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Literature DB >> 33951452

Can sequence-specific and dynamics-based metrics allow us to decipher the function in IDP sequences?

S Banu Ozkan¹.

Abstract

Entities: Chemical

Mesh：

Substances：

Year: 2021 PMID： 33951452 PMCID： PMC8204289 DOI： 10.1016/j.bpj.2021.04.008

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

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19 in total

1. Modulating charge patterning and ionic strength as a strategy to induce conformational changes in intrinsically disordered proteins.

Authors: Jonathan Huihui; Taylor Firman; Kingshuk Ghosh
Journal: J Chem Phys Date: 2018-08-28 Impact factor: 3.488

Review 2. Binding without folding - the biomolecular function of disordered polyelectrolyte complexes.

Authors: Benjamin Schuler; Alessandro Borgia; Madeleine B Borgia; Pétur O Heidarsson; Erik D Holmstrom; Daniel Nettels; Andrea Sottini
Journal: Curr Opin Struct Biol Date: 2019-12-23 Impact factor: 6.809

3. An analytical theory to describe sequence-specific inter-residue distance profiles for polyampholytes and intrinsically disordered proteins.

Authors: Jonathan Huihui; Kingshuk Ghosh
Journal: J Chem Phys Date: 2020-04-30 Impact factor: 3.488

4. A core subunit of Polycomb repressive complex 1 is broadly conserved in function but not primary sequence.

Authors: Leslie Y Beh; Lucy J Colwell; Nicole J Francis
Journal: Proc Natl Acad Sci U S A Date: 2012-04-18 Impact factor: 11.205

5. Control of transcriptional activity by design of charge patterning in the intrinsically disordered RAM region of the Notch receptor.

Authors: Kathryn P Sherry; Rahul K Das; Rohit V Pappu; Doug Barrick
Journal: Proc Natl Acad Sci U S A Date: 2017-10-12 Impact factor: 11.205

Can sequence-specific and dynamics-based metrics allow us to decipher the function in IDP sequences?

1. Modulating charge patterning and ionic strength as a strategy to induce conformational changes in intrinsically disordered proteins.

Review 2. Binding without folding - the biomolecular function of disordered polyelectrolyte complexes.

3. An analytical theory to describe sequence-specific inter-residue distance profiles for polyampholytes and intrinsically disordered proteins.

4. A core subunit of Polycomb repressive complex 1 is broadly conserved in function but not primary sequence.

5. Control of transcriptional activity by design of charge patterning in the intrinsically disordered RAM region of the Notch receptor.

6. Comparison and Evaluation of Force Fields for Intrinsically Disordered Proteins.

7. Intrachain interaction topology can identify functionally similar intrinsically disordered proteins.

8. Emergence and evolution of an interaction between intrinsically disordered proteins.

9. Proteome-wide signatures of function in highly diverged intrinsically disordered regions.

10. Information theoretic measures for quantifying sequence-ensemble relationships of intrinsically disordered proteins.

Review 1. Rules of Physical Mathematics Govern Intrinsically Disordered Proteins.