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Literature DB >> 19545568

Bridging the gap: from protein misfolding to protein misfolding diseases.

Abstract

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 protein aggregation in vertebrate animal models of these diseases. However, we argue here that the development and effective integration of emerging techniques such as the methods of nanoscience and the use of invertebrate models are now providing powerful new opportunities to advance our current understanding of the fundamental origins of these disorders.

Entities: Disease

Mesh：

Substances：
Amyloid
Proteins

Year: 2009 PMID： 19545568 DOI： 10.1016/j.febslet.2009.06.030

Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124

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Cited

34 in total

1. The impact of solubility and electrostatics on fibril formation by the H3 and H4 histones.

Authors: Traci B Topping; Lisa M Gloss
Journal: Protein Sci Date: 2011-11-09 Impact factor: 6.725

2. Comparing the folding and misfolding energy landscapes of phosphoglycerate kinase.

Authors: Gergely Agócs; Bence T Szabó; Gottfried Köhler; Szabolcs Osváth
Journal: Biophys J Date: 2012-06-19 Impact factor: 4.033

Review 3. Converting a protein into a switch for biosensing and functional regulation.

Authors: Margaret M Stratton; Stewart N Loh
Journal: Protein Sci Date: 2011-01 Impact factor: 6.725

4. A disease-causing mutation in the active site of serine palmitoyltransferase causes catalytic promiscuity.

Authors: Kenneth Gable; Sita D Gupta; Gongshe Han; Somashekarappa Niranjanakumari; Jeffrey M Harmon; Teresa M Dunn
Journal: J Biol Chem Date: 2010-05-26 Impact factor: 5.157

5. Protective spin-labeled fluorenes maintain amyloid beta peptide in small oligomers and limit transitions in secondary structure.

Authors: Robin Altman; Sonny Ly; Silvia Hilt; Jitka Petrlova; Izumi Maezawa; Tamás Kálai; Kálmán Hideg; Lee-Way Jin; Ted A Laurence; John C Voss
Journal: Biochim Biophys Acta Date: 2015-09-14

6. Conformation types of ubiquitin [M+8H]8+ Ions from water:methanol solutions: evidence for the N and A States in aqueous solution.

Authors: Huilin Shi; Nicholas A Pierson; Stephen J Valentine; David E Clemmer
Journal: J Phys Chem B Date: 2012-03-02 Impact factor: 2.991

Bridging the gap: from protein misfolding to protein misfolding diseases.

1. The impact of solubility and electrostatics on fibril formation by the H3 and H4 histones.

2. Comparing the folding and misfolding energy landscapes of phosphoglycerate kinase.

Review 3. Converting a protein into a switch for biosensing and functional regulation.

4. A disease-causing mutation in the active site of serine palmitoyltransferase causes catalytic promiscuity.

5. Protective spin-labeled fluorenes maintain amyloid beta peptide in small oligomers and limit transitions in secondary structure.

6. Conformation types of ubiquitin [M+8H]8+ Ions from water:methanol solutions: evidence for the N and A States in aqueous solution.

Review 7. Gene therapy for misfolding protein diseases of the central nervous system.

Review 8. Relationship of electrophilic stress to aging.

9. Insights into prion biology: integrating a protein misfolding pathway with its cellular environment.

10. Stress-independent activation of XBP1s and/or ATF6 reveals three functionally diverse ER proteostasis environments.