Team:KAIST-Korea/Project/References

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==Data sources==
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During our project, we required many data. We used the data of protein-protein interactions for signal transduction pathway deciding, protein sequence and domain description for modified FGFR design, gene sequence for modified FGFR sequence synthesis, structures or sequences of antibodies and FGF binding domain of FGFR for structural alignment. These data are from Uniprot, PID, NCBI and RCSB PDB.
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===Uniprot===
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Uniprot provides sequences of many proteins and domain description of well-researched proteins. Key advantage to use Uniprot is domain description. Without knowledge of function of each parts of protein, to design engineered protein for detecting ''Mycobacterium. Tubeculosis'' antigen MPT51 is impossible. Uniprot provided the information of location of FGF binding domain of FGFR which is replaced by our single-chain antibody 16A1. Uniprot also provided sequences of some antibodies to make single chain antibody sequences.
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===PID===
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PID(Pathway Interaction Database) provides the interaction networks between protein and protein or protein and DNA through certain signal transduction pathway. This Protein-protein interaction(PPI) and protein-DNA interaction(PDI) data helped us to port Human signal transduction pathway which is activated by FGF to fission yeast. Without knowledge of PPI and PDI through FGF signal pathway, we must undergo many trial and error of adding and removing of proteins and promoters to form working signal transduction pathway. With the data from PID, we decided to port the FGF->FGFR1->STAT1->GAS pathway from human to fission yeast.
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===NCBI===
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NCBI provides many data for biologists. We used protein sequence and DNA sequence from NCBI nucleotide database and protein database. DNA sequence is very important to us because gene sequence of original protein is required to synthesize novel engineered protein. Even we don't synthesize gene, we should know the sequence of gene because biobrick require not only nucleotide material, but also its sequence information. NCBI also provided sequences of some antibodis to make single chain antibody sequence, and many Journals through PubMed service.
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===RCSB PDB===
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RCSB PDB(Protein Data Bank) provides the data of structure of protein or other biomolecules. Key feature of data from PDB is the structure. NCBI or Uniprot provide the sequence of proteins, but it don't shows us the 3D-structure of them. With the structural similarity between FGF binding domain of FGFR and single chain antibody 16A1, we can sure that the replacement of FGF binding domain with 16A1 to detect MPT51 is appropriate.
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== References ==
== References ==
:Fig 1. Estimated TB incidence rates, 2008 WHO Library Cataloguing-in-Publication Data,  
:Fig 1. Estimated TB incidence rates, 2008 WHO Library Cataloguing-in-Publication Data,  

Revision as of 13:06, 9 August 2010

 

Data sources

During our project, we required many data. We used the data of protein-protein interactions for signal transduction pathway deciding, protein sequence and domain description for modified FGFR design, gene sequence for modified FGFR sequence synthesis, structures or sequences of antibodies and FGF binding domain of FGFR for structural alignment. These data are from Uniprot, PID, NCBI and RCSB PDB.

Uniprot

Uniprot provides sequences of many proteins and domain description of well-researched proteins. Key advantage to use Uniprot is domain description. Without knowledge of function of each parts of protein, to design engineered protein for detecting Mycobacterium. Tubeculosis antigen MPT51 is impossible. Uniprot provided the information of location of FGF binding domain of FGFR which is replaced by our single-chain antibody 16A1. Uniprot also provided sequences of some antibodies to make single chain antibody sequences.

PID

PID(Pathway Interaction Database) provides the interaction networks between protein and protein or protein and DNA through certain signal transduction pathway. This Protein-protein interaction(PPI) and protein-DNA interaction(PDI) data helped us to port Human signal transduction pathway which is activated by FGF to fission yeast. Without knowledge of PPI and PDI through FGF signal pathway, we must undergo many trial and error of adding and removing of proteins and promoters to form working signal transduction pathway. With the data from PID, we decided to port the FGF->FGFR1->STAT1->GAS pathway from human to fission yeast.

NCBI

NCBI provides many data for biologists. We used protein sequence and DNA sequence from NCBI nucleotide database and protein database. DNA sequence is very important to us because gene sequence of original protein is required to synthesize novel engineered protein. Even we don't synthesize gene, we should know the sequence of gene because biobrick require not only nucleotide material, but also its sequence information. NCBI also provided sequences of some antibodis to make single chain antibody sequence, and many Journals through PubMed service.

