| Year |
Citation |
Score |
| 2024 |
Kc S, Nguyen KH, Nicholson V, Walgren A, Trent T, Gollub E, Romero-Perez PS, Holehouse AS, Sukenik S, Boothby TC. Disordered proteins interact with the chemical environment to tune their protective function during drying. Elife. 13. PMID 39560655 DOI: 10.7554/eLife.97231 |
0.528 |
|
| 2024 |
Usher ET, Fossat MJ, Holehouse AS. Phosphorylation of disordered proteins tunes local and global intramolecular interactions. Biophysical Journal. 123: 4082-4096. PMID 39539017 DOI: 10.1016/j.bpj.2024.10.021 |
0.329 |
|
| 2024 |
Cubuk J, Jeremias Incicco J, Hall KB, Holehouse AS, Stuchell-Brereton MD, Soranno A. The dimerization domain of SARS CoV 2 Nucleocapsid protein is partially disordered as a monomer and forms a high affinity dynamic complex. Biorxiv : the Preprint Server For Biology. PMID 39386676 DOI: 10.1101/2024.09.25.614883 |
0.48 |
|
| 2024 |
Shammas S, Heller G, Bah A, Filippidi E, Holehouse A, Yu M, Lautenschläger J. Ordering the disordered. Structure (London, England : 1993). 32: 1288-1293. PMID 39241759 DOI: 10.1016/j.str.2024.08.004 |
0.459 |
|
| 2024 |
Romero-Pérez PS, Moran HM, Horani A, Truong A, Manriquez-Sandoval E, Ramirez JF, Martinez A, Gollub E, Hunter K, Lotthammer JM, Emenecker RJ, Boothby TC, Holehouse AS, Fried SD, Sukenik S. Protein surface chemistry encodes an adaptive resistance to desiccation. Biorxiv : the Preprint Server For Biology. PMID 39131385 DOI: 10.1101/2024.07.28.604841 |
0.489 |
|
| 2024 |
Usher ET, Fossat MJ, Holehouse AS. Phosphorylation of disordered proteins tunes local and global intramolecular interactions. Biorxiv : the Preprint Server For Biology. PMID 38915510 DOI: 10.1101/2024.06.10.598315 |
0.32 |
|
| 2024 |
Ginell GM, Emenecker RJ, Lotthammer JM, Usher ET, Holehouse AS. Direct prediction of intermolecular interactions driven by disordered regions. Biorxiv : the Preprint Server For Biology. PMID 38895487 DOI: 10.1101/2024.06.03.597104 |
0.393 |
|
| 2024 |
Alston JJ, Soranno A, Holehouse AS. Conserved molecular recognition by an intrinsically disordered region in the absence of sequence conservation. Research Square. PMID 38883712 DOI: 10.21203/rs.3.rs-4477977/v1 |
0.367 |
|
| 2024 |
Jankowski MS, Griffith D, Shastry DG, Pelham JF, Ginell GM, Thomas J, Karande P, Holehouse AS, Hurley JM. Disordered clock protein interactions and charge blocks turn an hourglass into a persistent circadian oscillator. Nature Communications. 15: 3523. PMID 38664421 DOI: 10.1038/s41467-024-47761-z |
0.517 |
|
| 2024 |
Kc S, Nguyen K, Nicholson V, Walgren A, Trent T, Gollub E, Romero S, Holehouse AS, Sukenik S, Boothby TC. Disordered proteins interact with the chemical environment to tune their protective function during drying. Biorxiv : the Preprint Server For Biology. PMID 38464187 DOI: 10.1101/2024.02.28.582506 |
0.528 |
|
| 2024 |
Lotthammer JM, Ginell GM, Griffith D, Emenecker RJ, Holehouse AS. Direct prediction of intrinsically disordered protein conformational properties from sequences. Nature Methods. PMID 38297184 DOI: 10.1038/s41592-023-02159-5 |
0.306 |
|
| 2024 |
