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Items: 28

1.

Unfolded states under folding conditions accommodate sequence-specific conformational preferences with random coil-like dimensions.

Peran I, Holehouse AS, Carrico IS, Pappu RV, Bilsel O, Raleigh DP.

Proc Natl Acad Sci U S A. 2019 Jun 5. pii: 201818206. doi: 10.1073/pnas.1818206116. [Epub ahead of print]

2.

Spontaneous driving forces give rise to protein-RNA condensates with coexisting phases and complex material properties.

Boeynaems S, Holehouse AS, Weinhardt V, Kovacs D, Van Lindt J, Larabell C, Van Den Bosch L, Das R, Tompa PS, Pappu RV, Gitler AD.

Proc Natl Acad Sci U S A. 2019 Apr 16;116(16):7889-7898. doi: 10.1073/pnas.1821038116. Epub 2019 Mar 29.

3.

Design and characterization of mutant and wildtype huntingtin proteins produced from a toolkit of scalable eukaryotic expression systems.

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.

J Biol Chem. 2019 Apr 26;294(17):6986-7001. doi: 10.1074/jbc.RA118.007204. Epub 2019 Mar 6.

PMID:
30842263
4.

Phase Separation of Intrinsically Disordered Proteins.

Posey AE, Holehouse AS, Pappu RV.

Methods Enzymol. 2018;611:1-30. doi: 10.1016/bs.mie.2018.09.035. Epub 2018 Oct 31.

PMID:
30471685
5.

Conformational preferences and phase behavior of intrinsically disordered low complexity sequences: insights from multiscale simulations.

Ruff KM, Pappu RV, Holehouse AS.

Curr Opin Struct Biol. 2018 Nov 12;56:1-10. doi: 10.1016/j.sbi.2018.10.003. [Epub ahead of print] Review.

PMID:
30439585
6.

Transcription factor dimerization activates the p300 acetyltransferase.

Ortega E, Rengachari S, Ibrahim Z, Hoghoughi N, Gaucher J, Holehouse AS, Khochbin S, Panne D.

Nature. 2018 Oct;562(7728):538-544. doi: 10.1038/s41586-018-0621-1. Epub 2018 Oct 15.

PMID:
30323286
7.

The Unfolded State of the C-Terminal Domain of L9 Expands at Low but Not at Elevated Temperatures.

Stenzoski NE, Luan B, Holehouse AS, Raleigh DP.

Biophys J. 2018 Aug 21;115(4):655-663. doi: 10.1016/j.bpj.2018.07.013. Epub 2018 Jul 23.

8.

A Molecular Grammar Governing the Driving Forces for Phase Separation of Prion-like RNA Binding Proteins.

Wang J, Choi JM, Holehouse AS, Lee HO, Zhang X, Jahnel M, Maharana S, Lemaitre R, Pozniakovsky A, Drechsel D, Poser I, Pappu RV, Alberti S, Hyman AA.

Cell. 2018 Jul 26;174(3):688-699.e16. doi: 10.1016/j.cell.2018.06.006. Epub 2018 Jun 28.

PMID:
29961577
9.

Sequence-to-Conformation Relationships of Disordered Regions Tethered to Folded Domains of Proteins.

Mittal A, Holehouse AS, Cohan MC, Pappu RV.

J Mol Biol. 2018 Aug 3;430(16):2403-2421. doi: 10.1016/j.jmb.2018.05.012. Epub 2018 May 12.

10.

A High-Throughput Mutational Scan of an Intrinsically Disordered Acidic Transcriptional Activation Domain.

Staller MV, Holehouse AS, Swain-Lenz D, Das RK, Pappu RV, Cohen BA.

Cell Syst. 2018 Apr 25;6(4):444-455.e6. doi: 10.1016/j.cels.2018.01.015. Epub 2018 Mar 7.

11.

Collapse Transitions of Proteins and the Interplay Among Backbone, Sidechain, and Solvent Interactions.

Holehouse AS, Pappu RV.

Annu Rev Biophys. 2018 Jan 18. doi: 10.1146/annurev-biophys-070317-032838. [Epub ahead of print]

PMID:
29345991
12.

Functional Implications of Intracellular Phase Transitions.

Holehouse AS, Pappu RV.

Biochemistry. 2018 May 1;57(17):2415-2423. doi: 10.1021/acs.biochem.7b01136. Epub 2018 Jan 24.

13.

Phase separation of a yeast prion protein promotes cellular fitness.

Franzmann TM, Jahnel M, Pozniakovsky A, Mahamid J, Holehouse AS, Nüske E, Richter D, Baumeister W, Grill SW, Pappu RV, Hyman AA, Alberti S.

Science. 2018 Jan 5;359(6371). pii: eaao5654. doi: 10.1126/science.aao5654.

PMID:
29301985
14.

Quantitative analysis of multilayer organization of proteins and RNA in nuclear speckles at super resolution.

