| Year |
Citation |
Score |
| 2024 |
Lemke EA, Babu MM, Kriwacki RW, Mittag T, Pappu RV, Wright PE, Forman-Kay JD. Intrinsic disorder: A term to define the specific physicochemical characteristic of protein conformational heterogeneity. Molecular Cell. 84: 1188-1190. PMID 38579677 DOI: 10.1016/j.molcel.2024.02.024 |
0.559 |
|
| 2023 |
Pesce F, Bremer A, Tesei G, Hopkins JB, Grace CR, Mittag T, Lindorff-Larsen K. Design of intrinsically disordered protein variants with diverse structural properties. Biorxiv : the Preprint Server For Biology. PMID 37961110 DOI: 10.1101/2023.10.22.563461 |
0.373 |
|
| 2023 |
Thomasen FE, Cuneo MJ, Mittag T, Lindorff-Larsen K. Conformational and oligomeric states of SPOP from small-angle X-ray scattering and molecular dynamics simulations. Elife. 12. PMID 36856266 DOI: 10.7554/eLife.84147 |
0.314 |
|
| 2021 |
Usher ET, Sabri N, Rohac R, Boal AK, Mittag T, Showalter SA. Intrinsically disordered substrates dictate SPOP subnuclear localization and ubiquitination activity. The Journal of Biological Chemistry. 100693. PMID 33894201 DOI: 10.1016/j.jbc.2021.100693 |
0.359 |
|
| 2020 |
Lazar T, Martínez-Pérez E, Quaglia F, Hatos A, Chemes LB, Iserte JA, Méndez NA, Garrone NA, Saldaño TE, Marchetti J, Rueda AJV, Bernadó P, Blackledge M, Cordeiro TN, Fagerberg E, ... ... Mittag T, et al. PED in 2021: a major update of the protein ensemble database for intrinsically disordered proteins. Nucleic Acids Research. PMID 33305318 DOI: 10.1093/nar/gkaa1021 |
0.558 |
|
| 2020 |
Gomes GW, Krzeminski M, Namini A, Martin EW, Mittag T, Head-Gordon T, Forman-Kay JD, Gradinaru CC. Conformational ensembles of an intrinsically disordered protein consistent with NMR, SAXS and single-molecule FRET. Journal of the American Chemical Society. PMID 32840111 DOI: 10.1021/Jacs.0C02088 |
0.568 |
|
| 2018 |
Mittag T, Parker R. Multiple Modes of Protein-Protein Interactions Promote RNP Granule Assembly. Journal of Molecular Biology. PMID 30099026 DOI: 10.1016/J.Jmb.2018.08.005 |
0.324 |
|
| 2017 |
Csizmok V, Orlicky S, Cheng J, Song J, Bah A, Delgoshaie N, Lin H, Mittag T, Sicheri F, Chan HS, Tyers M, Forman-Kay JD. An allosteric conduit facilitates dynamic multisite substrate recognition by the SCF(Cdc4) ubiquitin ligase. Nature Communications. 8: 13943. PMID 28045046 DOI: 10.1038/Ncomms13943 |
0.536 |
|
| 2016 |
Martin EW, Holehouse AS, Grace CR, Hughes A, Pappu RV, Mittag T. Sequence determinants of the conformational properties of an intrinsically disordered protein prior to and upon multisite phosphorylation. Journal of the American Chemical Society. PMID 27807972 DOI: 10.1021/Jacs.6B10272 |
0.401 |
|
| 2015 |
Pierce WK, Grace CR, Lee J, Nourse A, Marzahn MR, Watson ER, High AA, Peng J, Schulman BA, Mittag T. Multiple weak linear motifs enhance recruitment and processivity in SPOP-mediated substrate ubiquitination. Journal of Molecular Biology. PMID 26475525 DOI: 10.1016/J.Jmb.2015.10.002 |
0.373 |
|
| 2015 |
Mittag T, Marzahn MR. Protein disorder: wagging a tail at ubiquitin. Nature Chemical Biology. 11: 7-8. PMID 25517385 DOI: 10.1038/Nchembio.1716 |
