Difference between revisions of "HQ:Code Test"

Line 53: Line 53:
 
//pre jamboree data
 
//pre jamboree data
 
//place the results of the concatenate function here:  
 
//place the results of the concatenate function here:  
−
var data =[{'team_name':'Aachen', 'wiki_link':'https://2018.igem.org/Team:Aachen','location':'Germany', 'institution':'RWTH Aachen University','section':'Overgrad', 'project_title': 'Melasense', 'track':'Diagnostics', 'abstract':'We plan on developing a melatonin biosensor. Our approach for the biosensor is to genetically modify Saccharomyces cerevisiae by integrating a highly specific human melatonin receptor into the cells. Melatonin has a high membrane permeability which permits us to use the nuclear retinoid z receptor (RZR) which is directly regulating gene expression. We express the RZR as a fusion-protein with the recognition sequence of the human estrogen receptor alpha (ERα). When melatonin is bound, the modified receptor binds to the estrogen receptor responsive element (ERE) and as a consequence regulate expression of firefly luciferase reporter genes. In our second approach, we will use the membrane-receptor MT1 for our biosensor. When melatonin binds to the G protein-coupled receptor, β-arrestins can be recruited. This mechanism allows us to use an enzyme fragment complementation assay based on two fusion-proteins.', 'parts_link':'http://parts.igem.org/cgi/partsdb/pgroup.cgi?pgroup=iGEM2018&group=Aachen','region':'Europe','poster_zone':'Zone 5','poster_number':'302','presentation_day':'Saturday','presentation_room':'304','presentation_time':'4:45 PM - 5:15 PM', 'award':'-','nomination':'-'},
+
var data =[
 +
{'team_name':'Aachen', 'wiki_link':'https://2018.igem.org/Team:Aachen','location':'Germany', 'institution':'RWTH Aachen University','section':'Overgrad', 'project_title': 'Melasense', 'track':'Diagnostics', 'abstract':'We plan on developing a melatonin biosensor. Our approach for the biosensor is to genetically modify Saccharomyces cerevisiae by integrating a highly specific human melatonin receptor into the cells. Melatonin has a high membrane permeability which permits us to use the nuclear retinoid z receptor (RZR) which is directly regulating gene expression. We express the RZR as a fusion-protein with the recognition sequence of the human estrogen receptor alpha (ERα). When melatonin is bound, the modified receptor binds to the estrogen receptor responsive element (ERE) and as a consequence regulate expression of firefly luciferase reporter genes. In our second approach, we will use the membrane-receptor MT1 for our biosensor. When melatonin binds to the G protein-coupled receptor, β-arrestins can be recruited. This mechanism allows us to use an enzyme fragment complementation assay based on two fusion-proteins.', 'parts_link':'http://parts.igem.org/cgi/partsdb/pgroup.cgi?pgroup=iGEM2018&group=Aachen','region':'Europe','poster_zone':'Zone 5','poster_number':'302','presentation_day':'Saturday','presentation_room':'304','presentation_time':'4:45 PM - 5:15 PM', 'award':'-','nomination':'-'},
 
{'team_name':'Aalto-Helsinki', 'wiki_link':'https://2018.igem.org/Team:Aalto-Helsinki','location':'Finland', 'institution':'Aalto University','section':'Overgrad', 'project_title': 'Silkolor - A sustainable approach to dyeing industry using fusion proteins', 'track':'New Application', 'abstract':'Textile dyeing is one of the biggest polluters of natural waters. Many of the synthetic dyes used are non-biodegradable, toxic and large amounts of them end up in waters during the dyeing process. Natural dyes, although less toxic than synthetic ones, require mordants in order to bind to the fabric. Mordants often contain aluminum or other metals, which are harmful to the environment. We are addressing the problem by using two types of colorful fusion proteins. Chromoproteins are fused with binding domains to create colorful proteins which can bind cellulose or keratin based materials, such as cotton or wool, respectively. Spider silk is added to some of the proteins in order to make colored silk proteins that can be made into fibers, which would erase the need for the dyeing step from the textile value chain completely. Our experiments were focused on binding tests and silk fiber production.', 'parts_link':'http://parts.igem.org/cgi/partsdb/pgroup.cgi?pgroup=iGEM2018&group=Aalto-Helsinki','region':'Europe','poster_zone':'Zone 4','poster_number':'229','presentation_day':'Friday','presentation_room':'304','presentation_time':'4:45 PM - 5:15 PM', 'award':'-','nomination':'-'},
 
