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Context Info
Confidence 0.67
First Reported 1985
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 8
Total Number 8
Disease Relevance 3.49
Pain Relevance 1.68

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

ATPase activity (Dnahc8) cytoskeleton (Dnahc8) cilium (Dnahc8)
molecular_function (Dnahc8) biological_process (Dnahc8) cytoplasm (Dnahc8)
Anatomy Link Frequency
macrophages 1
cardiomyocytes 1
muscle 1
lumen 1
Osteoclasts 1
Dnahc8 (Mus musculus)
Pain Link Frequency Relevance Heat
Morphine 7 99.12 Very High Very High Very High
Pain 22 98.44 Very High Very High Very High
amygdala 1 94.20 High High
Hippocampus 2 93.80 High High
Catecholamine 1 84.64 Quite High
tolerance 3 83.56 Quite High
Inflammation 43 79.44 Quite High
withdrawal 4 79.32 Quite High
narcan 5 78.56 Quite High
addiction 3 76.68 Quite High
Disease Link Frequency Relevance Heat
Pain 21 98.44 Very High Very High Very High
Apoptosis 21 97.12 Very High Very High Very High
Acidosis 2 96.40 Very High Very High Very High
Hypercalcemia 3 94.92 High High
Osteoporosis 3 94.28 High High
Bone Cancer 1 93.16 High High
Arrhythmia Under Development 22 90.04 High High
Sudden Death 3 88.80 High High
Parkinson's Disease 116 83.60 Quite High
Disease 14 79.80 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
In the control animals the nucleus caudatus putamen, globus pallidus, hippocampus, nuclei of amygdala, nuclei hypothalami, substantia grisea centralis, griseum pontis, nucleus trapezoideus, nucleus prepositus hypoglossi, nucleus parabrachialis, nucleus vestibularis, nucleus nervi hypoglossi, nucleus dorsalis nervi vagi, nucleus olivaris and nucleus centralis superior are found to be very rich in ATPase.
Localization (rich) of ATPase in nucleus associated with hippocampus and amygdala
1) Confidence 0.67 Published 1985 Journal J Hirnforsch Section Abstract Doc Link 3005393 Disease Relevance 0 Pain Relevance 0.88
Osteoclasts degrade bone minerals by secreting protons through the vacuolar H+-ATPase, creating acidic microenvironments.
Localization (secreting) of ATPase in Osteoclasts
2) Confidence 0.35 Published 2006 Journal Bone Section Abstract Doc Link 16769263 Disease Relevance 1.26 Pain Relevance 0.67
secretion from macrophages, block surface ATPase activity and permeability of the cell to PI.
Localization (secretion) of ATPase in macrophages
3) Confidence 0.08 Published 2007 Journal Purinergic Signal Section Body Doc Link PMC2096758 Disease Relevance 0.34 Pain Relevance 0.08
The current study also reports the expression of testis specific genes such as ATPase class I type 8b member 3 which has hydrolase and phospholipid-translocating ATPase activity, and ATP-dependent aminophospholipid transporter which is exclusively expressed in the acrosomal region of spermatozoa [31].
Localization (translocating) of ATPase in spermatozoa
4) Confidence 0.04 Published 2007 Journal BMC Genomics Section Body Doc Link PMC1888706 Disease Relevance 0 Pain Relevance 0
Clear cells contain the vacuolar H+-ATPase and secrete protons into the lumen and thus participate in its acidification.
Localization (secrete) of ATPase in lumen
5) Confidence 0.03 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2972736 Disease Relevance 0 Pain Relevance 0
cardiomyocytes has been proposed to result from a deficiency of a complex of ankyrin-B with the Na/K ATPase, Na/Ca exchanger, and IP3 receptor localized in a specialized microdomain in cardiomyocyte transverse-tubules [16].
Localization (localized) of ATPase in cardiomyocytes
6) Confidence 0.03 Published 2007 Journal PLoS ONE Section Body Doc Link PMC2013943 Disease Relevance 1.08 Pain Relevance 0.04
Not only does this prevent ATP synthesis but it also enables the proton-translocating ATPase to reverse direction and so actively hydrolyse ATP rather than synthesise it.
Localization (translocating) of ATPase
7) Confidence 0.02 Published 2007 Journal Biochimica et Biophysica Acta Section Body Doc Link PMC2212780 Disease Relevance 0.53 Pain Relevance 0
These include ryanodine receptor, a Ca2+ release channel which participates in Ca2+ release from sarcoplasmic reticulum into muscle cells, Ca2+-ATPase, which drives Ca2+ uptake, and calsequestrin that binds with Ca2+.8-11 Thus, since Ca2+ uptake by the sarcoplasmic reticulum and Ca2+ release from the sarcoplasmic reticulum play key roles in the regulation of Ca2+ concentrations in muscle cells, the above proteins are important elements in studies on the mechanisms of muscle contraction and relaxation.
Localization (release) of ATPase in muscle
8) Confidence 0.01 Published 2006 Journal Yonsei Medical Journal Section Body Doc Link PMC2687630 Disease Relevance 0.29 Pain Relevance 0

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