INT241235

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Context Info
Confidence 0.48
First Reported 2007
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 11
Total Number 11
Disease Relevance 2.43
Pain Relevance 0.55

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

cytoskeletal protein binding (Pkd2) transport (Pkd2) endoplasmic reticulum (Pkd2)
plasma membrane (Pkd2) cilium (Pkd2) transmembrane transport (Pkd2)
Anatomy Link Frequency
oocytes 2
ciliary 1
Pkd2 (Mus musculus)
Pain Link Frequency Relevance Heat
TRP channel 56 99.56 Very High Very High Very High
Mechanosensation 22 97.40 Very High Very High Very High
qutenza 7 47.76 Quite Low
metalloproteinase 1 42.64 Quite Low
Cholecystokinin 1 20.88 Low Low
imagery 31 5.00 Very Low Very Low Very Low
Somatostatin 8 5.00 Very Low Very Low Very Low
tail-flick 7 5.00 Very Low Very Low Very Low
Inflammation 7 5.00 Very Low Very Low Very Low
Thermal hyperalgesia 7 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Disease 68 93.28 High High
Pressure And Volume Under Development 51 91.88 High High
Cyst 85 90.92 High High
Apoptosis 34 85.80 High High
Congenital Anomalies 26 83.28 Quite High
Polycystic Kidney Disease 173 77.92 Quite High
Targeted Disruption 40 71.92 Quite High
Fungal Infection 19 66.24 Quite High
Stress 29 60.68 Quite High
Helminth Infection 7 59.28 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
To study whether TRPP2 and TRPV4 also interact functionally, we expressed both channels in Xenopus laevis oocytes for electrophysiological analysis.
TRPP2 Binding (interact) of in oocytes
1) Confidence 0.48 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2500130 Disease Relevance 0.20 Pain Relevance 0.06
These findings demonstrate that TRPP2 and TRPV4 physically and functionally interact, thereby raising the question of whether TRPP2 nonspecifically alters the activity of TRP channels in vitro.
TRPP2 Binding (interact) of associated with trp channel
2) Confidence 0.48 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2500130 Disease Relevance 0.16 Pain Relevance 0.08
TRPP2 did not alter the whole cell currents mediated by expression of TRPC1 (unpublished data), which indicates that physical interaction with TRPP2 alone does not suffice to alter the functional properties of another TRP channel, at least under the experimental conditions used here.


TRPP2 Binding (interaction) of associated with trp channel
3) Confidence 0.37 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2500130 Disease Relevance 0.18 Pain Relevance 0.09
Functional interaction between TRPP2 and TRPV4
TRPP2 Binding (interaction) of
4) Confidence 0.37 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2500130 Disease Relevance 0.14 Pain Relevance 0.06
TRPP2 is known to interact with TRPC1 (Tsiokas et al., 1999); therefore, we tested whether TRPP2 influences the channel properties of TRPC1 in X. laevis oocytes.
TRPP2 Binding (interact) of in oocytes
5) Confidence 0.35 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2500130 Disease Relevance 0.15 Pain Relevance 0.09
These observations led us to speculate that TRPP2 may interact with TRPV4 to mediate tissue-specific functions such as ciliary mechanosensation.
TRPP2 Binding (interact) of in ciliary associated with mechanosensation
6) Confidence 0.35 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2500130 Disease Relevance 0.12 Pain Relevance 0.10
To confirm these coimmunoprecipitation assays, we used fluorescence resonance energy transfer (FRET) to test whether the carboxy-terminal domains of TRPP2 and TRPV4 associate within living cells.
TRPP2 Binding (associate) of
7) Confidence 0.35 Published 2008 Journal The Journal of Cell Biology Section Body Doc Link PMC2500130 Disease Relevance 0.05 Pain Relevance 0.08
Cystogenesis in humans and mice occurs in trans-heterozygotes with PKD1 and PKD2 mutations [26, 27].
PKD2 Binding (heterozygotes) of
8) Confidence 0.23 Published 2007 Journal Cell Mol Life Sci Section Body Doc Link PMC2775119 Disease Relevance 0.75 Pain Relevance 0
For example, polycystin-2 was found to directly interact with fibrocystin to regulate calcium responses in the kidneys [53].
polycystin-2 Binding (interact) of
9) Confidence 0.19 Published 2007 Journal Cell Mol Life Sci Section Body Doc Link PMC2775119 Disease Relevance 0.52 Pain Relevance 0
In addition siRNA targeting PKD1, but not that targeting PKD2, inhibited the killing of C. neoformans (Figure 5C), supporting an isoform-specific function.
PKD2 Binding (targeting) of
10) Confidence 0.13 Published 2010 Journal PLoS ONE Section Body Doc Link PMC3011003 Disease Relevance 0.12 Pain Relevance 0
We also performed growth inhibition experiments using various concentrations of both PC1 and PC2 (Figure S2).
PC2 Binding (concentrations) of
11) Confidence 0.04 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2858708 Disease Relevance 0.05 Pain Relevance 0

General Comments

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