Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Charlotte Nerelius"'
Publikováno v:
Biochemical and Biophysical Research Communications. 402:515-518
Amyloid consists of β-sheet polymers and is associated with disease and with functional assemblies. Amyloid-forming proteins differ widely in native structures and sequences. We describe here how conformational preferences of non-polar amino acid re
Publikováno v:
Biochemical and Biophysical Research Communications. 396:2-6
Amyloid consists of cross-beta-sheet fibrils and is associated with about 25 human diseases, including several neurodegenerative diseases, systemic and localized amyloidoses and type II diabetes mellitus. Amyloid-forming proteins differ in structures
Autor:
Adolf Gogoll, Anna Sandegren, Per I. Arvidsson, Thomas Norström, Partha Pratim Bose, Urmimala Chatterjee, Jan Johansson, Charlotte Nerelius, Emmanuelle Göthelid, Thavendran Govender
Publikováno v:
Journal of Medicinal Chemistry. 52:8002-8009
Alzheimer's disease (AD), an age related neurodegenerative disorder, threatens to become a major health-economic problem. Assembly of 40- or 42-residue amyloid beta-peptides (Abeta) into neurotoxic oligo-/polymeric beta-sheet structures is an importa
Autor:
Charlotte Nerelius, Damian C. Crowther, H. Sargsyan, Sara Imarisio, André Fisahn, U. Chatterjee, David A. Lomas, H. Leijonmarck, Jan Johansson, A. Sandegren, Roger Strömberg, R. Raunak
Publikováno v:
Proceedings of the National Academy of Sciences. 106:9191-9196
The amyloid-β peptide (Aβ) can generate cytotoxic oligomers, and their accumulation is thought to underlie the neuropathologic changes found in Alzheimer's disease. Known inhibitors of Aβ polymerization bind to undefined structures and can work as
Publikováno v:
Biochemistry. 48:3778-3786
Amyloid fibrils are found in approximately 25 different diseases, including Alzheimer's disease. Lung surfactant protein C (SP-C) forms fibrils in association with pulmonary disease. It was recently found that the C-terminal domain of proSP-C (CTC),
Autor:
Charlotte Nerelius, Timothy E. Weaver, Emily P. Martin, Jan Johansson, Kerstin Nordling, Siwei Peng, Magnus Gustafsson
Publikováno v:
Biochemical Journal. 416:201-209
The newly synthesized proSP-C (surfactant protein C precursor) is an integral ER (endoplasmic reticulum) membrane protein with a single metastable polyvaline alpha-helical transmembrane domain that comprises two-thirds of the mature peptide. More tha
Autor:
Kerri J. Kinghorn, David A. Lomas, Damian C. Crowther, Charlotte Nerelius, Howard T. Chang, David Gubb, Lynda K. Sharp, Richard L. Davis, Jan Johansson, Clare Green
Publikováno v:
Journal of Biological Chemistry. 281:29268-29277
Alzheimer disease is characterized by extracellular plaques composed of Abeta peptides. We show here that these plaques also contain the serine protease inhibitor neuroserpin and that neuroserpin forms a 1:1 binary complex with the N-terminal or midd
Publikováno v:
Journal of Molecular Biology. 389:227-229
A subset of protein misfolding diseases, including, for example, Alzheimer's disease, is associated with the formation of highly insoluble amyloid fibrils with a beta-sheet structure. The amyloidogenic human lung surfactant protein C (SP-C) is genera
Publikováno v:
Diabetes & C-Peptide ISBN: 9781617793905
This review summarizes results on peptide interactions of proinsulin C-peptide. As we see it, knowledge on functional interactions of C-peptide has passed through several stages of research, now with at least three modes of postulated molecular expla
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::259ef22e89317898ac94a1f377f4fbfb
https://doi.org/10.1007/978-1-61779-391-2_2
https://doi.org/10.1007/978-1-61779-391-2_2
Publikováno v:
Biochemical and biophysical research communications. 403(3-4)
Evidence has emerged that proinsulin C-peptide has at least three types of functional interactions in addition to its role during synthesis and secretion of insulin. Thus, C-peptide has been shown (i) to bind to cell membranes triggering G-protein-me