Moses D, Guadalupe K, Yu F, Flores E, Perez AR, McAnelly R, Shamoon NM, Kaur G, Cuevas-Zepeda E, Merg AD, Martin EW, Holehouse AS, Sukenik S. Structural biases in disordered proteins are prevalent in the cell. Nature Structural & Molecular Biology. PMID 38177684 DOI: 10.1038/s41594-023-01148-8 |
0.546 |
|
| 2023 |
Cubuk J, Alston JJ, Incicco JJ, Holehouse AS, Hall KB, Stuchell-Brereton MD, Soranno A. The disordered N-terminal tail of SARS-CoV-2 Nucleocapsid protein forms a dynamic complex with RNA. Nucleic Acids Research. PMID 38153183 DOI: 10.1093/nar/gkad1215 |
0.321 |
|
| 2023 |
Biswas S, Gollub E, Yu F, Ginell G, Holehouse A, Sukenik S, Boothby TC. Helicity of a tardigrade disordered protein contributes to its protective function during desiccation. Protein Science : a Publication of the Protein Society. e4872. PMID 38114424 DOI: 10.1002/pro.4872 |
0.582 |
|
| 2023 |
Holehouse A, Emenecker R, Guadalupe K, Shamoon N, Sukenik S. Sequence-ensemble-function relationships for disordered proteins in live cells. Research Square. PMID 37986812 DOI: 10.21203/rs.3.rs-3501110/v1 |
0.319 |
|
| 2023 |
Emenecker RJ, Guadalupe K, Shamoon NM, Sukenik S, Holehouse AS. Sequence-ensemble-function relationships for disordered proteins in live cells. Biorxiv : the Preprint Server For Biology. PMID 37961106 DOI: 10.1101/2023.10.29.564547 |
0.319 |
|
| 2023 |
Holehouse AS, Kragelund BB. The molecular basis for cellular function of intrinsically disordered protein regions. Nature Reviews. Molecular Cell Biology. 25: 187-211. PMID 37957331 DOI: 10.1038/s41580-023-00673-0 |
0.531 |
|
| 2023 |
Banerjee PR, Holehouse AS, Kriwacki R, Robustelli P, Jiang H, Sobolevsky AI, Hurley JM, Mendell JT. Dissecting the biophysics and biology of intrinsically disordered proteins. Trends in Biochemical Sciences. PMID 37949765 DOI: 10.1016/j.tibs.2023.10.002 |
0.388 |
|
| 2023 |
Moses D, Ginell GM, Holehouse AS, Sukenik S. Intrinsically disordered regions are poised to act as sensors of cellular chemistry. Trends in Biochemical Sciences. PMID 37657994 DOI: 10.1016/j.tibs.2023.08.001 |
0.53 |
|
| 2023 |
Alston JJ, Soranno A, Holehouse AS. Conserved molecular recognition by an intrinsically disordered region in the absence of sequence conservation. Biorxiv : the Preprint Server For Biology. PMID 37609146 DOI: 10.1101/2023.08.06.552128 |
0.358 |
|
| 2023 |
Lalmansingh JM, Keeley AT, Ruff KM, Pappu RV, Holehouse AS. SOURSOP: A Python Package for the Analysis of Simulations of Intrinsically Disordered Proteins. Journal of Chemical Theory and Computation. PMID 37463458 DOI: 10.1021/acs.jctc.3c00190 |
0.422 |
|
| 2023 |
Boeynaems S, Dorone Y, Zhuang Y, Shabardina V, Huang G, Marian A, Kim G, Sanyal A, Şen NE, Griffith D, Docampo R, Lasker K, Ruiz-Trillo I, Auburger G, Holehouse AS, et al. Poly(A)-binding protein is an ataxin-2 chaperone that regulates biomolecular condensates. Molecular Cell. PMID 37295429 DOI: 10.1016/j.molcel.2023.05.025 |
0.517 |
|
| 2023 |
Alston JJ, Ginell GM, Soranno A, Holehouse AS. The Analytical Flory Random Coil Is a Simple-to-Use Reference Model for Unfolded and Disordered Proteins. The Journal of Physical Chemistry. B. PMID 37200094 DOI: 10.1021/acs.jpcb.3c01619 |
0.359 |
|
| 2023 |