Fei J, Jadaliha M, Harmon TS, Li ITS, Hua B, Hao Q, Holehouse AS, Reyer M, Sun Q, Freier SM, Pappu RV, Prasanth KV, Ha T.

J Cell Sci. 2017 Dec 15;130(24):4180-4192. doi: 10.1242/jcs.206854. Epub 2017 Nov 13.

15.

Intrinsically disordered linkers determine the interplay between phase separation and gelation in multivalent proteins.

Harmon TS, Holehouse AS, Rosen MK, Pappu RV.

Elife. 2017 Nov 1;6. pii: e30294. doi: 10.7554/eLife.30294.

16.

Phase behaviour of disordered proteins underlying low density and high permeability of liquid organelles.

Wei MT, Elbaum-Garfinkle S, Holehouse AS, Chen CC, Feric M, Arnold CB, Priestley RD, Pappu RV, Brangwynne CP.

Nat Chem. 2017 Nov;9(11):1118-1125. doi: 10.1038/nchem.2803. Epub 2017 Jun 26.

PMID:
29064502
17.

FUS Zigzags Its Way to Cross Beta.

Holehouse AS, Pappu RV.

Cell. 2017 Oct 19;171(3):499-500. doi: 10.1016/j.cell.2017.10.007.

18.

SAXS versus FRET: A Matter of Heterogeneity?

Ruff KM, Holehouse AS.

Biophys J. 2017 Sep 5;113(5):971-973. doi: 10.1016/j.bpj.2017.07.024. Epub 2017 Aug 15. No abstract available.

19.

To Mix, or To Demix, That Is the Question.

Harmon TS, Holehouse AS, Pappu RV.

Biophys J. 2017 Feb 28;112(4):565-567. doi: 10.1016/j.bpj.2016.12.031. No abstract available.

20.

Evolutionary fine-tuning of conformational ensembles in FimH during host-pathogen interactions.

Kalas V, Pinkner JS, Hannan TJ, Hibbing ME, Dodson KW, Holehouse AS, Zhang H, Tolia NH, Gross ML, Pappu RV, Janetka J, Hultgren SJ.

Sci Adv. 2017 Feb 10;3(2):e1601944. doi: 10.1126/sciadv.1601944. eCollection 2017 Feb.

21.

CIDER: Resources to Analyze Sequence-Ensemble Relationships of Intrinsically Disordered Proteins.

Holehouse AS, Das RK, Ahad JN, Richardson MO, Pappu RV.

Biophys J. 2017 Jan 10;112(1):16-21. doi: 10.1016/j.bpj.2016.11.3200.

22.

Sequence Determinants of the Conformational Properties of an Intrinsically Disordered Protein Prior to and upon Multisite Phosphorylation.

Martin EW, Holehouse AS, Grace CR, Hughes A, Pappu RV, Mittag T.

J Am Chem Soc. 2016 Nov 30;138(47):15323-15335. Epub 2016 Nov 17.

23.

Sequence Determinants of Intracellular Phase Separation by Complex Coacervation of a Disordered Protein.

Pak CW, Kosno M, Holehouse AS, Padrick SB, Mittal A, Ali R, Yunus AA, Liu DR, Pappu RV, Rosen MK.

Mol Cell. 2016 Jul 7;63(1):72-85. doi: 10.1016/j.molcel.2016.05.042.

24.

Reproducible Analysis of Post-Translational Modifications in Proteomes--Application to Human Mutations.

Holehouse AS, Naegle KM.

PLoS One. 2015 Dec 14;10(12):e0144692. doi: 10.1371/journal.pone.0144692. eCollection 2015.

25.

Protein polymers: Encoding phase transitions.

Holehouse AS, Pappu RV.

Nat Mater. 2015 Nov;14(11):1083-4. doi: 10.1038/nmat4459. No abstract available.

PMID:
26490213
26.

OSCAR is a receptor for surfactant protein D that activates TNF-α release from human CCR2+ inflammatory monocytes.

Barrow AD, Palarasah Y, Bugatti M, Holehouse AS, Byers DE, Holtzman MJ, Vermi W, Skjødt K, Crouch E, Colonna M.

J Immunol. 2015 Apr 1;194(7):3317-26. doi: 10.4049/jimmunol.1402289. Epub 2015 Feb 25.

27.

Quantitative assessments of the distinct contributions of polypeptide backbone amides versus side chain groups to chain expansion via chemical denaturation.

Holehouse AS, Garai K, Lyle N, Vitalis A, Pappu RV.

J Am Chem Soc. 2015 Mar 4;137(8):2984-95. doi: 10.1021/ja512062h. Epub 2015 Feb 23.

28.

ProteomeScout: a repository and analysis resource for post-translational modifications and proteins.

Matlock MK, Holehouse AS, Naegle KM.

Nucleic Acids Res. 2015 Jan;43(Database issue):D521-30. doi: 10.1093/nar/gku1154. Epub 2014 Nov 20.

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