Scopus İndeksli Yayınlar Koleksiyonu / Scopus Indexed Publications Collection
Permanent URI for this collectionhttps://hdl.handle.net/11147/7148
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Article Citation - WoS: 30Citation - Scopus: 32Perylene-Embedded Electrospun Ps Fibers for White Light Generation(Elsevier Ltd., 2019) Güner, Tuğrul; Aksoy, Erkan; Demir, Mustafa Muammer; Varlıklı, CananPerylene dyes have been employed in the fabrication of white light due to their superior photophysical properties and relatively easy synthetic methods. However, their molecular aggregation in solid state is one of the main handicaps since it causes deviation in their optical properties and quenches photoluminescence quantum yields (Phi(f)). Investigation of the photophysical properties of a green (PTE), a yellow (PDI) and a new red (DiPhAPDI) emitting perylene derivative in solution, drop-casted films, polystyrene (PS) fibers and PS fibers embedded in poly (dimethyl siloxane) (PDMS) showed that PS:dye fibers prevent aggregation to some extend and allows high Of of dyes. The Of values of PTE, PDI and DiPhAPDI were all higher than 93.0% in solution and 84.8%, 94.3% and 73.6%, respectively in PS:dye fibers. Embedding the fibers in PDMS improved the photostabilities of the dyes two folds compared to their solution phases. The prepared dye containing fibers were combined together into a single PDMS film and utilized as a frequency conversion layer on a blue LED. Fabricated samples were found to show high color rendering index (>= 90), adjustable CCT (7500 K-5000 K), and power efficiency values exceeding 2001m/W depending on the used fiber amount in mass.Article Citation - WoS: 66Citation - Scopus: 71Signature of an Aggregation-Prone Conformation of Tau(Nature Publishing Group, 2017) Eschmann, Neil A.; Georgieva, Elka R.; Ganguly, Pritam; Borbat, Peter P.; Rappaport, Maxime D.; Akdoğan, Yaşar; Freed, Jack H.; Shea, Joan-Emma; Han, SongiThe self-assembly of the microtubule associated tau protein into fibrillar cell inclusions is linked to a number of devastating neurodegenerative disorders collectively known as tauopathies. The mechanism by which tau self-assembles into pathological entities is a matter of much debate, largely due to the lack of direct experimental insights into the earliest stages of aggregation. We present pulsed double electron-electron resonance measurements of two key fibril-forming regions of tau, PHF6 and PHF6∗, in transient as aggregation happens. By monitoring the end-to-end distance distribution of these segments as a function of aggregation time, we show that the PHF6 (∗) regions dramatically extend to distances commensurate with extended β-strand structures within the earliest stages of aggregation, well before fibril formation. Combined with simulations, our experiments show that the extended β-strand conformational state of PHF6 (∗) is readily populated under aggregating conditions, constituting a defining signature of aggregation-prone tau, and as such, a possible target for therapeutic interventions.