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Modulation of Intrinsically Disordered Protein Function by Post-translational Modifications
| Content Provider | Scilit |
|---|---|
| Author | Bah, Alaji Forman-Kay, Julie D. |
| Copyright Year | 2016 |
| Description | Journal: Journal of Biological Chemistry Post-translational modifications (PTMs) produce significant changes in the structural properties of intrinsically disordered proteins (IDPs) by affecting their energy landscapes. PTMs can induce a range of effects, from local stabilization or destabilization of transient secondary structure to global disorder-to-order transitions, potentially driving complete state changes between intrinsically disordered and folded states or dispersed monomeric and phase-separated states. Here, we discuss diverse biological processes that are dependent on PTM regulation of IDPs. We also present recent tools for generating homogenously modified IDPs for studies of PTM-mediated IDP regulatory mechanisms. |
| Related Links | http://www.jbc.org/content/291/13/6696.full.pdf https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4807257/pdf http://www.jbc.org/article/S0021925820429278/pdf |
| Ending Page | 6705 |
| Page Count | 10 |
| Starting Page | 6696 |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| DOI | 10.1074/jbc.r115.695056 |
| Journal | Journal of Biological Chemistry |
| Issue Number | 13 |
| Volume Number | 291 |
| Language | English |
| Publisher | Elsevier BV |
| Publisher Date | 2016-03-01 |
| Access Restriction | Open |
| Subject Keyword | Journal: Journal of Biological Chemistry Cell Biology Intrinsically Disordered Protein Post-translational Modification (ptm) Protein Conformation Protein-dna Interaction Protein-protein Interaction |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
