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Literature DB >> 19415709

Position-dependent electrostatic protection against protein aggregation.

Alexander K Buell¹, Gian Gaetano Tartaglia, Neil R Birkett, Christopher A Waudby, Michele Vendruscolo, Xavier Salvatella, Mark E Welland, Christopher M Dobson, Tuomas P J Knowles.

Abstract

Proteins with a high propensity to aggregate can be largely prevented from doing so with surprisingly small changes to their primary structure. By using a combination of rational design and quantitative measurements of aggregation rates, we show that adding a single charge in specific "gatekeeper" regions is sufficient to change the timescale for amyloid fibril growth from minutes to weeks, thereby dramatically reducing the efficiency of this process.

Entities: Disease Species

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Year: 2009 PMID： 19415709 DOI： 10.1002/cbic.200900144

Source DB: PubMed Journal: Chembiochem ISSN： 1439-4227 Impact factor: 3.164

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Cited

17 in total

1. Charge effects on the fibril-forming peptide KTVIIE: a two-dimensional replica exchange simulation study.

Authors: Joohyun Jeon; M Scott Shell
Journal: Biophys J Date: 2012-04-18 Impact factor: 4.033

2. Electrostatic effects in filamentous protein aggregation.

Authors: Alexander K Buell; Peter Hung; Xavier Salvatella; Mark E Welland; Christopher M Dobson; Tuomas P J Knowles
Journal: Biophys J Date: 2013-03-05 Impact factor: 4.033

3. Autonomous aggregation suppression by acidic residues explains why chaperones favour basic residues.

Authors: Bert Houben; Emiel Michiels; Meine Ramakers; Katerina Konstantoulea; Nikolaos Louros; Joffré Verniers; Rob van der Kant; Matthias De Vleeschouwer; Nuno Chicória; Thomas Vanpoucke; Rodrigo Gallardo; Joost Schymkowitz; Frederic Rousseau
Journal: EMBO J Date: 2020-04-01 Impact factor: 11.598

4. Charge Shielding Prevents Aggregation of Supercharged GFP Variants at High Protein Concentration.

Authors: Joshua R Laber; Barton J Dear; Matheus L Martins; Devin E Jackson; Andrea DiVenere; Jimmy D Gollihar; Andrew D Ellington; Thomas M Truskett; Keith P Johnston; Jennifer A Maynard
Journal: Mol Pharm Date: 2017-09-18 Impact factor: 4.939

5. High-resolution MAS NMR analysis of PI3-SH3 amyloid fibrils: backbone conformation and implications for protofilament assembly and structure .

Authors: Marvin J Bayro; Thorsten Maly; Neil R Birkett; Cait E Macphee; Christopher M Dobson; Robert G Griffin
Journal: Biochemistry Date: 2010-09-07 Impact factor: 3.162

Position-dependent electrostatic protection against protein aggregation.

1. Charge effects on the fibril-forming peptide KTVIIE: a two-dimensional replica exchange simulation study.

2. Electrostatic effects in filamentous protein aggregation.

3. Autonomous aggregation suppression by acidic residues explains why chaperones favour basic residues.

4. Charge Shielding Prevents Aggregation of Supercharged GFP Variants at High Protein Concentration.

5. High-resolution MAS NMR analysis of PI3-SH3 amyloid fibrils: backbone conformation and implications for protofilament assembly and structure .

6. Interactions between amyloidophilic dyes and their relevance to studies of amyloid inhibitors.

Review 7. The ribosome as a hub for protein quality control.

8. Fibrillation precursor of superoxide dismutase 1 revealed by gradual tuning of the protein-folding equilibrium.

9. Role of elongation and secondary pathways in S6 amyloid fibril growth.

10. Population of nonnative states of lysozyme variants drives amyloid fibril formation.