Protein aggregation: folding aggregates, inclusion bodies and amyloid
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TLDR
Substantial data support the hypothesis that partially folded intermediates are key precursors to aggregates, that aggregation involves specific intermolecular interactions and that most aggregates involve beta sheets.About:
This article is published in Folding and Design.The article was published on 1998-02-01 and is currently open access. It has received 1115 citations till now. The article focuses on the topics: Protein aggregation & Amyloid.read more
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Aggresomes, inclusion bodies and protein aggregation.
TL;DR: This work has suggested that, in animal cells, aggregated proteins are specifically delivered to inclusion bodies by dynein-dependent retrograde transport on microtubules and this microtubule-dependent inclusion body is called an aggresome.
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Physical Stability of Proteins in Aqueous Solution: Mechanism and Driving Forces in Nonnative Protein Aggregation
TL;DR: The purpose of the current review is to provide a fundamental understanding of the mechanisms by which proteins aggregate and by which varying solution conditions, such as temperature, pH, salt type, salt concentration, cosolutes, preservatives, and surfactants, affect this process.
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Intrinsically Disordered Proteins in Human Diseases: Introducing the D2 Concept
TL;DR: Overall, intriguing interconnections among intrinsic disorder, cell signaling, and human diseases suggest that protein conformational diseases may result not only from protein misfolding, but also from misidentification, missignaling, and unnatural or nonnative folding.
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Chaperone-Mediated Protein Folding
TL;DR: The availability of high-resolution structures has facilitated a more detailed understanding of the complex chaperone machinery and mechanisms, including the ATP-dependent reaction cycles of the GroEL and HSP70 chaperones.
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Conformational constraints for amyloid fibrillation: the importance of being unfolded.
TL;DR: In this review, recent findings are surveyed to illustrate that protein fibrillogenesis requires a partially folded conformation, which is relatively unfolded, and shares many structural properties with the pre-molten globule state.
References
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Molecular chaperones in cellular protein folding.
TL;DR: Significant progress has been made in the understanding of the ATP-dependent mechanisms used by the Hsp70 and chaperonin families of molecular chaperones, which can cooperate to assist in folding new polypeptide chains.
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MODELS OF AMYLOID SEEDING IN ALZHEIMER'S DISEASE AND SCRAPIE: Mechanistic Truths and Physiological Consequences of the Time-Dependent Solubility of Amyloid Proteins
James Harper,Peter T. Lansbury +1 more
TL;DR: A simple mechanistic model has emerged for both processes that involves a nucleation-dependent polymerization that dictates that aggregation is dependent on protein concentration and time.
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Molecular chaperone functions of heat-shock proteins
TL;DR: The Hsp70 DnaK and Dna! are a Chaperone Team and the Translocation-Competent State of Precursor Proteins is maintained, and Cells Under Metabolic Stress is studied.
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The Hofmeister effect and the behaviour of water at interfaces.
TL;DR: The first general, detailed qualitative molecular mechanism for the origins of ion-specific (Hofmeister) effects on the surface potential difference at an air-water interface is proposed; this mechanism suggests a simple model for the behaviour of water at all interfaces, regardless of whether the non-aqueous component is neutral or charged, polar or non-polar.
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Huntingtin-Encoded Polyglutamine Expansions Form Amyloid-like Protein Aggregates In Vitro and In Vivo
Eberhard Scherzinger,Rudi Lurz,Mark Turmaine,Laura Mangiarini,Birgit Hollenbach,Renate Hasenbank,Gillian P. Bates,Stephen W. Davies,Hans Lehrach,Erich E. Wanker +9 more
TL;DR: In this study, it is shown that the proteolytic cleavage of a GST-huntingtin fusion protein leads to the formation of insoluble high molecular weight protein aggregates only when the polyglutamine expansion is in the pathogenic range.