INT308839

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Context Info
Confidence 0.58
First Reported 2010
Last Reported 2010
Negated 0
Speculated 1
Reported most in Body
Documents 2
Total Number 23
Disease Relevance 7.38
Pain Relevance 0.11

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

Anatomy Link Frequency
heads 1
RBC 1
eggs 1
CHO 1
KRT31 (Homo sapiens)
Pain Link Frequency Relevance Heat
adenocard 14 89.04 High High
agonist 34 55.40 Quite High
anesthesia 22 5.00 Very Low Very Low Very Low
antagonist 14 5.00 Very Low Very Low Very Low
cINOD 2 5.00 Very Low Very Low Very Low
Central nervous system 1 5.00 Very Low Very Low Very Low
tolerance 1 5.00 Very Low Very Low Very Low
Potency 1 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Influenza Virus Infection 726 99.78 Very High Very High Very High
Sprains And Strains 264 98.48 Very High Very High Very High
Weight Loss 198 97.16 Very High Very High Very High
Infection 374 96.88 Very High Very High Very High
Fever 66 96.52 Very High Very High Very High
Egg Hypersensitivity 22 95.88 Very High Very High Very High
Immunization 110 80.00 Quite High
Influenza In Birds 22 49.44 Quite Low
Body Weight 22 5.60 Low Low
Disease 67 5.00 Very Low Very Low Very Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
CHO cells stably expressing the recombinant hA1 and hA3Rs, and HEK-293 cells stably expressing the hA2AAR were cultured in Dulbecco’s modified Eagle medium (DMEM) and F12 (1:1) supplemented with 10% fetal bovine serum, 100 units/mL penicillin, 100 ?
Gene_expression (expressing) of hA1 in CHO
1) Confidence 0.58 Published 2010 Journal Journal of Medicinal Chemistry Section Body Doc Link PMC2865168 Disease Relevance 0 Pain Relevance 0.08
Several HA1 fragments were expressed and purified from E. coli inclusion bodies, and were shown to be properly folded and presented conformational epitopes [12].
Gene_expression (expressed) of HA1
2) Confidence 0.23 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2902520 Disease Relevance 0.47 Pain Relevance 0
Based on these studies, we hypothesized that bacterially-expressed HA1 fragments if properly folded, could be useful as vaccines against emerging influenza strains.
Gene_expression (expressed) of HA1 associated with influenza virus infection and sprains and strains
3) Confidence 0.23 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2902520 Disease Relevance 0.49 Pain Relevance 0
Importantly, the bacterially expressed HA1 proteins were also shown to absorb most of the neutralizing activity in post infection and post vaccination sera [12], [13].
Gene_expression (expressed) of HA1 associated with infection
4) Confidence 0.23 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2902520 Disease Relevance 0.48 Pain Relevance 0
The bacterially expressed HA1 proteins were also shown to absorb most of the neutralizing activity in post-H5N1 infection and post-H5N1 vaccination sera [12], [13].
Gene_expression (expressed) of HA1 associated with infection
5) Confidence 0.23 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2902520 Disease Relevance 0.44 Pain Relevance 0
In the face of an impending influenza pandemic, HA1 proteins derived from the newly spreading virus can be rapidly expressed in bacterial systems several months before the traditional approach using vaccine strains generated via either gene reassortment or reverse genetics, followed by adaptation to growth in eggs.
Gene_expression (expressed) of HA1 in eggs associated with influenza virus infection and sprains and strains
6) Confidence 0.23 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2902520 Disease Relevance 0.57 Pain Relevance 0
E. coli Rosetta Gami cells (Novagen) were used for expression of H1N1-HA1 (1–330) and HA (1–480).
Gene_expression (expression) of HA1
7) Confidence 0.20 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2902520 Disease Relevance 0.29 Pain Relevance 0
Both bacterially expressed HA1 (1–330) and HA (1–480) proteins and the mammalian cell derived HA0 adsorbed most of the neutralizing activity of H1N1 hyperimmune sheep sera (NIBSC), reducing the MN titer from 1?
Gene_expression (expressed) of HA1
8) Confidence 0.20 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2902520 Disease Relevance 0.17 Pain Relevance 0
Again, the kinetics of immune responses and the peak neutralization titers were significantly higher for the sheep immunized with the bacterially-expressed HA1 (1–330) protein compared with the mammalian HA0 expressed and purified from 293 cells.