{'team_name':'Aalto-Helsinki', 'wiki_link':'https://2018.igem.org/Team:Aalto-Helsinki','location':'Finland', 'institution':'Aalto University','section':'Overgrad', 'project_title': 'Silkolor - A sustainable approach to dyeing industry using fusion proteins', 'track':'New Application', 'abstract':'Textile dyeing is one of the biggest polluters of natural waters. Many of the synthetic dyes used are non-biodegradable, toxic and large amounts of them end up in waters during the dyeing process. Natural dyes, although less toxic than synthetic ones, require mordants in order to bind to the fabric. Mordants often contain aluminum or other metals, which are harmful to the environment. We are addressing the problem by using two types of colorful fusion proteins. Chromoproteins are fused with binding domains to create colorful proteins which can bind cellulose or keratin based materials, such as cotton or wool, respectively. Spider silk is added to some of the proteins in order to make colored silk proteins that can be made into fibers, which would erase the need for the dyeing step from the textile value chain completely. Our experiments were focused on binding tests and silk fiber production.', 'parts_link':'http://parts.igem.org/cgi/partsdb/pgroup.cgi?pgroup=iGEM2018&group=Aalto-Helsinki','region':'Europe','poster_zone':'Zone 4','poster_number':'229','presentation_day':'Friday','presentation_room':'304','presentation_time':'4:45 PM - 5:15 PM', 'award':'-','nomination':'-'},
 
{'team_name':'ACIBADEM ISTANBUL', 'wiki_link':'https://2018.igem.org/Team:ACIBADEM_ISTANBUL','location':'Turkey', 'institution':'ACIBADEM UNIVERSITY','section':'Undergrad', 'project_title': 'LTNF 2.0: Circularized Venom Neutralizing Factor', 'track':'Therapeutics', 'abstract':'The Opossum (Didelphimorphia) is an animal with a very unique characteristic; it displays an outstanding resistance to toxins, snake venoms in particular. This anti-venom ability is gained through a single protein; the Lethal Toxin Neutralizing Factor (LTNF). We are attempting to produce an improved version of this anti-venom, LTNF 2.0 if you will, as a synthetic anti-venom for human use. LTNF 2.0 incorporates the post-translational modification process known as circularization, a process that comprises of adding cysteine amino acids to both ends of a polypeptide chain; triggering the formation of a disulphide bridge, ultimately leading to a circular structure, hence the name circularization. Circularized proteins are known for not only greater stability but also greater efficacy of the protein, thereby improving its shelf life and lowering the required dosage for treatment, ultimately providing a more efficient bioproduct.', 'parts_link':'http://parts.igem.org/cgi/partsdb/pgroup.cgi?pgroup=iGEM2018&group=ACIBADEM_ISTANBUL','region':'Europe','poster_zone':'Zone 5','poster_number':'305','presentation_day':'Saturday','presentation_room':'310','presentation_time':'11:30 AM - 12:00 PM', 'award':'-','nomination':'-'},
 
{'team_name':'ACIBADEM ISTANBUL', 'wiki_link':'https://2018.igem.org/Team:ACIBADEM_ISTANBUL','location':'Turkey', 'institution':'ACIBADEM UNIVERSITY','section':'Undergrad', 'project_title': 'LTNF 2.0: Circularized Venom Neutralizing Factor', 'track':'Therapeutics', 'abstract':'The Opossum (Didelphimorphia) is an animal with a very unique characteristic; it displays an outstanding resistance to toxins, snake venoms in particular. This anti-venom ability is gained through a single protein; the Lethal Toxin Neutralizing Factor (LTNF). We are attempting to produce an improved version of this anti-venom, LTNF 2.0 if you will, as a synthetic anti-venom for human use. LTNF 2.0 incorporates the post-translational modification process known as circularization, a process that comprises of adding cysteine amino acids to both ends of a polypeptide chain; triggering the formation of a disulphide bridge, ultimately leading to a circular structure, hence the name circularization. Circularized proteins are known for not only greater stability but also greater efficacy of the protein, thereby improving its shelf life and lowering the required dosage for treatment, ultimately providing a more efficient bioproduct.', 'parts_link':'http://parts.igem.org/cgi/partsdb/pgroup.cgi?pgroup=iGEM2018&group=ACIBADEM_ISTANBUL','region':'Europe','poster_zone':'Zone 5','poster_number':'305','presentation_day':'Saturday','presentation_room':'310','presentation_time':'11:30 AM - 12:00 PM', 'award':'-','nomination':'-'},
Line 372: Line 373:
 