RCSB PDB

RCSB PDB(Protein Data Bank) provides the data of structure of protein or other biomolecules. Key feature of data from PDB is the structure. NCBI or Uniprot provide the sequence of proteins, but it don't shows us the 3D-structure of them. With the structural similarity between FGF binding domain of FGFR and single chain antibody 16A1, we can sure that the replacement of FGF binding domain with 16A1 to detect MPT51 is appropriate.


References

Fig 1. Estimated TB incidence rates, 2008 WHO Library Cataloguing-in-Publication Data,
Global tuberculosis control: a short update to the 2009 report
Fig 2. People suffering from malaria and TB
Mother nature network, article “New form of malaria threatens Thai-Cambodia border”
Fig 3. Researching disease
Fondation Merieux Research Programs
http://www.fondation-merieux.org/-research-programmes.html
Fig 4. Antibody
Cytomx http://cytomx.com/technologies.html
Fig 5. MPT51
RCSB Protein Database, "The crystal structure of Mycobacterium tuberculosis MPT51"
Fig 6. E.coli Statistics
http://redpoll.pharmacy.ualberta.ca/CCDB/cgi-bin/STAT_NEW.cgi
Fig 7. Yeast homologous recombinant
Bioneer http://pombe.bioneer.co.kr/technic_infomation/construction.jsp
Fig 8. CRYSTAL STRUCTURE OF A TERNARY FGF2-FGFR1-HEPARIN COMPLEX
RCSB Protein Database, "CRYSTAL STRUCTURE OF A TERNARY FGF2-FGFR1-HEPARIN COMPLEX"
Fig 9. FGF signaling pathway
Nature Pathway Interation Database, "FGF signaling pathway"
http://pid.nci.nih.gov/search/pathway_landing.shtml?pathway_id=fgf_pathway&source=NCI-Nature%20curated&what=graphic&jpg=on&ppage=1
Fig 10. Unneccesary Syndecan-2 Function
http://www.kaomp.org/new/board_view.htm?table_name=photo_0&currPage=6&aq_id=92&aq_type=&aq_value
Fig 11. Structural bases of unphosphorylated STAT1 association and receptor binding
RCSB Protein Database, "Structural bases of unphosphorylated STAT1 association and receptor binding"
Fig 12. Roberto, Proteína fluorescente verde – história e perspectivas, Química de Produtos Naturais (2009)
Fig 13. KAIST success!
http://imperfectaction.com/blog/2009/03/04/entrepreneurship/definition-of-success/


[1] International Union of Pure and Applied Chemistry. "biosensor". Compendium of Chemical Terminology :: Internet edition.
[2] Garrett, R.H., and Grisham, C.M. Biochemistry, 2nd Edition (2002), pg. 32
[3] RCSB PDB(protein database), http://www.rcsb.org/
[4] Walker K, Skelton H, Smith K. (2002). accessdate=2009-11-28 "Cutaneous lesions showing giant yeast forms of Blastomyces dermatitidis". Journal of Cutaneous Pathology 29 (10): 616–18. doi:10.1034/j.1600-0560.2002.291009.x
[5] LUCI´A CITORES,1* LING BAI,2 VIGDIS SØRENSEN,2 AND SJUR OLSNES2, Fibroblast Growth Factor Receptor-Induced Phosphorylation of STAT1 at the Golgi Apparatus Without Translocation to the Nucleus, Cellular Physiology (2007)
[6] Ronit A loni-Grinstein, Andrew Seddon, 1 and A vner Yayon*, Reconstitution of Fibroblast Growth Factor Receptor Interactions in the Yeast Two Hybrid System, MOLECULRR BIOTECHNOLOGY (1999)
[7] Fariba Barahmand-Pour, Andreas Meinke, Bernd Groner‡, and Thomas Decker§, Jak2-Stat5 Interactions Analyzed in Yeast*, The American Society for Biochemistry and Molecular Biology (1998)
[8] Hong Xu‡§¶, Kyung W. Lee‡§¶, and Mitchell Goldfarb‡i, Novel Recognition Motif on Fibroblast Growth Factor Receptor Mediates Direct Association and Activation of SNT Adapter Proteins*, The American Society for Biochemistry and Molecular Biology (1998)