Gene_expression (expressed) of HA1
9) Confidence 0.20 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2902520 Disease Relevance 0.13 Pain Relevance 0
We have recently confirmed that bacterially expressed HA1 globular heads from multiple influenza strains (avian H5N1 and seasonal strains), can be produced at high yield.
Gene_expression (expressed) of HA1 in heads associated with influenza virus infection and sprains and strains
10) Confidence 0.20 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2902520 Disease Relevance 0.43 Pain Relevance 0
In the current study, we found that expression and purification of properly folded H1N1 HA1 (1–330) (lacking HA2) in bacterial system was more efficient and gave higher yield compared with the larger HA ectodomain (1–480).
Gene_expression (expression) of HA1
11) Confidence 0.18 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2902520 Disease Relevance 0.43 Pain Relevance 0
In a subsequent study, we found that following vaccination with inactivated H5N1 (A/Vietnam/1203/2004) influenza vaccine the immune sera from the MF59-adjuvanted vaccinated individuals bound with much higher avidity to bacterially expressed properly folded H5 HA1 proteins compared with unadjuvanted vaccine sera [13].
Gene_expression (expressed) of HA1 associated with influenza virus infection
12) Confidence 0.18 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2902520 Disease Relevance 0.47 Pain Relevance 0
Bacterially expressed H1N1 HA1 (1–330) protein (containing trimers and oligomers) also agglutinated human RBC very efficiently, even at the lowest concentration of 45 ng/ml.
Gene_expression (expressed) of HA1 in RBC
13) Confidence 0.18 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2902520 Disease Relevance 0.09 Pain Relevance 0
The bacterially expressed HA1 (1–330), HA (1–480), and a mammalian cell derived recombinant full length HA (HA0) (from Immune Technology Corp, NY) were tested for binding to fetuin coated on biosensor chips.
Gene_expression (expressed) of HA1
14) Confidence 0.17 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2902520 Disease Relevance 0.06 Pain Relevance 0
Expression vector and cloning of H1N1-HA1 (1–330) and HA (1–480)
Gene_expression (Expression) of HA1
15) Confidence 0.17 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2902520 Disease Relevance 0.61 Pain Relevance 0
DNA encoding HA1 (1–330) and HA (1–480) were cloned as NotI-PacI inserts in the pSK expression vector.


Gene_expression (expression) of HA1
16) Confidence 0.17 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2902520 Disease Relevance 0.37 Pain Relevance 0
In a separate study, sheep were vaccinated with mammalian derived HA0 (Immune Technology Corps) or with the bacterially–expressed HA1 (1–330) (Table 2, bottom panels).
Gene_expression (expressed) of HA1
17) Confidence 0.17 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2902520 Disease Relevance 0.14 Pain Relevance 0
Here, we describe the properties of two novel H1N1 swine-like HA proteins, HA1 (1–330) and HA (1–480), expressed in E. coli.
Gene_expression (expressed) of HA1
18) Confidence 0.15 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2902520 Disease Relevance 0.09 Pain Relevance 0.03
The main findings in the current study are: (a) bacterially expressed H1N1 HA1 (1–330) and HA (1–480) can be purified as properly folded proteins as determined by CD spectroscopy, SPR analyses with H1N1 immune sera, and adsorption of neutralizing activity from post-infection and post vaccination sera; (b) the HA1 (1–330) contained >50% trimeric and oligomeric forms and could bind to fetuin and agglutinated human RBC, while the HA (1–480) and mammalian cell expressed HA0 proteins were predominantly monomeric, did not bind fetuin, and did not agglutinate RBC; (c) the HA1 (1–330) induced higher titers of neutralizing antibodies compared with HA (1–480) or mammalian derived recombinant HA0 in rabbits and sheep; (d) in a ferret H1N1 challenge model, high-dose vaccination (30 ?
Gene_expression (expressed) of HA1 associated with infection
19) Confidence 0.15 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2902520 Disease Relevance 0.41 Pain Relevance 0
To determine if the bacterially expressed (unglycosylated) HA1 (1–330) and HA (1–480) proteins are properly folded they were analyzed by CD spectroscopy.
Spec (determine) Gene_expression (expressed) of HA1
20) Confidence 0.15 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2902520 Disease Relevance 0.13 Pain Relevance 0

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