{'team_name':'Yale', 'wiki_link':'https://2018.igem.org/Team:Yale','location':'United States', 'institution':'Yale University','section':'Undergrad', 'project_title': 'Engineering a synthetic bacterial co-culture to degrade and metabolize PET plastics', 'track':'Environment', 'abstract':'Polyethylene terephthalate (PET) is a polymer used to make plastic products ranging from synthetic fibers to water bottles. Large amounts of PET end up accumulating in the environment as pollution. A bacterium named Ideonella sakaiensis was found to degrade PET by using two enzymes, PETase and MHETase, to break PET into two monomers: ethylene glycol (EG) and terephthalic acid (TPA). However, I. sakaiensis inability to breakdown PET on a practical time scale undermines its usefulness in eliminating PET pollution. Our project aimed to tackle PET pollution by engineering a synthetic Escherichia coli and Aceintobacter baylyi co-culture to degrade and metabolize PET. Since both E. coli and A. baylyi are more characterized than I. sakaiensis and also capable of high-throughput mutagenesis, PET degradation and metabolism pathways in an engineered synthetic E. coli and A. baylyi co-culture potentially could be optimized to be more efficient than those natively found in I. sakaiensis.', 'parts_link':'http://parts.igem.org/cgi/partsdb/pgroup.cgi?pgroup=iGEM2018&group=Yale','region':'North America','poster_zone':'Zone 1','poster_number':'81','presentation_day':'Friday','presentation_room':'207','presentation_time':'4:15 PM - 4:45 PM', 'award':'-','nomination':'-'},
 
{'team_name':'Yale', 'wiki_link':'https://2018.igem.org/Team:Yale','location':'United States', 'institution':'Yale University','section':'Undergrad', 'project_title': 'Engineering a synthetic bacterial co-culture to degrade and metabolize PET plastics', 'track':'Environment', 'abstract':'Polyethylene terephthalate (PET) is a polymer used to make plastic products ranging from synthetic fibers to water bottles. Large amounts of PET end up accumulating in the environment as pollution. A bacterium named Ideonella sakaiensis was found to degrade PET by using two enzymes, PETase and MHETase, to break PET into two monomers: ethylene glycol (EG) and terephthalic acid (TPA). However, I. sakaiensis inability to breakdown PET on a practical time scale undermines its usefulness in eliminating PET pollution. Our project aimed to tackle PET pollution by engineering a synthetic Escherichia coli and Aceintobacter baylyi co-culture to degrade and metabolize PET. Since both E. coli and A. baylyi are more characterized than I. sakaiensis and also capable of high-throughput mutagenesis, PET degradation and metabolism pathways in an engineered synthetic E. coli and A. baylyi co-culture potentially could be optimized to be more efficient than those natively found in I. sakaiensis.', 'parts_link':'http://parts.igem.org/cgi/partsdb/pgroup.cgi?pgroup=iGEM2018&group=Yale','region':'North America','poster_zone':'Zone 1','poster_number':'81','presentation_day':'Friday','presentation_room':'207','presentation_time':'4:15 PM - 4:45 PM', 'award':'-','nomination':'-'},
 
{'team_name':'ZJU-China', 'wiki_link':'https://2018.igem.org/Team:ZJU-China','location':'China', 'institution':'Zhejiang University','section':'Undergrad', 'project_title': 'A Detector - A Framework of Multi-enzyme Assembly', 'track':'New Application', 'abstract':'Injuries–resulting from traffic collisions, drowning, falls or burns - and violence - from acts of war–kill more than 5 million people worldwide annually and cause harm to millions more. A waste of prehospital time led to high mortality. In response to these situations, ZJU-China developed A Detector for point-of-care testing (POCT), a manufacturing platform for other biosensors. Developers can assemble customized enzymes with Tag/Catcher labels in the expected order and immobilize them on a biocompatible matrix of curli fibers. In traumatic shock detecting, a triple-enzyme complex is constructed and performs as a logic gate to integrate two clinical parameters on molecular level. The result is exported through redox reaction on electrodes. Besides, in silicon machine learning is used to build a bridge between real clinical data and currents in our design. In brief, we propose an innovative new application by introducing A Detector, a Tag-Enzyme-Catcher assembly for fast response.', 'parts_link':'http://parts.igem.org/cgi/partsdb/pgroup.cgi?pgroup=iGEM2018&group=ZJU-China','region':'Asia','poster_zone':'Zone 5','poster_number':'311','presentation_day':'Thursday','presentation_room':'310','presentation_time':'2:45 PM - 3:15 PM', 'award':'-','nomination':'-'},
 