Jing H, Yang X, Emenecker RJ, Feng J, Zhang J, Figueiredo MRA, Chaisupa P, Wright RC, Holehouse AS, Strader LC, Zuo J. Nitric oxide-mediated S-nitrosylation of IAA17 protein in intrinsically disordered region represses auxin signaling. Journal of Genetics and Genomics = Yi Chuan Xue Bao. PMID 37187411 DOI: 10.1016/j.jgg.2023.05.001 |
0.415 |
|
| 2023 |
Alston JJ, Ginell GM, Soranno A, Holehouse AS. The analytical Flory random coil is a simple-to-use reference model for unfolded and disordered proteins. Biorxiv : the Preprint Server For Biology. PMID 36993592 DOI: 10.1101/2023.03.12.531990 |
0.359 |
|
| 2023 |
Lalmansingh JM, Keeley AT, Ruff KM, Pappu RV, Holehouse AS. SOURSOP: A Python package for the analysis of simulations of intrinsically disordered proteins. Biorxiv : the Preprint Server For Biology. PMID 36824878 DOI: 10.1101/2023.02.16.528879 |
0.407 |
|
| 2022 |
González-Foutel NS, Glavina J, Borcherds WM, Safranchik M, Barrera-Vilarmau S, Sagar A, Estaña A, Barozet A, Garrone NA, Fernandez-Ballester G, Blanes-Mira C, Sánchez IE, de Prat-Gay G, Cortés J, Bernadó P, ... ... Holehouse AS, et al. Conformational buffering underlies functional selection in intrinsically disordered protein regions. Nature Structural & Molecular Biology. 29: 781-790. PMID 35948766 DOI: 10.1038/s41594-022-00811-w |
0.566 |
|
| 2021 |
Holehouse AS, Ginell GM, Griffith D, Böke E. Clustering of Aromatic Residues in Prion-like Domains Can Tune the Formation, State, and Organization of Biomolecular Condensates. Biochemistry. 60: 3566-3581. PMID 34784177 DOI: 10.1021/acs.biochem.1c00465 |
0.324 |
|
| 2021 |
Taneja I, Holehouse AS. Folded domain charge properties influence the conformational behavior of disordered tails. Current Research in Structural Biology. 3: 216-228. PMID 34557680 DOI: 10.1016/j.crstbi.2021.08.002 |
0.322 |
|
| 2021 |
Emenecker RJ, Griffith D, Holehouse AS. Metapredict: a fast, accurate, and easy-to-use predictor of consensus disorder and structure. Biophysical Journal. PMID 34480923 DOI: 10.1016/j.bpj.2021.08.039 |
0.395 |
|
| 2021 |
Dorone Y, Boeynaems S, Flores E, Jin B, Hateley S, Bossi F, Lazarus E, Pennington JG, Michiels E, De Decker M, Vints K, Baatsen P, Bassel GW, Otegui MS, Holehouse AS, et al. A prion-like protein regulator of seed germination undergoes hydration-dependent phase separation. Cell. PMID 34233164 DOI: 10.1016/j.cell.2021.06.009 |
0.331 |
|
| 2021 |
Emenecker RJ, Holehouse AS, Strader LC. Sequence determinants of in cell condensate morphology, dynamics, and oligomerization as measured by number and brightness analysis. Cell Communication and Signaling : Ccs. 19: 65. PMID 34090478 DOI: 10.1186/s12964-021-00744-9 |
0.401 |
|
| 2021 |
Alston JJ, Soranno A, Holehouse AS. Integrating single-molecule spectroscopy and simulations for the study of intrinsically disordered proteins. Methods (San Diego, Calif.). PMID 33831596 DOI: 10.1016/j.ymeth.2021.03.018 |
0.448 |
|
| 2021 |
Cubuk J, Alston JJ, Incicco JJ, Singh S, Stuchell-Brereton MD, Ward MD, Zimmerman MI, Vithani N, Griffith D, Wagoner JA, Bowman GR, Hall KB, Soranno A, Holehouse AS. The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA. Nature Communications. 12: 1936. PMID 33782395 DOI: 10.1038/s41467-021-21953-3 |
