De novo design of a biologically active amyloid. Gallardo, R., Ramakers, M., De Smet, F., Claes, F., Khodaparast, L., Khodaparast, L., Couceiro, J., R., Langenberg, T., Siemons, M., Nyström, S., Young, L., J., Laine, R., F., Young, L., Radaelli, E., Benilova, I., Kumar, M., Staes, A., Desager, M., Beerens, M., Vandervoort, P., Luttun, A., Gevaert, K., Bormans, G., Dewerchin, M., Van Eldere, J., Carmeliet, P., Vande Velde, G., Verfaillie, C., Kaminski, C., F., De Strooper, B., Hammarström, P., Nilsson, K., P., R., Serpell, L., Schymkowitz, J., & Rousseau, F. Science, 354(6313):aah4949, 11, 2016. Paper Website abstract bibtex INTRODUCTION: It has been shown that most proteins possess amyloidogenic segments. How-ever, only about 30 human proteins are known to be involved in amyloid-associated pathologies, and it is still not clear what determines amyloid toxicity in these diseases. We investigated wheth-er an endogenously expressed protein that contains sequences with known amyloidogenic segments, but is not known to aggregate either under normal or pathological conditions, can be induced to do so by seeding it with a peptide comprising the protein's own amyloidogenic fragment. We chose to target the protein vascular endothelial growth factor receptor 2 (VEGFR2) because it has well-characterized biological func-tion and so could provide a model system with which to investigate the relationship between protein loss of function and amyloid toxicity in different cellular contexts.
@article{
title = {De novo design of a biologically active amyloid},
type = {article},
year = {2016},
identifiers = {[object Object]},
pages = {aah4949},
volume = {354},
websites = {http://www.sciencemag.org/cgi/doi/10.1126/science.aah4949,http://www.sciencemag.org/lookup/doi/10.1126/science.aah4949},
month = {11},
day = {11},
id = {fd6092a4-d2e3-3afc-9153-ea41e8d6949d},
created = {2016-11-16T17:27:52.000Z},
file_attached = {true},
profile_id = {9b1c14de-b75a-3e23-a406-ef006d6fed26},
last_modified = {2017-06-22T09:03:31.078Z},
read = {false},
starred = {false},
authored = {true},
confirmed = {false},
hidden = {false},
abstract = {INTRODUCTION: It has been shown that most proteins possess amyloidogenic segments. How-ever, only about 30 human proteins are known to be involved in amyloid-associated pathologies, and it is still not clear what determines amyloid toxicity in these diseases. We investigated wheth-er an endogenously expressed protein that contains sequences with known amyloidogenic segments, but is not known to aggregate either under normal or pathological conditions, can be induced to do so by seeding it with a peptide comprising the protein's own amyloidogenic fragment. We chose to target the protein vascular endothelial growth factor receptor 2 (VEGFR2) because it has well-characterized biological func-tion and so could provide a model system with which to investigate the relationship between protein loss of function and amyloid toxicity in different cellular contexts.},
bibtype = {article},
author = {Gallardo, Rodrigo and Ramakers, Meine and De Smet, Frederik and Claes, Filip and Khodaparast, Ladan and Khodaparast, Laleh and Couceiro, José R. and Langenberg, Tobias and Siemons, Maxime and Nyström, Sofie and Young, Laurence J. and Laine, Romain F. and Young, Lydia and Radaelli, Enrico and Benilova, Iryna and Kumar, Manoj and Staes, An and Desager, Matyas and Beerens, Manu and Vandervoort, Petra and Luttun, Aernout and Gevaert, Kris and Bormans, Guy and Dewerchin, Mieke and Van Eldere, Johan and Carmeliet, Peter and Vande Velde, Greetje and Verfaillie, Catherine and Kaminski, Clemens F. and De Strooper, Bart and Hammarström, Per and Nilsson, K. Peter R. and Serpell, Louise and Schymkowitz, Joost and Rousseau, Frederic},
