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文章名     作者     期刊名     摘要     卷     期         如果没有找到您所需要的文献，请点击 ——此处申请     共16条记录   Protein folding, misfolding and disease Preface [作者：Hammarstrom, P,期刊：FEBS Letters, 页码：2579-2580 , 文章类型： Editorial Material，,卷期：2009年583-16] Bridging the gap: From protein misfolding to protein misfolding diseases [作者：Luheshi, LM; Dobson, CM,期刊：FEBS Letters, 页码：2581-2586 , 文章类型： Review，,卷期：2009年583-16] Protein misfolding and aggregation are pathognomic for a number of the most common age-related degenerative diseases. Great progress has been made in studying protein aggregation in the test tube and also in replicating ... Biosensor-based label-free assays of amyloid growth [作者：White, DA; Buell, AK; Dobson, CM; Welland, ME; Knowles, TPJ,期刊：FEBS Letters, 页码：2587-2592 , 文章类型： Review，,卷期：2009年583-16] Uncontrolled fibrous protein aggregation is implicated in a range of aberrant biological phenomena. Much effort has consequently been directed towards establishing quantitative in vitro assays of this process with the ai... Small organic probes as amyloid specific ligands - Past and recent molecular scaffolds [作者：Nilsson, KPR,期刊：FEBS Letters, 页码：2593-2599 , 文章类型： Review，,卷期：2009年583-16] Molecular probes for selective staining and imaging of protein aggregates, such as amyloid, are important to advance our understanding of the molecular mechanisms underlying protein misfolding diseases and also for obtai... Methods for structural characterization of prefibrillar intermediates and amyloid fibrils [作者：Langkilde, AE; Vestergaard, B,期刊：FEBS Letters, 页码：2600-2609 , 文章类型： Review，,卷期：2009年583-16] Protein fibrillation is first and foremost a structural phenomenon. Adequate structural investigation of the central conformational individuals of the fibrillation process is however exceedingly difficult. This is due to... Structure-activity relationship of amyloid fibrils [作者：Maji, SK; Wang, L; Greenwald, J; Riek, R,期刊：FEBS Letters, 页码：2610-2617 , 文章类型： Review，,卷期：2009年583-16] Protein aggregation is a process in which proteins self-associate into imperfectly ordered macroscopic entities. Such aggregates are generally classified as either amorphous or highly ordered, the most common form of the... Switching in amyloid structure within individual fibrils: Implication for strain adaptation, species barrier and strain classification [作者：Baskakov, IV,期刊：FEBS Letters, 页码：2618-2622 , 文章类型： Review，,卷期：2009年583-16] Amyloid fibrils are highly ordered crystal-like structures. It is generally assumed that individual amyloid fibrils consist of conformationally uniform cross-beta-sheet structures that enable the amyloids to replicate th... Glimpses of the molecular mechanisms of beta(2)-microglobulin fibril formation in vitro: Aggregation on a complex energy landscape [作者：Platt, GW; Radford, SE,期刊：FEBS Letters, 页码：2623-2629 , 文章类型： Review，,卷期：2009年583-16] beta(2)-microglobulin (beta(2)m) is a 99-residue protein that aggregates to form amyloid fibrils in dialysis-related amyloidosis. The protein provides a powerful model for exploration of the structural molecular mechanis... Native-like aggregation of the acylphosphatase from Sulfolobus solfataricus and its biological implications [作者：Bemporad, F; Chiti, F,期刊：FEBS Letters, 页码：2630-2638 , 文章类型： Review，,卷期：2009年583-16] Studies in vitro show that globular proteins can experience the formation of native-like conformational states able to self-assemble with no need of transitions across the energy barrier for unfolding, and that such proc... The proteostasis boundary in misfolding diseases of membrane traffic [作者：Hutt, DM; Powers, ET; Balch, WE,期刊：FEBS Letters, 页码：2639-2646 , 文章类型： Review，,卷期：2009年583-16] Protein function is regulated by the proteostasis network (PN) [Balch, W. E., Morimoto, R. I., Dillin, A. and Kelly, J.W. (2008) Adapting proteostasis for disease intervention. Science 319, 916-919], an integrated biolog... The role of molecular chaperones in human misfolding diseases [作者：Broadley, SA; Hartl, FU,期刊：FEBS Letters, 页码：2647-2653 , 文章类型： Review，,卷期：2009年583-16] Human misfolding diseases arise when proteins adopt non-native conformations that endow them with a tendency to aggregate and form intra- and/or extra-cellular deposits. Molecular chaperones, such as Hsp70 and TCP-1 Ring... The GroEL/GroES cis cavity as a passive anti-aggregation device [作者：Horwich, AL; Apetri, AC; Fenton, WA,期刊：FEBS Letters, 页码：2654-2662 , 文章类型： Review，,卷期：2009年583-16] The GroEL/GroES chaperonin folding chamber is an encapsulated space of similar to 65 angstrom diameter with a hydrophilic wall, inside of which many cellular proteins reach the native state. The question of whether the c... Animal models of human amyloidoses: Are transgenic mice worth the time and trouble? [作者：Buxbaum, JN,期刊：FEBS Letters, 页码：2663-2673 , 文章类型： Review，,卷期：2009年583-16] The amyloidoses are the prototype gain of toxic function protein misfolding diseases. As such, several naturally occurring animal models and their inducible variants provided some of the first insights into these disorde... Cells and prions: A license to replicate [作者：Nuvolone, M; Aguzzi, A; Heikenwalder, M,期刊：FEBS Letters, 页码：2674-2684 , 文章类型： Review，,卷期：2009年583-16] Prion diseases are neurodegenerative, infectious disorders characterized by the aggregation of a misfolded isoform of the cellular prion protein (PrPC). The infectious agent - termed prion - is mainly composed of misfold... Serum amyloid A and protein AA: Molecular mechanisms of a transmissible amyloidosis [作者：Westermark, GT; Westermark, P,期刊：FEBS Letters, 页码：2685-2690 , 文章类型： Review，,卷期：2009年583-16] Systemic AA-amyloidosis is a complication of chronic inflammatory diseases and the fibril protein AA derives from the acute phase reactant serum AA. AA-amyloidosis can be induced in mice by an inflammatory challenge. The... Physiological responses to protein aggregates: Fibrinolysis, coagulation and inflammation (new roles for old factors) [作者：Gebbink, MFBG; Bouma, B; Maas, C; Bouma, BN,期刊：FEBS Letters, 页码：2691-2699 , 文章类型： Review，,卷期：2009年583-16] Misfolding is an inherent and potentially problematic propensity of proteins. Misfolded proteins tend to aggregate and the deposition of aggregated proteins is associated with a variety of highly debilitating diseases kn...