Zobrazeno 1 - 10
of 27
pro vyhledávání: '"Bernardo-Gancedo A"'
Autor:
Cater, Jordan H., Kumita, Janet R., Abdallah, Rafaa Zeineddine, Zhao, Guomao, Bernardo-Gancedo, Ana, Henry, Amanda, Winata, Wendy, Chi, Mengna, Grenyer, Brin S. F., Townsend, Michelle L., Ranson, Marie, Buhimschi, Catalin S., Charnock-Jones, Stephen, Dobson, Christopher M., Wilson, Mark R., Buhimschi, Irina A., Wyatt, Amy R.
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America, 2019 Mar . 116(13), 6101-6110.
Externí odkaz:
https://www.jstor.org/stable/26696670
Autor:
Liza Bergkvist, Daniel R Richards, Ana Bernardo-Gancedo, Janet R Kumita, Peter R Nilsson, Ann-Christin Brorsson
Publikováno v:
PLoS ONE, Vol 15, Iss 1, p e0227227 (2020)
Many conflicting reports about the involvement of serum amyloid P component (SAP) in amyloid diseases have been presented over the years; SAP is known to be a universal component of amyloid aggregates but it has been suggested that it can both induce
Externí odkaz:
https://doaj.org/article/7359655e77e2474595d357244b1390e7
Autor:
Wendy Winata, Ana Bernardo-Gancedo, Amanda Henry, Catalin S. Buhimschi, D. Stephen Charnock-Jones, Guomao Zhao, Jordan H. Cater, Rafaa Zeineddine Abdallah, Marie Ranson, Mark R. Wilson, Michelle L. Townsend, Janet R. Kumita, Christopher M. Dobson, Irina A. Buhimschi, Mengna Chi, Amy R. Wyatt, Brin S. F. Grenyer
Publikováno v:
Proceedings of the National Academy of Sciences of the United States of America
Significance Pregnancy is a unique physiological state involving biological stresses that promote protein damage (misfolding) within the maternal body. Currently, little is known regarding how the maternal body copes with elevated protein misfolding
Autor:
Bergkvist, Liza, Richards, Daniel R, Bernardo-Gancedo, Ana, Kumita, Janet R, Nilsson, Peter R, Brorsson, Ann-Christin
Publikováno v:
PLoS ONE, Vol 15, Iss 1, p e0227227 (2020)
Funder: Stiftelsen Apotekare Hedbergs Fond för Medicinsk Forskning; funder-id: http://dx.doi.org/10.13039/501100009791
Funder: Sthones stiftelse
Many conflicting reports about the involvement of serum amyloid P component (SAP) in amyloid d
Funder: Sthones stiftelse
Many conflicting reports about the involvement of serum amyloid P component (SAP) in amyloid d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d3091b6d14a8ca09fea7f6ed768cd8b
Autor:
Liza, Bergkvist, Daniel R, Richards, Ana, Bernardo-Gancedo, Janet R, Kumita, Peter R, Nilsson, Ann-Christin, Brorsson
Publikováno v:
PLoS ONE
Many conflicting reports about the involvement of serum amyloid P component (SAP) in amyloid diseases have been presented over the years; SAP is known to be a universal component of amyloid aggregates but it has been suggested that it can both induce
Autor:
Bernardo Gancedo, Ana
Human lysozyme (HuL) is a widely characterised protein whose mutational variants misfold, forming amyloid fibrils that are associated with a rare systemic amyloidosis. Given that a number of proteins, including lysozyme, can misfold and give rise to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2d4733f1daf6a389de03f1d57a57ec4a
Autor:
Ahn, Minkoo, Waudby, Christopher A., Bernardo-Gancedo, Ana, De Genst, Erwin, Dhulesia, Anne, Salvatella, Xavier, Christodoulou, John, Dobson, Christopher M., Kumita, Janet R.
Publikováno v:
Scientific Reports
Scientific Reports, Vol 7, Iss 1, Pp 1-12 (2017)
Scientific Reports, Vol 7, Iss 1, Pp 1-12 (2017)
Populating transient and partially unfolded species is a crucial step in the formation and accumulation of amyloid fibrils formed from pathogenic variants of human lysozyme linked with a rare but fatal hereditary systemic amyloidosis. The partially u
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::29af0f697fc8da0b0c0cb08f52679dba
Autor:
Ahn, M, Hagan, CL, Bernardo-Gancedo, A, De Genst, E, Newby, FN, Christodoulou, J, Dhulesia, A, Dumoulin, M, Robinson, CV, Dobson, CM, Kumita, JR
The conversion of human lysozyme into amyloid fibrils is associated with a rare but fatal hereditary form of nonneuropathic systemic amyloidosis. The accumulation of large amounts of aggregated protein is thought to be initiated by the formation of t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bc50596ba9dc6bb8ff5e360a3bbc5978
https://eprints.bbk.ac.uk/id/eprint/18499/1/18499.pdf
https://eprints.bbk.ac.uk/id/eprint/18499/1/18499.pdf
Akademický článek
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Autor:
Minkoo, Ahn, Christine L, Hagan, Ana, Bernardo-Gancedo, Erwin, De Genst, Francisco N, Newby, John, Christodoulou, Anne, Dhulesia, Mireille, Dumoulin, Carol V, Robinson, Christopher M, Dobson, Janet R, Kumita
Publikováno v:
Biophysical journal. 111(11)
The conversion of human lysozyme into amyloid fibrils is associated with a rare but fatal hereditary form of nonneuropathic systemic amyloidosis. The accumulation of large amounts of aggregated protein is thought to be initiated by the formation of t