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Year | Number of Results |
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2007 | 1 |
2010 | 1 |
2012 | 2 |
2013 | 2 |
2024 | 0 |
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A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils.
PLoS Biol. 2007 May;5(5):e134. doi: 10.1371/journal.pbio.0050134.
PLoS Biol. 2007.
PMID: 17472440
Free PMC article.
Structural features of proinsulin C-peptide oligomeric and amyloid states.
Lind J, Lindahl E, Perálvarez-Marín A, Holmlund A, Jörnvall H, Mäler L.
Lind J, et al.
FEBS J. 2010 Sep;277(18):3759-68. doi: 10.1111/j.1742-4658.2010.07777.x. Epub 2010 Aug 3.
FEBS J. 2010.
PMID: 20738396
Free article.
Item in Clipboard
SERF protein is a direct modifier of amyloid fiber assembly.
Falsone SF, Meyer NH, Schrank E, Leitinger G, Pham CL, Fodero-Tavoletti MT, Holmberg M, Dulle M, Scicluna B, Gesslbauer B, Rückert HM, Wagner GE, Merle DA, Nollen EA, Kungl AJ, Hill AF, Cappai R, Zangger K.
Falsone SF, et al.
Cell Rep. 2012 Aug 30;2(2):358-71. doi: 10.1016/j.celrep.2012.06.012. Epub 2012 Jul 26.
Cell Rep. 2012.
PMID: 22854022
Free PMC article.
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Insulin solubility transitions by pH-dependent interactions with proinsulin C-peptide.
Landreh M, Alvelius G, Willander H, Stukenborg JB, Söder O, Johansson J, Jörnvall H.
Landreh M, et al.
FEBS J. 2012 Dec;279(24):4589-97. doi: 10.1111/febs.12045. Epub 2012 Nov 21.
FEBS J. 2012.
PMID: 23106816
Free article.
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Amino acid sequence determinants in self-assembly of insulin chiral amyloid superstructures: role of C-terminus of B-chain in association of fibrils.
Babenko V, Dzwolak W.
Babenko V, et al.
FEBS Lett. 2013 Mar 18;587(6):625-30. doi: 10.1016/j.febslet.2013.02.010. Epub 2013 Feb 14.
FEBS Lett. 2013.
PMID: 23416304
Free article.
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Peptides that form β-sheets on hydrophobic surfaces accelerate surface-induced insulin amyloidal aggregation.
Nault L, Vendrely C, Bréchet Y, Bruckert F, Weidenhaupt M.
Nault L, et al.
FEBS Lett. 2013 May 2;587(9):1281-6. doi: 10.1016/j.febslet.2012.11.036. Epub 2013 Mar 16.
FEBS Lett. 2013.
PMID: 23510797
Free article.
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