0.402 |
|
| 2021 |
Davis ZH, Mediani L, Antoniani F, Vinet J, Li S, Alberti S, Lu B, Holehouse AS, Carra S, Brandman O. Protein products of nonstop mRNA disrupt nucleolar homeostasis. Cell Stress & Chaperones. PMID 33619693 DOI: 10.1007/s12192-021-01200-w |
0.381 |
|
| 2021 |
Ginell GM, Holehouse AS. Analyzing the Sequences of Intrinsically Disordered Regions with CIDER and localCIDER. Methods in Molecular Biology (Clifton, N.J.). 2141: 103-126. PMID 32696354 DOI: 10.1007/978-1-0716-0524-0_5 |
0.43 |
|
| 2020 |
Moses D, Yu F, Ginell GM, Shamoon NM, Koenig PS, Holehouse AS, Sukenik S. Revealing the Hidden Sensitivity of Intrinsically Disordered Proteins to their Chemical Environment. The Journal of Physical Chemistry Letters. 10131-10136. PMID 33191750 DOI: 10.1021/acs.jpclett.0c02822 |
0.497 |
|
| 2020 |
Martin EW, Holehouse AS. Intrinsically disordered protein regions and phase separation: sequence determinants of assembly or lack thereof. Emerging Topics in Life Sciences. PMID 33078839 DOI: 10.1042/ETLS20190164 |
0.327 |
|
| 2020 |
Stenzoski NE, Zou J, Piserchio A, Ghose R, Holehouse AS, Raleigh DP. The Cold-Unfolded State is Expanded but Contains Long- and Medium-range Contacts and Is Poorly Described by Homopolymer Models. Biochemistry. PMID 32786415 DOI: 10.1021/Acs.Biochem.0C00469 |
0.307 |
|
| 2020 |
Zeng X, Holehouse AS, Chilkoti A, Mittag T, Pappu RV. Connecting Coil-to-Globule Transitions to Full Phase Diagrams for Intrinsically Disordered Proteins. Biophysical Journal. PMID 32619404 DOI: 10.1016/J.Bpj.2020.06.014 |
0.323 |
|
| 2020 |
Cubuk J, Alston JJ, Incicco JJ, Singh S, Stuchell-Brereton MD, Ward MD, Zimmerman MI, Vithani N, Griffith D, Wagoner JA, Bowman GR, Hall KB, Soranno A, Holehouse AS. The SARS-CoV-2 nucleocapsid protein is dynamic, disordered, and phase separates with RNA. Biorxiv : the Preprint Server For Biology. PMID 32587966 DOI: 10.1101/2020.06.17.158121 |
0.433 |
|
| 2020 |
Holehouse AS, Sukenik S. Controlling Structural Bias in Intrinsically Disordered Proteins Using Solution Space Scanning. Journal of Chemical Theory and Computation. 16: 1794-1805. PMID 31999450 DOI: 10.1021/acs.jctc.9b00604 |
0.426 |
|
| 2019 |
Powers SK, Holehouse AS, Korasick DA, Schreiber KH, Clark NM, Jing H, Emenecker R, Han S, Tycksen E, Hwang I, Sozzani R, Jez JM, Pappu RV, Strader LC. Nucleo-cytoplasmic Partitioning of ARF Proteins Controls Auxin Responses in Arabidopsis thaliana. Molecular Cell. PMID 31421981 DOI: 10.1016/J.Molcel.2019.06.044 |
0.401 |
|
| 2019 |
Harding RJ, Loppnau P, Ackloo S, Lemak A, Hutchinson A, Hunt B, Holehouse AS, Ho JC, Fan L, Toledo-Sherman L, Seitova A, Arrowsmith CH. Design and characterization of mutant and wild-type huntingtin proteins produced from a toolkit of scalable eukaryotic expression systems. The Journal of Biological Chemistry. PMID 30842263 DOI: 10.1074/jbc.RA118.007204 |
0.428 |
|
| 2018 |
Posey AE, Holehouse AS, Pappu RV. Phase Separation of Intrinsically Disordered Proteins. Methods in Enzymology. 611: 1-30. PMID 30471685 DOI: 10.1016/Bs.Mie.2018.09.035 |
0.451 |
|
| 2018 |
