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Literature DB >> 29395045

Effect of Grafting on Aggregation of Intrinsically Disordered Proteins.

Abstract

A significant part of the proteome is composed of intrinsically disordered proteins (IDPs). These proteins do not fold into a well-defined structure and behave like ordinary polymers. In this work, we consider IDPs that have the tendency to aggregate, model them as heteropolymers that contain a small number of associating monomers, and use computer simulations to compare the aggregation of such IDPs that are grafted to a surface or free in solution. We then discuss how such grafting may affect the analysis of in vitro experiments and could also be used to suppress harmful aggregation.

Entities: Chemical Disease

Mesh：

Substances：

Year: 2018 PMID： 29395045 PMCID： PMC5985032 DOI： 10.1016/j.bpj.2017.08.062

Source DB: PubMed Journal: Biophys J ISSN： 0006-3495 Impact factor: 4.033

20 in total

Review 1. Principles of protein folding, misfolding and aggregation.

Authors: Christopher M Dobson
Journal: Semin Cell Dev Biol Date: 2004-02 Impact factor: 7.727

Review 2. Converging on the function of intrinsically disordered nucleoporins in the nuclear pore complex.

Authors: Orit Peleg; Roderick Y H Lim
Journal: Biol Chem Date: 2010-07 Impact factor: 3.915

3. Binding dynamics of isolated nucleoporin repeat regions to importin-beta.

Authors: Timothy A Isgro; Klaus Schulten
Journal: Structure Date: 2005-12 Impact factor: 5.006

4. Neurofilament sidearms modulate parallel and crossed-filament orientations inducing nematic to isotropic and re-entrant birefringent hydrogels.

Authors: Joanna Deek; Peter J Chung; Jona Kayser; Andreas R Bausch; Cyrus R Safinya
Journal: Nat Commun Date: 2013 Impact factor: 14.919

5. Facilitated aggregation of FG nucleoporins under molecular crowding conditions.

Authors: Sigrid Milles; Khanh Huy Bui; Christine Koehler; Mikhail Eltsov; Martin Beck; Edward A Lemke
Journal: EMBO Rep Date: 2012-12-14 Impact factor: 8.807

Review 6. Structures and interactions in 'bottlebrush' neurofilaments: the role of charged disordered proteins in forming hydrogel networks.

Authors: Roy Beck; Joanna Deek; Cyrus R Safinya
Journal: Biochem Soc Trans Date: 2012-10 Impact factor: 5.407

7. Effect of charge, hydrophobicity, and sequence of nucleoporins on the translocation of model particles through the nuclear pore complex.

Authors: Mario Tagliazucchi; Orit Peleg; Martin Kröger; Yitzhak Rabin; Igal Szleifer
Journal: Proc Natl Acad Sci U S A Date: 2013-02-12 Impact factor: 11.205

Effect of Grafting on Aggregation of Intrinsically Disordered Proteins.

Review 1. Principles of protein folding, misfolding and aggregation.

Review 2. Converging on the function of intrinsically disordered nucleoporins in the nuclear pore complex.

3. Binding dynamics of isolated nucleoporin repeat regions to importin-beta.

4. Neurofilament sidearms modulate parallel and crossed-filament orientations inducing nematic to isotropic and re-entrant birefringent hydrogels.

5. Facilitated aggregation of FG nucleoporins under molecular crowding conditions.

Review 6. Structures and interactions in 'bottlebrush' neurofilaments: the role of charged disordered proteins in forming hydrogel networks.

7. Effect of charge, hydrophobicity, and sequence of nucleoporins on the translocation of model particles through the nuclear pore complex.

8. Super-resolution 3D tomography of interactions and competition in the nuclear pore complex.

9. Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded.

Review 10. Neurofilaments and neurological disease.

1. Physical modeling of multivalent interactions in the nuclear pore complex.

2. Sequence effects on internal structure of droplets of associative polymers.