journal = {Science},
number = {6313}
}
Downloads: 0
{"_id":"mJut7RTw7jAq9zm3a","bibbaseid":"gallardo-ramakers-desmet-claes-khodaparast-khodaparast-couceiro-langenberg-etal-denovodesignofabiologicallyactiveamyloid-2016","downloads":0,"creationDate":"2017-02-17T14:41:49.312Z","title":"De novo design of a biologically active amyloid","author_short":["Gallardo, R.","Ramakers, M.","De Smet, F.","Claes, F.","Khodaparast, L.","Khodaparast, L.","Couceiro, J., R.","Langenberg, T.","Siemons, M.","Nyström, S.","Young, L., J.","Laine, R., F.","Young, L.","Radaelli, E.","Benilova, I.","Kumar, M.","Staes, A.","Desager, M.","Beerens, M.","Vandervoort, P.","Luttun, A.","Gevaert, K.","Bormans, G.","Dewerchin, M.","Van Eldere, J.","Carmeliet, P.","Vande Velde, G.","Verfaillie, C.","Kaminski, C., F.","De Strooper, B.","Hammarström, P.","Nilsson, K., P., R.","Serpell, L.","Schymkowitz, J.","Rousseau, F."],"year":2016,"bibtype":"article","biburl":null,"bibdata":{"title":"De novo design of a biologically active amyloid","type":"article","year":"2016","identifiers":"[object Object]","pages":"aah4949","volume":"354","websites":"http://www.sciencemag.org/cgi/doi/10.1126/science.aah4949,http://www.sciencemag.org/lookup/doi/10.1126/science.aah4949","month":"11","day":"11","id":"fd6092a4-d2e3-3afc-9153-ea41e8d6949d","created":"2016-11-16T17:27:52.000Z","file_attached":"true","profile_id":"9b1c14de-b75a-3e23-a406-ef006d6fed26","last_modified":"2017-06-22T09:03:31.078Z","read":false,"starred":false,"authored":"true","confirmed":false,"hidden":false,"abstract":"INTRODUCTION: It has been shown that most proteins possess amyloidogenic segments. How-ever, only about 30 human proteins are known to be involved in amyloid-associated pathologies, and it is still not clear what determines amyloid toxicity in these diseases. We investigated wheth-er an endogenously expressed protein that contains sequences with known amyloidogenic segments, but is not known to aggregate either under normal or pathological conditions, can be induced to do so by seeding it with a peptide comprising the protein's own amyloidogenic fragment. We chose to target the protein vascular endothelial growth factor receptor 2 (VEGFR2) because it has well-characterized biological func-tion and so could provide a model system with which to investigate the relationship between protein loss of function and amyloid toxicity in different cellular contexts.","bibtype":"article","author":"Gallardo, Rodrigo and Ramakers, Meine and De Smet, Frederik and Claes, Filip and Khodaparast, Ladan and Khodaparast, Laleh and Couceiro, José R. and Langenberg, Tobias and Siemons, Maxime and Nyström, Sofie and Young, Laurence J. and Laine, Romain F. and Young, Lydia and Radaelli, Enrico and Benilova, Iryna and Kumar, Manoj and Staes, An and Desager, Matyas and Beerens, Manu and Vandervoort, Petra and Luttun, Aernout and Gevaert, Kris and Bormans, Guy and Dewerchin, Mieke and Van Eldere, Johan and Carmeliet, Peter and Vande Velde, Greetje and Verfaillie, Catherine and Kaminski, Clemens F. and De Strooper, Bart and Hammarström, Per and Nilsson, K. Peter R. and Serpell, Louise and Schymkowitz, Joost and Rousseau, Frederic","journal":"Science","number":"6313","bibtex":"@article{\n title = {De novo design of a biologically active amyloid},\n type = {article},\n year = {2016},\n identifiers = {[object Object]},\n pages = {aah4949},\n volume = {354},\n websites = {http://www.sciencemag.org/cgi/doi/10.1126/science.aah4949,http://www.sciencemag.org/lookup/doi/10.1126/science.aah4949},\n