...Mei Nakagawa; Takayuki Obita; Mineyuki Mizuguchi Destabilization of human transthyretin leads to its aggregation into amyloid fibrils, which causes a rare, progressive and fatal systemic disorder called ATTR amyloidosis. By contrast, murine transthyretin is known to be very stable and therefore...

... conditions encountered during its lifecycle. How parasite's chaperone machinery is able to maintain its aggregation-prone proteome in functional state, is poorly understood. As HSP70–40 system forms the central hub in cellular proteostasis, we investigated the protein folding capacity of PfHSP70-1...

...Igor Lima; Ambuja Navalkar; Samir K. Maji; Jerson L. Silva; Guilherme A.P. de Oliveira; Elio A. Cino Aggregation is the cause of numerous protein conformation diseases. A common facet of these maladies is the transition of a protein from its functional native state into higher order forms...

... ) * These authors contributed equally to this work. 12 3 2019 22 5 2019 27 5 2019 28 5 2019 © 2019 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society 2019 aggregation Alzheimer disease amyloid-beta neuroblastoma peptides toxicity...

...Eva Illes-Toth; Mafalda Ribeiro Ramos; Roberto Cappai; Caroline Dalton; David P Smith Misfolding and aggregation of α-synuclein (α-syn) into Lewy bodies is associated with a range of neurological disorders, including Parkinson's disease (PD). The cell-to-cell transmission of α-syn pathology has...

..., expresses a cryptic epitope also present in the oligomer. aggregation antibody α 1 -antitrypsin polymerization protein stability α 1 -Antitrypsin ( SERPINA1 ) is an acute-phase glycoprotein, secreted by hepatocytes and abundant in the plasma. A member of the serpin superfamily, the primary...

...Kristen E. Funk; Stefani N. Thomas; Kelsey N. Schafer; Grace L. Cooper; Zhongping Liao; David J. Clark; Austin J. Yang; Jeff Kuret In Alzheimer's disease, the microtubule-associated protein tau dissociates from the neuronal cytoskeleton and aggregates to form cytoplasmic inclusions. Although...

... of the EGFR kinase domain asymmetric dimer. Activation of the kinase domain by Peptide C also enhances phosphorylation of other substrates. Aggregation of the EGFR kinase domain by Peptide C probably underlies activation, and Peptide C precipitates several other proteins. Peptide C was found to form fibrils...

... to a β-rich intermediate state which initiates an aggregation pathway. This aggregation pathway is not an amyloid fibril pathway, as is that followed by the Aβ peptide, but rather a worm-like fibril pathway which, noticeably, turns out to be non-toxic. On the other hand, this pathway is thermodynamically...

... of classical and dynamic light scattering and NMR spectroscopy to demonstrate that AHSP forms a heterodimeric complex with α o that inhibits α o aggregation and promotes α o folding in the absence of haem. These findings indicate that AHSP may function as an α o -specific chaperone, and suggest an important...

...-dependent β-sheet formation and aggregation by thioflavin-T fluorescence in solution, whereas rA (rat amylin) did not. HSP70, GRP78/BiP and HSP40/DnaJ each independently suppressed hA misfolding. Maximal molar protein/hA ratios at which chaperone activity was detected were 1:200 (HSP70, HSP40/DnaJ and GRP78...

...Yo-hei Watanabe; Yosuke Nakazaki; Ryoji Suno; Masasuke Yoshida The ClpB chaperone forms a hexamer ring and rescues aggregated proteins in co-operation with the DnaK system. Each subunit of ClpB has two nucleotide-binding modules, AAA (ATPase associated with various cellular activities)-1 and AAA-2...

.... The results support the notion that self-aggregation is at the core of granule formation and sorting into the regulated pathway. 1 These authors have contributed equally to this work. 2 To whom correspondence should be addressed (email [email protected] ). 9 10 2007 16 10...

...Paul Evans; Christine Slingsby; B. A. Wallace Age-related cataract is a result of crystallins, the predominant lens proteins, forming light-scattering aggregates. In the low protein turnover environment of the eye lens, the crystallins are susceptible to modifications that can reduce stability...

...Isabel Cardoso; Maria Rosário Almeida; Nelson Ferreira; Gemma Arsequell; Gregorio Valencia; Maria João Saraiva Destabilization of the tetrameric fold of TTR (transthyretin) is important for aggregation of the protein which culminates in amyloid fibril formation. Many TTR mutations interfere...

... mentioned. In the experiments with thromboxane A 2 measurements, the treatment of PRP with aspirin was omitted. aggregation calcium mitogen-activated protein kinase (MAPK) protein kinase C Src family kinase Platelet activation is important for haemostasis and abnormal activation...

... , and the other with five more octapeptide repeats, rPrP 10OR . We found that the insertion mutant proteins are more prone to aggregate, and the degree and kinetics of aggregation are proportional to the number of inserts. The octapeptide-repeat and α-helix 1 regions are important in aggregate formation, because...

... LEA protein from wheat, have been subjected to functional analysis. Heat-stress experiments with citrate synthase, which is susceptible to aggregation at high temperatures, suggest that LEA proteins do not behave as classical molecular chaperones, but they do exhibit a protective, synergistic effect...

... to occur with some flavone glycones, including the C-glycosylflavone orientin. Inhibition of relaxation activity by flavonoids was found to be difficult to quantify and was most likely to be due to non-specific inhibition through flavonoid aggregation. As part of a structure–activity analysis, we also...

... structures, cross-linking and high-molecular-mass aggregation. Notwithstanding these structural changes, methylglyoxal- and glyoxal-modified α-crystallin showed enhanced anti-aggregation activity in various in vitro aggregation assays. Paradoxically, increased chaperone-like activity of modified α-crystallin...

..., Belgium 2 To whom correspondence should be addressed (e-mail [email protected] ). 7 5 2002 4 11 2002 8 11 2002 8 11 2002 The Biochemical Society, London ©2003 2003 aggregation antiparallel β-structure denaturation gel formation human interferon-γ...

...′-dimethyl-bis-( o -aminophenoxy)ethane- N , N , N ′, N ′-tetra-acetic acid], a high-affinity calcium chelator. All the experiments were performed with human platelets treated with aspirin, to avoid positive feedback from thromboxane A2. In the presence of Ro 31-8220, platelet aggregation caused by U46619...

...-specific ligands in murine platelets. We show that levels of GPVI—FcRγ of the order of 50% and 20% of wild-type levels caused 2- and 5-fold shifts to the right respectively in the dose—response curve for aggregation in response to collagen, the snake toxin convulxin and the monoclonal antibody JAQ1...

...) formed aberrant disulphide-bonded high-molecular-mass aggregates devoid of enzyme activity. Cell-surface biotinylation and digestion with phosphatidylinositol-specific phospholipase C showed that TNSALP (N153D) failed to reach the cell surface. Instead, double immunofluorescence demonstrated that TNSALP...