Search Results - "FINK, ANTHONY L."

Conformational constraints for amyloid fibrillation: the importance of being unfolded by Uversky, Vladimir N., Fink, Anthony L.

“…Recent reports give strong support to the idea that amyloid fibril formation and the subsequent development of protein deposition diseases originate from…”
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Chaperone-Mediated Protein Folding by Fink, Anthony L

“…Department of Chemistry and Biochemistry, The University of California, Santa Cruz, California Fink, Anthony L. The folding of most newly synthesized proteins…”
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Early Events in the Fibrillation of Monomeric Insulin by Ahmad, Atta, Uversky, Vladimir N., Hong, Dongpyo, Fink, Anthony L.

“…Insulin has a largely α-helical structure and exists as a mixture of hexameric, dimeric, and monomeric states in solution, depending on the conditions: the…”
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Effects of Various Flavonoids on the α-Synuclein Fibrillation Process by Uversky, Vladimir N., Fink, Anthony L., Munishkina, Larissa A., Meng, Xiaoyun

“…α-Synuclein aggregation and fibrillation are closely associated with the formation of Lewy bodies in neurons and are implicated in the causative pathogenesis…”
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Disorder in the Nuclear Pore Complex: The FG Repeat Regions of Nucleoporins Are Natively Unfolded by Denning, Daniel P., Patel, Samir S., Uversky, Vladimir, Fink, Anthony L., Rexach, Michael

“…Nuclear transport proceeds through nuclear pore complexes (NPCs) that are embedded in the nuclear envelope of eukaryotic cells. The Saccharomyces cerevisiae…”
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Effect of Environmental Factors on the Kinetics of Insulin Fibril Formation:  Elucidation of the Molecular Mechanism by Nielsen, Liza, Khurana, Ritu, Coats, Alisa, Frokjaer, Sven, Brange, Jens, Vyas, Sandip, Uversky, Vladimir N, Fink, Anthony L

“…In the search for the molecular mechanism of insulin fibrillation, the kinetics of insulin fibril formation were studied under different conditions using the…”
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The Aggregation and Fibrillation of α-Synuclein by Fink, Anthony L

“…α-Synuclein is a small (14 kDa), abundant, intrinsically disordered presynaptic protein, whose aggregation is believed to be a critical step in Parkinson's…”
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Tau Filaments from Human Brain and from in vitro Assembly of Recombinant Protein Show Cross-β Structure by Berriman, John, Serpell, Louise C., Oberg, Keith A., Fink, Anthony L., Goedert, Michel, Crowther, R. Anthony

“…Abnormal filaments consisting of hyperphosphorylated microtubule-associated protein tau form in the brains of patients with Alzheimer's disease, Down's…”
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The effect of macromolecular crowding on protein aggregation and amyloid fibril formation by Munishkina, Larissa A., Cooper, Elisa M., Uversky, Vladimir N., Fink, Anthony L.

“…Macromolecular crowding is expected to have several significant effects on protein aggregation; the major effects will be those due to excluded volume and…”
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Partially Folded Intermediates in Insulin Fibrillation by Ahmad, Atta, Millett, Ian S, Doniach, Sebastian, Uversky, Vladimir N, Fink, Anthony L

“…Native zinc-bound insulin exists as a hexamer at neutral pH. Under destabilizing conditions, the hexamer dissociates, and is very prone to forming fibrils…”
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Fibrillation of Human Insulin A and B Chains by Hong, Dong-Pyo, Ahmad, Atta, Fink, Anthony L

“…Human insulin, which consists of disulfide cross-linked A and B polypeptide chains, readily forms amyloid fibrils under slightly destabilizing conditions. We…”
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Surface-catalyzed Amyloid Fibril Formation by Zhu, Min, Souillac, Pierre O., Ionescu-Zanetti, Cristian, Carter, Sue A., Fink, Anthony L.

“…Light chain (or AL) amyloidosis is characterized by the pathological deposition of insoluble fibrils of immunoglobulin light chain fragments in various…”
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Characterization of the non-fibrillar α-synuclein oligomers by Hong, Dong-Pyo, Han, Shubo, Fink, Anthony L, Uversky, Vladimir N

“…Under certain in vitro conditions, α-Synuclein is an abundant 14 kDa presynaptic intrinsically disordered protein, involved in the pathogenesis of Parkinson's…”
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Structural Characterization of the Partially Folded Intermediates of an Immunoglobulin Light Chain Leading to Amyloid Fibrillation and Amorphous Aggregation by Qin, Zhijie, Hu, Dongmei, Zhu, Min, Fink, Anthony L

“…Immunoglobulin light chain deposition diseases involve various types of extracellular deposition of light chain variable domains, including amyloid fibrils and…”
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Oxidized quercetin inhibits α-synuclein fibrillization by Zhu, Min, Han, Shubo, Fink, Anthony L.

“…α-Synucein is a small (14kDa), abundant, intrinsically disordered presynaptic protein, whose aggregation is believed to be a critical step in Parkinson's…”
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Natively unfolded proteins by Fink, Anthony L

“…It is now clear that a significant fraction of eukaryotic genomes encode proteins with substantial regions of disordered structure. In spite of the lack of…”
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Partially Folded Intermediates as Critical Precursors of Light Chain Amyloid Fibrils and Amorphous Aggregates by Khurana, Ritu, Gillespie, Joel R, Talapatra, Anupam, Minert, Lauren J, Ionescu-Zanetti, Cristian, Millett, Ian, Fink, Anthony L

“…Light chain, or AL, amyloidosis is a pathological condition arising from systemic extracellular deposition of monoclonal immunoglobulin light chain variable…”
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Protein aggregation: folding aggregates, inclusion bodies and amyloid by Fink, Anthony L

“…Aggregation results in the formation of inclusion bodies, amyloid fibrils and folding aggregates. Substantial data support the hypothesis that partially folded…”
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Distinct β‑Sheet Structure in Protein Aggregates Determined by ATR–FTIR Spectroscopy by Shivu, Bhavana, Seshadri, Sangita, Li, Jie, Oberg, Keith A, Uversky, Vladimir N, Fink, Anthony L

“…Attenuated total reflectance Fourier transform infrared spectroscopy (ATR–FTIR) was used to study the conformation of aggregated proteins in vivo and in vitro…”
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Stimulation of Insulin Fibrillation by Urea-induced Intermediates by Ahmad, Atta, Millett, Ian S., Doniach, Sebastian, Uversky, Vladimir N., Fink, Anthony L.

“…Fibrillar deposits of insulin cause serious problems in implantable insulin pumps, commercial production of insulin, and for some diabetics. We performed a…”
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