Holehouse AS - Search Results

1

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

Holehouse AS, Naegle KM. Holehouse AS, et al. PLoS One. 2015 Dec 14;10(12):e0144692. doi: 10.1371/journal.pone.0144692. eCollection 2015. PLoS One. 2015. PMID: 26659599 Free PMC article.

2

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

Matlock MK, Holehouse AS, Naegle KM. Matlock MK, et al. Among authors: holehouse as. Nucleic Acids Res. 2015 Jan;43(Database issue):D521-30. doi: 10.1093/nar/gku1154. Epub 2014 Nov 20. Nucleic Acids Res. 2015. PMID: 25414335 Free PMC article.

3

Protein polymers: Encoding phase transitions.

Holehouse AS, Pappu RV. Holehouse AS, et al. Nat Mater. 2015 Nov;14(11):1083-4. doi: 10.1038/nmat4459. Nat Mater. 2015. PMID: 26490213 No abstract available.

4

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. Harding RJ, et al. Among authors: holehouse as. J Biol Chem. 2019 Apr 26;294(17):6986-7001. doi: 10.1074/jbc.RA118.007204. Epub 2019 Mar 6. J Biol Chem. 2019. PMID: 30842263 Free PMC article.

5

Investigating the ferric ion binding site of magnetite biomineralisation protein Mms6.

Rawlings AE, Liravi P, Corbett S, Holehouse AS, Staniland SS. Rawlings AE, et al. Among authors: holehouse as. PLoS One. 2020 Feb 25;15(2):e0228708. doi: 10.1371/journal.pone.0228708. eCollection 2020. PLoS One. 2020. PMID: 32097412 Free PMC article.

6

Analyzing the Sequences of Intrinsically Disordered Regions with CIDER and localCIDER.

Ginell GM, Holehouse AS. Ginell GM, et al. Among authors: holehouse as. Methods Mol Biol. 2020;2141:103-126. doi: 10.1007/978-1-0716-0524-0_5. Methods Mol Biol. 2020. PMID: 32696354

7

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. Pak CW, et al. Among authors: holehouse as. Mol Cell. 2016 Jul 7;63(1):72-85. doi: 10.1016/j.molcel.2016.05.042. Mol Cell. 2016. PMID: 27392146 Free PMC article.

8

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. Martin EW, et al. Among authors: holehouse as. J Am Chem Soc. 2016 Nov 30;138(47):15323-15335. doi: 10.1021/jacs.6b10272. Epub 2016 Nov 17. J Am Chem Soc. 2016. PMID: 27807972 Free PMC article.

9

PARROT is a flexible recurrent neural network framework for analysis of large protein datasets.

Griffith D, Holehouse AS. Griffith D, et al. Among authors: holehouse as. Elife. 2021 Sep 17;10:e70576. doi: 10.7554/eLife.70576. Elife. 2021. PMID: 34533455 Free PMC article.

10

Directed mutational scanning reveals a balance between acidic and hydrophobic residues in strong human activation domains.

Staller MV, Ramirez E, Kotha SR, Holehouse AS, Pappu RV, Cohen BA. Staller MV, et al. Among authors: holehouse as. Cell Syst. 2022 Apr 20;13(4):334-345.e5. doi: 10.1016/j.cels.2022.01.002. Epub 2022 Feb 3. Cell Syst. 2022. PMID: 35120642 Free PMC article.

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