{'team_name':'ZJU-China', 'wiki_link':'https://2018.igem.org/Team:ZJU-China','location':'China', 'institution':'Zhejiang University','section':'Undergrad', 'project_title': 'A Detector - A Framework of Multi-enzyme Assembly', 'track':'New Application', 'abstract':'Injuries–resulting from traffic collisions, drowning, falls or burns - and violence - from acts of war–kill more than 5 million people worldwide annually and cause harm to millions more. A waste of prehospital time led to high mortality. In response to these situations, ZJU-China developed A Detector for point-of-care testing (POCT), a manufacturing platform for other biosensors. Developers can assemble customized enzymes with Tag/Catcher labels in the expected order and immobilize them on a biocompatible matrix of curli fibers. In traumatic shock detecting, a triple-enzyme complex is constructed and performs as a logic gate to integrate two clinical parameters on molecular level. The result is exported through redox reaction on electrodes. Besides, in silicon machine learning is used to build a bridge between real clinical data and currents in our design. In brief, we propose an innovative new application by introducing A Detector, a Tag-Enzyme-Catcher assembly for fast response.', 'parts_link':'http://parts.igem.org/cgi/partsdb/pgroup.cgi?pgroup=iGEM2018&group=ZJU-China','region':'Asia','poster_zone':'Zone 5','poster_number':'311','presentation_day':'Thursday','presentation_room':'310','presentation_time':'2:45 PM - 3:15 PM', 'award':'-','nomination':'-'},
−
{'team_name':'ZJUT-China', 'wiki_link':'https://2018.igem.org/Team:ZJUT-China','location':'China', 'institution':'Zhejiang University of Technology','section':'Undergrad', 'project_title': 'LiGEM-DARG: Light-controlled Genetic Engineering Machine for Degrading Antibiotic Resistance Genes', 'track':'Environment', 'abstract':'Due to antibiotic resistance genes (ARGs), microbial infections are increasingly difficult to be treated with antibiotics. The spread of ARGs has become a global challenge. Eliminating ARGs of microbes (e.g. from fermentation industry or laboratories) can reduce the amount of ARGs in the environment. To this end, we developed a light-controlled genetic engineering machine for degrading ARGs, which is comprised of the following modules: 1) To cleave an ARG, Cas9 was expressed under the control of arabinose promoter and guided by the sgRNA which targets at the ARG. 2) To control the expression of Cas9 through light, the efficiency of the light-controlled part was measured with eGFP as reporter. 3) To reduce leaky transcription of sgRNA, the arabinose-controlled repressor LacI was constructed and evaluated with eGFP. 4) A module for cell lysis was constructed to disrupt cells after eliminating the ARG. Together, we provided a novel strategy for controlling ARGs.', 'parts_link':'http://parts.igem.org/cgi/partsdb/pgroup.cgi?pgroup=iGEM2018&group=ZJUT-China','region':'Asia','poster_zone':'Zone 5','poster_number':'307','presentation_day':'Friday','presentation_room':'310','presentation_time':'4:15 PM - 4:45 PM', 'award':'-','nomination':'-'},];
+
{'team_name':'ZJUT-China', 'wiki_link':'https://2018.igem.org/Team:ZJUT-China','location':'China', 'institution':'Zhejiang University of Technology','section':'Undergrad', 'project_title': 'LiGEM-DARG: Light-controlled Genetic Engineering Machine for Degrading Antibiotic Resistance Genes', 'track':'Environment', 'abstract':'Due to antibiotic resistance genes (ARGs), microbial infections are increasingly difficult to be treated with antibiotics. The spread of ARGs has become a global challenge. Eliminating ARGs of microbes (e.g. from fermentation industry or laboratories) can reduce the amount of ARGs in the environment. To this end, we developed a light-controlled genetic engineering machine for degrading ARGs, which is comprised of the following modules: 1) To cleave an ARG, Cas9 was expressed under the control of arabinose promoter and guided by the sgRNA which targets at the ARG. 2) To control the expression of Cas9 through light, the efficiency of the light-controlled part was measured with eGFP as reporter. 3) To reduce leaky transcription of sgRNA, the arabinose-controlled repressor LacI was constructed and evaluated with eGFP. 4) A module for cell lysis was constructed to disrupt cells after eliminating the ARG. Together, we provided a novel strategy for controlling ARGs.', 'parts_link':'http://parts.igem.org/cgi/partsdb/pgroup.cgi?pgroup=iGEM2018&group=ZJUT-China','region':'Asia','poster_zone':'Zone 5','poster_number':'307','presentation_day':'Friday','presentation_room':'310','presentation_time':'4:15 PM - 4:45 PM', 'award':'-','nomination':'-'}];
 
 
 
// awards
 
// awards

Revision as of 16:43, 19 September 2019

Loading...

Code setup page

This page will help you setup the awards and results page

  1. Go to : here
  2. Place the variables indicated on the code on this page
  3. Place the resulting data bases into the results and all teams info pages

Results page

All teams info

iGEM Foundation

The International Genetically Engineered Machine (iGEM) Foundation is an independent, non-profit organization dedicated to the advancement of synthetic biology, education and competition, and the development of an open community and collaboration. Visit us at igem.org


hq AT igem DOT org


27 Drydock Avenue
Suite 27E-230
Boston, MA 02210


+1.617.500.3106