Results 11 to 20 of about 69,622 (226)

Mammalian amyloidogenic proteins promote prion nucleation in yeast. [PDF]

J Biol Chem, 2018
Fibrous cross-β aggregates (amyloids) and their transmissible forms (prions) cause diseases in mammals (including humans) and control heritable traits in yeast. Initial nucleation of a yeast prion by transiently overproduced prion-forming protein or its (typically, QN-rich) prion domain is efficient only in the presence of another aggregated (in most ...
Chandramowlishwaran P, Sun M, Casey KL, Romanyuk AV, Grizel AV, Sopova JV, Rubel AA, Nussbaum-Krammer C, Vorberg IM, Chernoff YO.   +9 more
europepmc   +5 more sources

Predicting Amyloidogenic Proteins in the Proteomes of Plants. [PDF]

Int J Mol Sci, 2017
Amyloids are protein fibrils with characteristic spatial structure. Though amyloids were long perceived to be pathogens that cause dozens of incurable pathologies in humans and mammals, it is currently clear that amyloids also represent a functionally important form of protein structure implicated in a variety of biological processes in organisms ...
Antonets KS, Nizhnikov AA.
europepmc   +4 more sources

Yeast Approach in Amyloidogenic Proteins Study

Proceedings
Self-reproducing protein aggregates of a fibrillar nature (amyloids) are associated with a number of animal and human diseases [...]
Andrew A. Zelinsky, Marina V. Ryabinina, Yury O. Chernoff, Aleksandr A. Rubel   +3 more
doaj   +2 more sources

Apolipoprotein E and Alzheimer's disease: the influence of apolipoprotein E on amyloid-β and other amyloidogenic proteins. [PDF]

J Lipid Res, 2017
Huynh TV, Davis AA, Ulrich JD, Holtzman DM.   +3 more
europepmc   +3 more sources

Amyloids: Regulators of Metal Homeostasis in the Synapse

Molecules, 2020
Conformational changes in amyloidogenic proteins, such as β-amyloid protein, prion proteins, and α-synuclein, play a critical role in the pathogenesis of numerous neurodegenerative diseases, including Alzheimer’s disease, prion disease, and Lewy body ...
Masahiro Kawahara, Midori Kato-Negishi, Ken-ichiro Tanaka   +2 more
doaj   +1 more source

Amyloidogenic sequences in native protein structures [PDF]

Protein Science, 2010
AbstractNumerous short peptides have been shown to form β‐sheet amyloid aggregates in vitro. Proteins that contain such sequences are likely to be problematic for a cell, due to their potential to aggregate into toxic structures. We investigated the structures of 30 proteins containing 45 sequences known to form amyloid, to see how the proteins cope ...
Tzotzos, Susan, Doig, Andrew J.
openaire   +3 more sources

An in vitro workflow of neuron-laden agarose-laminin hydrogel for studying small molecule-induced amyloidogenic condition.

PLoS ONE, 2022
In vitro studies have been popularly used to determine the cellular and molecular mechanisms for many decades. However, the traditional two-dimension (2D) cell culture which grows cells on a flat surface does not fully recapitulate the pathological ...
Poommaree Namchaiw, Patapon Bunreangsri, Piyaporn Eiamcharoen, Salita Eiamboonsert, Rungtiva P Poo-Arporn   +4 more
doaj   +1 more source

Fibril-forming motifs are essential and sufficient for the fibrillization of human Tau. [PDF]

PLoS ONE, 2012
BACKGROUND: The misfolding of amyloidogenic proteins including human Tau protein, human prion protein, and human α-synuclein is involved in neurodegenerative diseases such as Alzheimer disease, prion disease, and Parkinson disease.
Sheng-Rong Meng, Ying-Zhu Zhu, Tong Guo, Xiao-Ling Liu, Jie Chen, Yi Liang   +5 more
doaj   +1 more source

CARs-DB: A Database of Cryptic Amyloidogenic Regions in Intrinsically Disordered Proteins

Frontiers in Molecular Biosciences, 2022
Proteome-wide analyses suggest that most globular proteins contain at least one amyloidogenic region, whereas these aggregation-prone segments are thought to be underrepresented in intrinsically disordered proteins (IDPs).
Carlos Pintado-Grima, Oriol Bárcenas, Zoe Manglano-Artuñedo, Rita Vilaça, Sandra Macedo-Ribeiro, Irantzu Pallarès, Jaime Santos, Salvador Ventura   +7 more
doaj   +1 more source

ReRF-Pred: predicting amyloidogenic regions of proteins based on their pseudo amino acid composition and tripeptide composition

BMC Bioinformatics, 2021
Background Amyloids are insoluble fibrillar aggregates that are highly associated with complex human diseases, such as Alzheimer’s disease, Parkinson’s disease, and type II diabetes.
Zhixia Teng, Zitong Zhang, Zhen Tian, Yanjuan Li, Guohua Wang   +4 more
doaj   +1 more source