplasia 13 58.88 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Furthermore we have shown that the PROK1–PROKR1 induction of IL-11 is mediated via the calcineurin signalling pathway in a Gq/11, calcium and ERK dependent manner as shown schematically in Fig. 6.
Positive_regulation (induction) of PROK1-PROKR1
1) Confidence 0.65 Published 2010 Journal Molecular Human Reproduction Section Body Doc Link PMC2816169 Disease Relevance 0 Pain Relevance 0.09
IL-11 induction via PROK1–PROKR1 may affect blastocyst implantation by increasing the expression of the metalloproteinase inhibitor, ?
Positive_regulation (induction) of PROK1-PROKR1 associated with metalloproteinase
2) Confidence 0.47 Published 2010 Journal Molecular Human Reproduction Section Body Doc Link PMC2816169 Disease Relevance 0.15 Pain Relevance 0.09
Moreover we have shown that overexpression of RCAN1-4 leads to a reduction in PROK1 induced IL-11 indicating that RCAN1-4 is acting as a negative regulator of PROK1–PROKR1 mediated IL-11 signalling as summarized in Fig. 6.
Positive_regulation (induced) of PROK1
3) Confidence 0.47 Published 2010 Journal Molecular Human Reproduction Section Body Doc Link PMC2816169 Disease Relevance 0 Pain Relevance 0
PROK1–PROKR1 stimulation in PROKR1 Ishikawa cells resulted in a significant increase in IL-11 mRNA expression which was maximal between 8 and 12 h (P < 0.005, Fig. 1A).
Positive_regulation (stimulation) of PROK1-PROKR1
4) Confidence 0.44 Published 2010 Journal Molecular Human Reproduction Section Body Doc Link PMC2816169 Disease Relevance 0.08 Pain Relevance 0
PROK1 and PROKR1 show differential expression across the menstrual cycle and in first trimester decidua, with increased endometrial expression of PROK1 observed in the mid-secretory phase and both PROK1 and PROKR1 increased in first trimester decidua.
Positive_regulation (increased) of PROK1 in decidua
5) Confidence 0.44 Published 2010 Journal Molecular Human Reproduction Section Body Doc Link PMC2816169 Disease Relevance 0.29 Pain Relevance 0.08
Their sequences are almost identical in the transmembrane domains [16], suggesting that their activation mechanisms are identical and that small-molecule analogues will not discriminate between the receptors, as is the case for PK1 and PK2.
Positive_regulation (case) of PK1
6) Confidence 0.40 Published 2007 Journal Trends in Endocrinology and Metabolism Section Body Doc Link PMC2694302 Disease Relevance 0.07 Pain Relevance 0.03
In the corpus luteum, the mRNA expression of PK1 increases as the corpus luteum matures, whereas VEGF expression is already maximal at the early luteal phase [21,22].
Positive_regulation (increases) of PK1 in corpus luteum
7) Confidence 0.40 Published 2007 Journal Trends in Endocrinology and Metabolism Section Body Doc Link PMC2694302 Disease Relevance 0.06 Pain Relevance 0
This resulted in a 5-fold greater affinity for IL2R and a 10-fold increase in potency.25,26 The resulting DAB389-IL2 fusion protein toxin is otherwise known as denileukin diftitox.
Positive_regulation (increase) of protein toxin in IL2R associated with potency
8) Confidence 0.02 Published 2010 Journal Cancer management and research Section Body Doc Link PMC3004568 Disease Relevance 0.33 Pain Relevance 0.18
Both CINODs donated bioavailable NO, as detected by cGMP induction in the pig kidney transformed cell line, LLC-PK1, but NMI-1182 was more potent by 30-100 times than AZD3582, GTN, GDN, and ISDN and considerably faster in inducing cGMP synthesis than AZD3582.
Positive_regulation (induction) of LLC-PK1 in kidney
9) Confidence 0.01 Published 2005 Journal Biochem. Pharmacol. Section Abstract Doc Link 16168964 Disease Relevance 0 Pain Relevance 0.23

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