Four of these keratin springs are twisted together to form a rope, called a protofibril, and eleven of these protofibrils are twisted together to form a thicker rope, called a microfibril. ❋ Carla (2006)
After refolding of MstnPP, misfolded yet soluble aggregates that form amyloid protofibrils and fibrils at a lowered pH can be observed. ❋ Carlene S. Starck Et Al. (2010)
Inability to enter the stacking gel is not a definitive indication of proteolysis resistance since partial hydrolysis may result in products smaller than fibrils and/or protofibrils yet still large enough to be retained in the stacking gel. ❋ Carlene S. Starck Et Al. (2010)
A defining characteristic of amyloid fibrils and protofibrils is their ability to bind the fluorescent dye thioflavin T (ThT) [63] - [65] ❋ Carlene S. Starck Et Al. (2010)
Cells incubated in media containing buffer (B) only (50 mM Tris-HCl pH 8.5, 150 mM NaCl for soluble aggregates and dimer; 0.005 mM HCl, pH 5.3 for protofibrils and fibrils) were used as a control. ❋ Carlene S. Starck Et Al. (2010)
These results suggest that a population of MstnPP can aggregate spontaneously to form amyloid-like protofibrils. ❋ Carlene S. Starck Et Al. (2010)
If the production of misfolded proteins overwhelms the UPR, protein aggregation may result in the generation of cytotoxic amyloid protofibrils and mature amyloid fibrils, contributing to amyloid diseases, including sIBM ❋ Carlene S. Starck Et Al. (2010)
The susceptibility of the soluble aggregates to trypsin digest suggests an open, flexible structure, consistent with CD results and supporting the conclusion that this species represents a prefibrillar intermediate rather than protofibrils. ❋ Carlene S. Starck Et Al. (2010)
(A-B) TEM of MstnPP soluble aggregates and C. insulin positive control containing both protofibrils (black arrow) and mature fibrils (white arrow). ❋ Carlene S. Starck Et Al. (2010)
Importantly, MstnPP aggregates and protofibrils have a negative effect on the viability of myoblasts. ❋ Carlene S. Starck Et Al. (2010)
Mohanty SK, Udgaonkar JB (2007) Mechanism of formation of amyloid protofibrils of barstar from soluble oligomers: evidence for multiple steps and lateral association coupled to conformational conversion. ❋ Carlene S. Starck Et Al. (2010)
The presence of MstnPP amyloid-like protofibrils suggests that amyloid fibril formation is also possible. ❋ Carlene S. Starck Et Al. (2010)
The cytotoxicity exhibited by MstnPP aggregates and protofibrils in C2C12 cells supports a mechanism in which aggregation by MstnPP in sIBM contributes to muscle degeneration. ❋ Carlene S. Starck Et Al. (2010)
To address this possibility, TEM analysis revealed that both MstnPP protofibrils ❋ Carlene S. Starck Et Al. (2010)
ThT binding assays were carried out on the MstnPP aggregates and compared to a solution containing a mixture of insulin protofibrils and fibrils as a positive control. ❋ Carlene S. Starck Et Al. (2010)
Significantly, MstnPP aggregates and protofibrils have a negative effect on the viability of C2C12 mouse myoblasts when added to the culture medium. ❋ Carlene S. Starck Et Al. (2010)
Figure 2: Characterization of Aβ42 oligomers, protofibrils and fibrils. ❋ Mahiuddin Ahmed (2010)
As the CD spectra of protofibrils of other amyloid-forming proteins is characterised by β-sheet absorption at 215-218 nm ❋ Carlene S. Starck Et Al. (2010)