month = {11},\n day = {11},\n id = {fd6092a4-d2e3-3afc-9153-ea41e8d6949d},\n created = {2016-11-16T17:27:52.000Z},\n file_attached = {true},\n profile_id = {9b1c14de-b75a-3e23-a406-ef006d6fed26},\n last_modified = {2017-06-22T09:03:31.078Z},\n read = {false},\n starred = {false},\n authored = {true},\n confirmed = {false},\n hidden = {false},\n abstract = {INTRODUCTION: It has been shown that most proteins possess amyloidogenic segments. How-ever, only about 30 human proteins are known to be involved in amyloid-associated pathologies, and it is still not clear what determines amyloid toxicity in these diseases. We investigated wheth-er an endogenously expressed protein that contains sequences with known amyloidogenic segments, but is not known to aggregate either under normal or pathological conditions, can be induced to do so by seeding it with a peptide comprising the protein's own amyloidogenic fragment. We chose to target the protein vascular endothelial growth factor receptor 2 (VEGFR2) because it has well-characterized biological func-tion and so could provide a model system with which to investigate the relationship between protein loss of function and amyloid toxicity in different cellular contexts.},\n bibtype = {article},\n author = {Gallardo, Rodrigo and Ramakers, Meine and De Smet, Frederik and Claes, Filip and Khodaparast, Ladan and Khodaparast, Laleh and Couceiro, José R. and Langenberg, Tobias and Siemons, Maxime and Nyström, Sofie and Young, Laurence J. and Laine, Romain F. and Young, Lydia and Radaelli, Enrico and Benilova, Iryna and Kumar, Manoj and Staes, An and Desager, Matyas and Beerens, Manu and Vandervoort, Petra and Luttun, Aernout and Gevaert, Kris and Bormans, Guy and Dewerchin, Mieke and Van Eldere, Johan and Carmeliet, Peter and Vande Velde, Greetje and Verfaillie, Catherine and Kaminski, Clemens F. and De Strooper, Bart and Hammarström, Per and Nilsson, K. Peter R. and Serpell, Louise and Schymkowitz, Joost and Rousseau, Frederic},\n journal = {Science},\n number = {6313}\n}","author_short":["Gallardo, R.","Ramakers, M.","De Smet, F.","Claes, F.","Khodaparast, L.","Khodaparast, L.","Couceiro, J., R.","Langenberg, T.","Siemons, M.","Nyström, S.","Young, L., J.","Laine, R., F.","Young, L.","Radaelli, E.","Benilova, I.","Kumar, M.","Staes, A.","Desager, M.","Beerens, M.","Vandervoort, P.","Luttun, A.","Gevaert, K.","Bormans, G.","Dewerchin, M.","Van Eldere, J.","Carmeliet, P.","Vande Velde, G.","Verfaillie, C.","Kaminski, C., F.","De Strooper, B.","Hammarström, P.","Nilsson, K., P., R.","Serpell, L.","Schymkowitz, J.","Rousseau, F."],"urls":{"Paper":"http://bibbase.org/service/mendeley/9b1c14de-b75a-3e23-a406-ef006d6fed26/file/5093e186-f453-c7d3-1368-5c4e106943d3/2016-De_novo_design_of_a_biologically_active_amyloid.pdf.pdf","Website":"http://www.sciencemag.org/cgi/doi/10.1126/science.aah4949,http://www.sciencemag.org/lookup/doi/10.1126/science.aah4949"},"bibbaseid":"gallardo-ramakers-desmet-claes-khodaparast-khodaparast-couceiro-langenberg-etal-denovodesignofabiologicallyactiveamyloid-2016","role":"author","downloads":0},"search_terms":["novo","design","biologically","active","amyloid","gallardo","ramakers","de smet","claes","khodaparast","khodaparast","couceiro","langenberg","siemons","nyström","young","laine","young","radaelli","benilova","kumar","staes","desager","beerens","vandervoort","luttun","gevaert","bormans","dewerchin","van eldere","carmeliet","vande velde","verfaillie","kaminski","de strooper","hammarström","nilsson","serpell","schymkowitz","rousseau"],"keywords":[],"authorIDs":[]}