0.374 |
|
| 2013 |
Forman-Kay JD, Mittag T. From sequence and forces to structure, function, and evolution of intrinsically disordered proteins. Structure (London, England : 1993). 21: 1492-9. PMID 24010708 DOI: 10.1016/j.str.2013.08.001 |
0.584 |
|
| 2012 |
Tang X, Orlicky S, Mittag T, Csizmok V, Pawson T, Forman-Kay JD, Sicheri F, Tyers M. Composite low affinity interactions dictate recognition of the cyclin-dependent kinase inhibitor Sic1 by the SCF Cdc4 ubiquitin ligase Proceedings of the National Academy of Sciences of the United States of America. 109: 3287-3292. PMID 22328159 DOI: 10.1073/Pnas.1116455109 |
0.542 |
|
| 2010 |
Mittag T, Marsh J, Grishaev A, Orlicky S, Lin H, Sicheri F, Tyers M, Forman-Kay JD. Structure/Function Implications in a Dynamic Complex of the Intrinsically Disordered Sic1 with the Cdc4 Subunit of an SCF Ubiquitin Ligase Structure. 18: 494-506. PMID 20399186 DOI: 10.1016/J.Str.2010.01.020 |
0.644 |
|
| 2010 |
Mittag T, Kay LE, Forman-Kay JD. Protein dynamics and conformational disorder in molecular recognition. Journal of Molecular Recognition : Jmr. 23: 105-16. PMID 19585546 DOI: 10.1002/Jmr.961 |
0.647 |
|
| 2008 |
Mittag T, Orlicky S, Choy WY, Tang X, Lin H, Sicheri F, Kay LE, Tyers M, Forman-Kay JD. Dynamic equilibrium engagement of a polyvalent ligand with a single-site receptor. Proceedings of the National Academy of Sciences of the United States of America. 105: 17772-7. PMID 19008353 DOI: 10.1073/Pnas.0809222105 |
0.642 |
|
| 2007 |
Borg M, Mittag T, Pawson T, Tyers M, Forman-Kay JD, Chan HS. Polyelectrostatic interactions of disordered ligands suggest a physical basis for ultrasensitivity. Proceedings of the National Academy of Sciences of the United States of America. 104: 9650-5. PMID 17522259 DOI: 10.1073/Pnas.0702580104 |
0.602 |
|
| 2007 |
Mittag T, Forman-Kay JD. Atomic-level characterization of disordered protein ensembles. Current Opinion in Structural Biology. 17: 3-14. PMID 17250999 DOI: 10.1016/j.sbi.2007.01.009 |
0.616 |
|
| 2006 |
Mittag T, Franzoni L, Cavazzini D, Schaffhausen B, Rossi GL, Günther UL. Retinol modulates site-specific mobility of apo-cellular retinol-binding protein to promote ligand binding. Journal of the American Chemical Society. 128: 9844-8. PMID 16866541 DOI: 10.1021/Ja0616128 |
0.419 |
|
| 2006 |
Koglin A, Mofid MR, Löhr F, Schäfer B, Rogov VV, Blum MM, Mittag T, Marahiel MA, Bernhard F, Dötsch V. Conformational switches modulate protein interactions in peptide antibiotic synthetases Science. 312: 273-276. PMID 16614225 DOI: 10.1126/Science.1122928 |
0.319 |
|
| 2004 |
Mittag T, Schaffhausen B, Günther UL. Tracing kinetic intermediates during ligand binding. Journal of the American Chemical Society. 126: 9017-23. PMID 15264834 DOI: 10.1021/Ja0392519 |
0.376 |
|
| 2003 |
Mittag T, Schaffhausen B, Günther UL. Direct observation of protein-ligand interaction kinetics. Biochemistry. 42: 11128-36. PMID 14503863 DOI: 10.1021/Bi0347499 |
0.365 |
|
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