INT57425

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Context Info
Confidence 0.11
First Reported 1994
Last Reported 2010
Negated 1
Speculated 0
Reported most in Body
Documents 12
Total Number 12
Disease Relevance 2.33
Pain Relevance 1.26

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

cytoplasm (MYH14)
Anatomy Link Frequency
filament 2
sarcomere 1
smooth muscle 1
muscle 1
bridge 1
MYH14 (Homo sapiens)
Pain Link Frequency Relevance Heat
sodium channel 1 88.12 High High
Pain 6 83.56 Quite High
adenocard 1 83.36 Quite High
ischemia 17 78.48 Quite High
cva 48 78.12 Quite High
Action potential 3 76.84 Quite High
Spinal cord 3 75.12 Quite High
cocaine 3 75.00 Quite High
Angina 6 72.12 Quite High
Calcium channel 5 69.32 Quite High
Disease Link Frequency Relevance Heat
Disease 96 92.08 High High
Fatigue 21 89.24 High High
Deafness 77 80.28 Quite High
Cv Unclassified Under Development 35 78.48 Quite High
Cv General 3 Under Development 52 78.12 Quite High
Left Ventricular Hypertrophy 1 77.68 Quite High
Injury 11 75.00 Quite High
Heart Rate Under Development 24 74.96 Quite High
Motor Neuron Diseases 4 73.84 Quite High
Pre-term Labor 12 73.36 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
To clarify whether the treatments altered responsiveness of the contractile elements to Ca2+, the effect of 2,3-butanedione monoxime (BDM), an agent that interferes with the interaction of actin and myosin, was tested after prior addition of histamine or increased Ca2+.
myosin Binding (interaction) of
1) Confidence 0.11 Published 1997 Journal J. Cardiovasc. Pharmacol. Section Abstract Doc Link 9300320 Disease Relevance 0.06 Pain Relevance 0.13
From then on, the tendons undergo no additional changes, so that the actin-myosin interaction may be transferred onto the extremity lever without loss of contraction energy [7].
actin-myosin Neg (no) Binding (interaction) of in lever
2) Confidence 0.11 Published 2008 Journal Biomed Eng Online Section Body Doc Link PMC2492863 Disease Relevance 0.05 Pain Relevance 0
Cross-reactivity with myosin from skeletal muscle was seen.
myosin Binding (Cross-reactivity) of in skeletal muscle
3) Confidence 0.10 Published 1994 Journal Cardiology Section Abstract Doc Link 8174143 Disease Relevance 0.83 Pain Relevance 0.41
The contractions have to be maintained over several seconds while the muscle length is decreasing from maximal to minimal in performing the movement, whereas both the pre-stretching length of the examined muscle and the number of actin-myosin bindings within the sarcomere are changing constantly.
actin-myosin Binding (bindings) of in muscle
4) Confidence 0.08 Published 2008 Journal Biomed Eng Online Section Body Doc Link PMC2492863 Disease Relevance 0.15 Pain Relevance 0
On the other hand, in single twitches, the active state (the actin-myosin interaction) is maximal only for a short period of time, which is too short to completely tense the serial elastic elements.
actin-myosin Binding (interaction) of
5) Confidence 0.08 Published 2008 Journal Biomed Eng Online Section Body Doc Link PMC2492863 Disease Relevance 0.08 Pain Relevance 0.08
The single twitches have a limited duration, which leads to a limited contraction length that allows for the number of actin-myosin bindings to remain relatively constant during the contraction.
actin-myosin Binding (bindings) of
6) Confidence 0.08 Published 2008 Journal Biomed Eng Online Section Body Doc Link PMC2492863 Disease Relevance 0.09 Pain Relevance 0.08
Metabolic power increases with contraction speed because the power developed by a contracting muscle fiber is due to myosin cross-bridge cycling within the fiber, each cycle requiring the hydrolysis of ATP.
myosin Binding (cross) of in bridge
7) Confidence 0.07 Published 2010 Journal PLoS Computational Biology Section Body Doc Link PMC2958805 Disease Relevance 0 Pain Relevance 0
Furthermore, as predicted by the known effects of CaD to inhibit Ca-dependent acto-myosin interactions in vitro, we have directly shown that human myometrial smooth muscle from pregnant women (>37 week, not in labor) exhibits an increased Ca2+i threshold for contraction (decreased Ca sensitivity) as CaD levels increase with gestation.
myosin Binding (interactions) of in smooth muscle
8) Confidence 0.05 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2759504 Disease Relevance 0.26 Pain Relevance 0
Likewise, among the enriched cellular components, are “stereocilium” (GO:0032420), “myosin complex” (GO:0016459), “cell junction” (GO:0030054), and among the molecular functions, “actin binding” (GO:0003779), “actin filament binding” (GO:0051015), and so forth.
myosin Binding (binding) of in filament
9) Confidence 0.05 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2946934 Disease Relevance 0.33 Pain Relevance 0.13
Since h-CaD is known to inhibit acto-myosin interactions in vitro [15], we tested the relative Ca sensitivity of activation of the contractile filaments of human myometrial preparations permeabilized with alpha toxin [10].
myosin Binding (interactions) of in filaments
10) Confidence 0.05 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2759504 Disease Relevance 0 Pain Relevance 0
The power generated in a muscle contraction is provided by the interaction of the actin and myosin components within the sarcomere.
myosin Binding (interaction) of in sarcomere
11) Confidence 0.04 Published 2009 Journal Osteoporos Int Section Body Doc Link PMC2832869 Disease Relevance 0 Pain Relevance 0.12
The intracellular sodium then permits release of calcium intracellularly from the sarcoplasmic reticulum, which binds with actin and myosin, leading to myocardial contraction.
myosin Binding (binds) of in reticulum
12) Confidence 0.01 Published 2010 Journal Therapeutics and Clinical Risk Management Section Body Doc Link PMC2963161 Disease Relevance 0.48 Pain Relevance 0.31

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