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Literature DB >> 31606122

Competing Ligands Can Both Obstruct and Enhance Protein-Complex Formation.

Gideon Schreiber¹.

Abstract

Year: 2019 PMID： 31606122 PMCID： PMC6839003 DOI： 10.1016/j.bpj.2019.09.036

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

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10 in total

Review 1. Formation of transient protein complexes.

Authors: Jesika Schilder; Marcellus Ubbink
Journal: Curr Opin Struct Biol Date: 2013-08-07 Impact factor: 6.809

2. Physicochemical code for quinary protein interactions in Escherichia coli.

Authors: Xin Mu; Seongil Choi; Lisa Lang; David Mowray; Nikolay V Dokholyan; Jens Danielsson; Mikael Oliveberg
Journal: Proc Natl Acad Sci U S A Date: 2017-05-23 Impact factor: 11.205

Review 3. The bacterial phosphoenolpyruvate:carbohydrate phosphotransferase system: regulation by protein phosphorylation and phosphorylation-dependent protein-protein interactions.

Authors: Josef Deutscher; Francine Moussan Désirée Aké; Meriem Derkaoui; Arthur Constant Zébré; Thanh Nguyen Cao; Houda Bouraoui; Takfarinas Kentache; Abdelhamid Mokhtari; Eliane Milohanic; Philippe Joyet
Journal: Microbiol Mol Biol Rev Date: 2014-06 Impact factor: 11.056

4. Information capacity of specific interactions.

Authors: Miriam H Huntley; Arvind Murugan; Michael P Brenner
Journal: Proc Natl Acad Sci U S A Date: 2016-05-06 Impact factor: 11.205

Review 5. Structure, dynamics and biophysics of the cytoplasmic protein-protein complexes of the bacterial phosphoenolpyruvate: sugar phosphotransferase system.

Authors: G Marius Clore; Vincenzo Venditti
Journal: Trends Biochem Sci Date: 2013-09-19 Impact factor: 13.807

Competing Ligands Can Both Obstruct and Enhance Protein-Complex Formation.

Review 1. Formation of transient protein complexes.

2. Physicochemical code for quinary protein interactions in Escherichia coli.

Review 3. The bacterial phosphoenolpyruvate:carbohydrate phosphotransferase system: regulation by protein phosphorylation and phosphorylation-dependent protein-protein interactions.

4. Information capacity of specific interactions.

Review 5. Structure, dynamics and biophysics of the cytoplasmic protein-protein complexes of the bacterial phosphoenolpyruvate: sugar phosphotransferase system.

6. Promiscuous Protein Binding as a Function of Protein Stability.

7. Model of a Kinetically Driven Crosstalk between Paralogous Protein Encounter Complexes.

8. Potential Regulatory Role of Competitive Encounter Complexes in Paralogous Phosphotransferase Systems.

Review 9. Fundamental aspects of protein-protein association kinetics.

10. Transient protein-protein interactions perturb E. coli metabolome and cause gene dosage toxicity.