Ruff KM, Pappu RV, Holehouse AS. Conformational preferences and phase behavior of intrinsically disordered low complexity sequences: insights from multiscale simulations. Current Opinion in Structural Biology. 56: 1-10. PMID 30439585 DOI: 10.1016/J.Sbi.2018.10.003 |
0.423 |
|
| 2018 |
Staller MV, Holehouse AS, Swain-Lenz D, Das RK, Pappu RV, Cohen BA. A High-Throughput Mutational Scan of an Intrinsically Disordered Acidic Transcriptional Activation Domain. Cell Systems. PMID 29525204 DOI: 10.1016/J.Cels.2018.01.015 |
0.312 |
|
| 2018 |
Holehouse AS, Pappu RV. Collapse Transitions of Proteins and the Interplay Among Backbone, Sidechain, and Solvent Interactions. Annual Review of Biophysics. PMID 29345991 DOI: 10.1146/Annurev-Biophys-070317-032838 |
0.537 |
|
| 2018 |
Franzmann TM, Jahnel M, Pozniakovsky A, Mahamid J, Holehouse AS, Nüske E, Richter D, Baumeister W, Grill SW, Pappu RV, Hyman AA, Alberti S. Phase separation of a yeast prion protein promotes cellular fitness. Science (New York, N.Y.). 359. PMID 29301985 DOI: 10.1126/Science.Aao5654 |
0.302 |
|
| 2017 |
Harmon TS, Holehouse AS, Rosen MK, Pappu RV. Intrinsically disordered linkers determine the interplay between phase separation and gelation in multivalent proteins. Elife. 6. PMID 29091028 DOI: 10.7554/Elife.30294 |
0.416 |
|
| 2017 |
Wei MT, Elbaum-Garfinkle S, Holehouse AS, Chen CC, Feric M, Arnold CB, Priestley RD, Pappu RV, Brangwynne CP. Phase behaviour of disordered proteins underlying low density and high permeability of liquid organelles. Nature Chemistry. 9: 1118-1125. PMID 29064502 DOI: 10.1038/Nchem.2803 |
0.481 |
|
| 2017 |
Holehouse AS, Das RK, Ahad JN, Richardson MO, Pappu RV. CIDER: Resources to Analyze Sequence-Ensemble Relationships of Intrinsically Disordered Proteins. Biophysical Journal. 112: 16-21. PMID 28076807 DOI: 10.1016/J.Bpj.2016.11.3200 |
0.39 |
|
| 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 |
0.323 |
|
| 2016 |
Pak CW, Kosno M, Holehouse AS, Padrick SB, Mittal A, Ali R, Yunus AA, Liu DR, Pappu RV, Rosen MK. Sequence Determinants of Intracellular Phase Separation by Complex Coacervation of a Disordered Protein. Molecular Cell. 63: 72-85. PMID 27392146 DOI: 10.1016/J.Molcel.2016.05.042 |
0.405 |
|
| 2015 |
Holehouse AS, Naegle KM. Reproducible Analysis of Post-Translational Modifications in Proteomes--Application to Human Mutations. Plos One. 10: e0144692. PMID 26659599 DOI: 10.1371/journal.pone.0144692 |
0.369 |
|
| 2015 |
Holehouse AS, Pappu RV. Protein polymers: Encoding phase transitions. Nature Materials. 14: 1083-4. PMID 26490213 DOI: 10.1038/Nmat4459 |
0.344 |
|
| 2015 |
Holehouse AS, Garai K, Lyle N, Vitalis A, Pappu RV. Quantitative assessments of the distinct contributions of polypeptide backbone amides versus side chain groups to chain expansion via chemical denaturation. Journal of the American Chemical Society. 137: 2984-95. PMID 25664638 DOI: 10.1021/Ja512062H |
0.342 |
|
| 2014 |
Matlock MK, Holehouse AS, Naegle KM. ProteomeScout: a repository and analysis resource for post-translational modifications and proteins. Nucleic Acids Research. 43: D521-30. PMID 25414335 DOI: 10.1093/nar/gku1154 |
0.455 |
|
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