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TopProtein Misfolding, Prions and Amyloid
January 2010

Protein Misfolding, Prions and Amyloid

Papers Selected by Ferdinand Hucho, Jan Johansson and Hermona Soreq

Front cover: Fig. 2 and 3 from I V Baskakov, FEBS J 274 pp 3756-3765 3.

This Virtual Issue of the FEBS Journal is on protein misfolding, prions and amyloid and is the first in a series featuring current topics of neurochemistry. We have compiled reviews and original publications which have appeared in the FEBS Journal in the last two years. These topics are currently of special interest, as judged by the number of citations and downloads and even more so from the great number of manuscripts submitted to FEBS Journal in these areas. Many valuable articles were not included in this selection, which is not an indication of their lesser quality but rather a reflection of limitations on space.

Amyloid has been found to be associated with about 25 human diseases, many of which are neurodegenerative. It consists of disease-specific proteins or peptides with widely different native structures that have turned into insoluble ß-sheet fibrils. However, amyloid is also found in functional assemblies like bacterial curli fimbriae, yeast translation regulating proteins, and human pigment binding templates. In spite of significant recent advances in the understanding of the amyloid state at a molecular level, several important questions remain unanswered. Prions and amyloids bridge the gap between fundamental and applied research, because both the protein chemistry of misfolding and fibril formation and the molecular basis of the observed pathological effects are poorly understood. The majority of disease-related papers included in the list are reviews and research publications on Alzheimer’s Disease and Parkinson’s Disease, but functional amyloid and methodological aspects are also covered.

We hope this selection of FEBS Journal publications in the field of Neurochemistry will be informative and useful, for the beginner and specialist alike.

Review Articles

Cell biology, regulation and inhibition of β-secretase (BACE-1) (276, p 1845-1859)
Clare E. Hunt, Anthony J. Turner

Emerging pathways in genetic Parkinson's disease: Autosomal-recessive genes in Parkinson's disease – a common pathway? (275, p 5758-5766)
Julia C. Fitzgerald, Helene Plun-Favreau

Emerging pathways in genetic Parkinson's disease: tangles, Lewy bodies and LRRK2 (275, p 5748-5757)
Michael J. Devine, Patrick A. Lewis

Therapeutic approaches for prion and Alzheimer's diseases (274, p 3784-3798)
Thomas Wisniewski, Einar M. Sigurdsson

The modulation of metal bio-availability as a therapeutic strategy for the treatment of Alzheimer's disease (274, p 3775-3783)
Peter J. Crouch, Anthony R. White, Ashley I. Bush

Branched chain mechanism of polymerization and ultrastructure of prion protein amyloid fibrils (274, p 3756-3765)
Ilia V. Baskakov

The spread of prions through the body in naturally acquired transmissible spongiform encephalopathies (274, p 588-605)
Michael Beekes, Patricia A. McBride

Original Articles

The thioflavin T fluorescence assay for amyloid fibril detection can be biased by the presence of exogenous compounds (276, p 5960-5972)
Sean A. Hudson, Heath Ecroyd, Tak W. Kee, John A. Carver

An orphan dermaseptin from frog skin reversibly assembles to amyloid-like aggregates in a pH-dependent fashion (276, p 5849-5859)
Ruth Gößler-Schöfberger, Günter Hesser, Martin Muik, Christian Wechselberger, Alexander Jilek

Energy barriers for HET-s prion forming domain amyloid formation (276, p 5053-5064)
Raimon Sabaté, Virginia Castillo, Alba Espargaró, Sven J. Saupe and Salvador Ventura

Insulin is a kinetic but not a thermodynamic inhibitor of amylin aggregation (276, p 3365-3371)
Wei Cui, Jing-wen Ma, Peng Lei, Wei-hui Wu, Ye-ping Yu, Yu Xiang, Ai-jun Tong, Yu-fen Zhao, Yan-mei Li

Perturbation of membranes by the amyloid β-peptide – a molecular dynamics study (276, p 3060-3075)
Justin A. Lemkul, David R. Bevan

Interactions between the amyloid precursor protein C-terminal domain and G proteins mediate calcium dysregulation and amyloid β toxicity in Alzheimer's disease (276, p 2736-2751)
Gideon M. Shaked, Stephanie Chauv, Kiren Ubhi, Lawrence A. Hansen, Eliezer Masliah

Prion protein library of recombinant constructs for structural biology (276, p 2359-2367)
Simone Hornemann, Barbara Christen, Christine von Schroetter, Daniel R. Pérez, Kurt Wüthrich

The effects of α-secretase ADAM10 on the proteolysis of neuregulin-1 (276, p 1568-1580)
Christian Freese, Alistair N. Garratt, Falk Fahrenholz, Kristina Endres

A facile method for expression and purification of the Alzheimer's disease-associated amyloid β-peptide (276, p 1266-1281)
Dominic M. Walsh, Eva Thulin, Aedín M. Minogue, Niklas Gustavsson, Eric Pang, David B. Teplow, Sara Linse

Formation of highly toxic soluble amyloid beta oligomers by the molecular chaperone prefoldin (275, p 5982-5993)
Masafumi Sakono, Tamotsu Zako, Hiroshi Ueda, Masafumi Yohda, Mizuo Maeda

Lipid-induced conformational transition of the amyloid core fragment Aβ(28–35) and its A30G and A30I mutants (275, p 2415-2427)
Sureshbabu Nagarajan, Kirubagaran Ramalingam, P. Neelakanta Reddy, Damiano M. Cereghetti, E. J. Padma Malar, Jayakumar Rajadas

Linkage-dependent contribution of repeat peptides to self-aggregation of three- or four-repeat microtubule-binding domains in tau protein (275, p 1529-1539)
Kayoko Okuyama, Chisato Nishiura, Fumie Mizushima, Katsuhiko Minoura, Miho Sumida, Taizo Taniguchi, Koji Tomoo, Toshimasa Ishida

Active γ-secretase is localized to detergent-resistant membranes in human brain (275, p 1174-1187)
Ji-Yeun Hur, Hedvig Welander, Homira Behbahani, Mikio Aoki, Jenny Frånberg, Bengt Winblad, Susanne Frykman, Lars O. Tjernberg

Dynamics of α-synuclein aggregation and inhibition of pore-like oligomer development by β-synuclein (274, p 1862-1877)
Igor F. Tsigelny, Pazit Bar-On, Yuriy Sharikov, Leslie Crews, Makoto Hashimoto, Mark A. Miller, Steve H. Keller, Oleksandr Platoshyn, Jason X.-J. Yuan, Eliezer Masliah

RCAN1-1L is overexpressed in neurons of Alzheimer's disease patients (274, p 1715-1724)
Cathryn D. Harris, Gennady Ermak, Kelvin J. A. Davies

The C-terminal region of CHD3/ZFH interacts with the CIDD region of the Ets transcription factor ERM and represses transcription of the human presenilin 1 gene (274, p 1434-1448)
Martine Pastorcic, Hriday K. Das

Docosahexaenoic acid stabilizes soluble amyloid-β protofibrils and sustains amyloid-β-induced neurotoxicity in vitro (274, p 990-1000)
Ann-Sofi Johansson, Anita Garlind, Fredrik Berglind-Dehlin, Göran Karlsson, Katarina Edwards, Pär Gellerfors, Frida Ekholm-Pettersson, Jan Palmblad, Lars Lannfelt

High-resolution NMR studies of the zinc-binding site of the Alzheimer's amyloid β-peptide (274, p 46-59)
Jens Danielsson, Roberta Pierattelli, Lucia Banci, Astrid Gräslund