Transient dynamics of Aβ contribute to toxicity in Alzheimer's disease

Autor: Kris Pauwels, Kerensa Broersen, Ellen Hubin, N. A. J. van Nuland

Publikováno v: Cellular and Molecular Life Sciences
Cellular and Molecular Life Sciences, 71(18), 3507-3521. Birkhäuser

The aggregation and deposition of the amyloid-beta peptide (Abeta) in the brain has been linked with neuronal death, which progresses in the diagnostic and pathological signs of Alzheimer's disease (AD). The transition of an unstructured monomeric pe

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::041515d7a0848c40e671653794194c47
https://pubmed.ncbi.nlm.nih.gov/24803005

Experimental evidence for a reversible alfa to beta transition of abeta-(1-42) in aqueous media: A step by step conformational analysis pinpoints the location of the beta conformation seeding

Autor: S. Tomaselli, N. A. J. van Nuland, A. M. J. J. Bonvin, S. Salvadori, T. Tancredi, P. A. Temussi, PICONE, DELIA

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______3730::dcd1cd37885deceebdd3f459f630adf5
http://hdl.handle.net/11588/516532

Conformational Stability of Muscle Acylphosphatase: The Role of Temperature, Denaturant Concentration, and pH

Autor: Niccolò Taddei, Fabrizio Chiti, Francesca Magherini, Christopher M. Dobson, Massimo Stefani, Giampietro Ramponi, N. A. J. Van Nuland

Publikováno v: Biochemistry. 37:1447-1455

The conformational stability (delta G) of muscle acylphosphatase, a small alpha/beta globular protein, has been determined as a function of temperature, urea concentration, and pH. A combination of thermally induced and urea-induced unfolding, monito

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::561f79afb5b85cbbb31069d6afaa711e
https://doi.org/10.1021/bi971692f

Conformation and aggregation of M13 coat protein studied by molecular dynamics

Autor: N. A. J. Van Nuland, J.C. Sanders, Olle Edholm, Marcus A. Hemminga

Publikováno v: Biophysical Chemistry, 41, 193-202
Biophysical Chemistry 41 (1991)

Molecular dynamics (MD) simulations are performed on M13 coat protein, a small membrane protein for which both alpha- and beta-structures have been suggested. The simulations are started from initial conformations that are either monomers or dimers o

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3c7afc1e294d75b70b26f5a44c26a48d
https://doi.org/10.1016/0301-4622(91)80019-n

A NMR investigation on the interactions of the alpha-oligomeric form of the M13 coat protein with lipids, which mimic the Escherichia coli inner membrane

Autor: N. A. J. Van Nuland, Ruud B. Spruijt, Marcus A. Hemminga, Johan C. Sanders, Trevor W. Poile, Anthony Watts

Publikováno v: Biochimica et biophysica acta-protein structure and molecular enzymology 1066 (1991)
Biochimica et biophysica acta-protein structure and molecular enzymology, 1066, 102-108

The interaction of the M13 bacteriophage major coat protein in the alpha-oligomeric form with specifically deuterated phospholipid headgroups which mimic the Escherichia coli inner membrane, has been studied using NMR methods. As can be seen from the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::704aa6459cafb99885b00410f075ca32
http://ora.ox.ac.uk/objects/uuid:499fd922-8c36-4719-aa0a-cb7027beb76e