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# $program.funding_codes_as_text = ['123456789'] # TODO cannot set funding codes
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# Discussion links...
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$program.save!
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end
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# Configuration
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Seek::Config.home_description='<p style="text-align:center;font-size:larger;font-weight:bolder">Welcome to the SEEK Sandbox</p>
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<p style="text-align:center;font-size:larger;font-weight:bolder">You can log in with the username: <em>guest</em> and password: <em>guest</em></p>
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<p style="text-align:center">For more information about SEEK and to see a video, please visit our <a href="http://www.seek4science.org">Website</a>.</p>'
Seek::Config.tag_threshold=0# TODO set to 0 or 1 so the tags created in this example_data seeds will be visiblw on the front page.
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puts'Finish configuration'
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puts'Please visit admin site for further configuration, e.g. site_base_host, pubmed_api_email, crossref_api_email, bioportal_api_key, email, doi, admin email'
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puts'Admin account: username admin, password adminadmin. You might want to change admin password.'
sop=Sop.new(title: 'Reconstituted Enzyme System Protocol',
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description: 'Standard operating procedure for reconstituting the gluconeogenic enzyme system from Sulfolobus solfataricus to study metabolic pathway efficiency at high temperatures.')
# ISA - Investigation, Study, Assays, Observation Units
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investigation=Investigation.new(title: 'Central Carbon Metabolism of Sulfolobus solfataricus',
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description: 'An investigation in the CCM of S. solfataricus with a focus on the unique temperature adaptations and regulation; using a combined modelling and experimental approach.')
exp_assay=Assay.new(title: 'Reconstituted system reference state',
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description: 'The four purified enzymes were incubated in assay buffer and consumption of 3PG and production of F6P were measured in time, together with GAP and DHAP concentrations.')
# exp_assay.observation_units = [observation_unit] # TODO ActiveRecord::HasManyThroughNestedAssociationsAreReadonly: Cannot modify association 'Assay#observation_units' because it goes through more than one other association. (ActiveRecord::HasManyThroughNestedAssociationsAreReadonly)
program=Programme.where(title: 'Default Programme').first_or_create(web_page: 'http://www.seek4science.org',funding_details: 'Funding H2020X01Y001',description: 'This is a test programme for the SEEK sandbox.')
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project=Project.where(title: 'Default Project').first_or_create(:programme_id=>program.id,description: 'A description for the default project')# TODO this link is not working
title: 'Intermediate instability at high temperature leads to low pathway efficiency for an in vitro reconstituted system of gluconeogenesis in Sulfolobus solfataricus',
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abstract: "Four enzymes of the gluconeogenic pathway in Sulfolobus solfataricus were purified and kinetically characterized. The enzymes were reconstituted in vitro to quantify the contribution of temperature instability of the pathway intermediates to carbon loss from the system.
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The reconstituted system, consisting of phosphoglycerate kinase, glyceraldehyde 3-phosphate dehydrogenase, triose phosphate isomerase and the fructose 1,6-bisphosphate aldolase/phosphatase, maintained a constant consumption rate of 3-phosphoglycerate and production of
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fructose 6-phosphate over a 1-h period. Cofactors ATP and NADPH were regenerated via pyruvate kinase and glucose dehydrogenase. A mathematical model was constructed on the basis of the kinetics of the purified enzymes and the measured half-life times of the pathway intermediates.
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The model quantitatively predicted the system fluxes and metabolite concentrations. Relative enzyme concentrations were chosen such that half the carbon in the system was lost due to degradation of the thermolabile intermediates dihydroxyacetone phosphate, glyceraldehyde 3-phosphate
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and 1,3-bisphosphoglycerate, indicating that intermediate instability at high temperature can significantly affect pathway efficiency.",
publication.citation="Kouril, T. et al. Intermediate instability at high temperature leads to low pathway efficiency for an in vitro reconstituted system of gluconeogenesis in Sulfolobus solfataricus. FEBS J. 2015;687:100-108."
title: 'Intermediate instability at high temperature leads to low pathway efficiency for an in vitro reconstituted system of gluconeogenesis in Sulfolobus solfataricus',
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description: "Four enzymes of the gluconeogenic pathway in Sulfolobus solfataricus were purified and kinetically characterized. The enzymes were reconstituted in vitro to quantify the contribution of temperature instability of the pathway intermediates to carbon loss from the system.
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The reconstituted system, consisting of phosphoglycerate kinase, glyceraldehyde 3-phosphate dehydrogenase, triose phosphate isomerase and the fructose 1,6-bisphosphate aldolase/phosphatase, maintained a constant consumption rate of 3-phosphoglycerate and production of
FileUtils.cpFile.dirname(__FILE__) + '/' + presentation.content_blob.original_filename,presentation.content_blob.filepath# TODO results in "This version is not available"
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presentation.version=1
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presentation.save!
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puts'Seeded 1 presentation.'
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# Create an event
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event=Event.new(title: 'Event for publication',description: 'Event for publication',start_date: Date.today,end_date: Date.today + 1.day)
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