INT287862

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Context Info
Confidence 0.42
First Reported 2007
Last Reported 2007
Negated 0
Speculated 0
Reported most in Body
Documents 1
Total Number 9
Disease Relevance 0.07
Pain Relevance 0.12

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 (Tnnt2) protein binding, bridging (Tnnt2) cytoplasm (Tnnt2)
Anatomy Link Frequency
myocytes 1
hearts 1
Tnnt2 (Rattus norvegicus)
Pain Link Frequency Relevance Heat
Thoracotomy 9 98.24 Very High Very High Very High
ketamine 9 92.64 High High
imagery 9 53.92 Quite High
addiction 27 20.44 Low Low
lidocaine 45 5.00 Very Low Very Low Very Low
agonist 9 5.00 Very Low Very Low Very Low
adenocard 9 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Targeted Disruption 27 70.28 Quite High
Coronary Heart Disease 9 5.00 Very Low Very Low Very Low
Hypertrophic Cardiomyopathy 9 5.00 Very Low Very Low Very Low
Myocardial Infarction 9 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Significant differences were found in the phosphorylation of cMyBP-C, cTnI, MLC-1 and MLC-2 in the three groups (ANOVA),while cTnT phosphorylation (approximately 80% of total cTnT) remained the same.
Phosphorylation (phosphorylation) of cTnT
1) Confidence 0.42 Published 2007 Journal Basic Res Cardiol Section Body Doc Link PMC2780643 Disease Relevance 0 Pain Relevance 0
In both cases cTnT phosphorylation, expressed as a percentage for 2D-gels or normalized for cMyBP-C protein content in each sample derived from Sypro Ruby stained 1D-gels, did not vary between groups.
Phosphorylation (phosphorylation) of cTnT
2) Confidence 0.42 Published 2007 Journal Basic Res Cardiol Section Body Doc Link PMC2780643 Disease Relevance 0 Pain Relevance 0
There was good agreement in the results of protein phosphorylation in the samples of the various groups, where comparisons could be made (cTnT and MLC-2).
Phosphorylation (phosphorylation) of cTnT
3) Confidence 0.42 Published 2007 Journal Basic Res Cardiol Section Body Doc Link PMC2780643 Disease Relevance 0 Pain Relevance 0
The 2D-gels (pH range 4–7) allow the distinction between different phosphorylated forms of cTnT,MLC-1 and MLC-2 and permit the quantification of the relative distribution of these forms of each protein.
Phosphorylation (phosphorylated) of cTnT
4) Confidence 0.42 Published 2007 Journal Basic Res Cardiol Section Body Doc Link PMC2780643 Disease Relevance 0 Pain Relevance 0
Significant differences were found in the phosphorylation of cMyBP-C, cTnI, MLC-1 and MLC-2 in the three groups (ANOVA),while cTnT phosphorylation (approximately 80% of total cTnT) remained the same.
Phosphorylation (phosphorylation) of cTnT
5) Confidence 0.42 Published 2007 Journal Basic Res Cardiol Section Body Doc Link PMC2780643 Disease Relevance 0 Pain Relevance 0
The degree of cTnT phosphorylation was very similar as can be seen from the correspondence in the relative distribution of the intensities in the U, P and 2P spotsFig. 5A Representative 4–15 % gradient gel stained with Pro-Q Diamond from samples (approximately 35 µg dry weight) of the Quiescence (Q), Contraction (C) and Isoprenaline (Iso) group.
Phosphorylation (phosphorylation) of cTnT
6) Confidence 0.41 Published 2007 Journal Basic Res Cardiol Section Body Doc Link PMC2780643 Disease Relevance 0 Pain Relevance 0
The endogenous phosphorylation levels of contractile proteins in TCA-treated tissue from the flash frozen hearts were determined from 2D-gels (cTnT, MLC-1 and MLC-2) and from ProQ Diamond stained 1D-gels (cMyBP-C, cTnT, cTnI and MLC-2).
Phosphorylation (phosphorylation) of cTnT in hearts
7) Confidence 0.41 Published 2007 Journal Basic Res Cardiol Section Body Doc Link PMC2780643 Disease Relevance 0 Pain Relevance 0
Therefore, in the present study we induced differences in the degree of phosphorylation of the myofilaments to explore the role of phosphorylation of cMyBPC in isolated rat ventricular myocytes under physiological conditions, taken into account the phosphorylation levels of the other contractile proteins such as MLC-2, cTnT and cTnI.


Phosphorylation (phosphorylation) of cTnT in myocytes
8) Confidence 0.32 Published 2007 Journal Basic Res Cardiol Section Body Doc Link PMC2780643 Disease Relevance 0.07 Pain Relevance 0.10
Freeze dried samples were homogenized in 1D sample buffer (62.5 mM TRIS (pH 6.8), 15% glycerol, 1% SDS and 1.5% hydroxyethyldisulfide), and diluted [1:17] in 2D sample buffer (7 M urea, 2.5 M thiourea, 4% CHAPS, 0.5% ampholytes pH 4–7, 10% glycerol and 10 % isopropanol). 2D-gel electrophoresis of the samples (200 µg dry weight) was performed using immobiline strips with a pH gradient of 4–7 as described previously [42] to determine MLC-1, MLC-2 and cTnT phosphorylation from the Coomassie stained gels.


Phosphorylation (phosphorylation) of cTnT
9) Confidence 0.32 Published 2007 Journal Basic Res Cardiol Section Body Doc Link PMC2780643 Disease Relevance 0 Pain Relevance 0.03

General Comments

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