Publications

A Protein Semisynthesis-Based Strategy to Investigate the Functional Impact of Linker Histone Serine ADP-Ribosylation.

Tashiro K, Mohapatra J, Brautigam CA, Liszczak G, 2022 Mar ACS Chem Biol

Mutations linked to neurological disease enhance self-association of low-complexity protein sequences.

Zhou X, Sumrow L, Tashiro K, Sutherland L, Liu D, Qin T, Kato M, Liszczak G, McKnight SL, 2022 Jul Science 6601 377 eabn5582

Transiently structured head domains control intermediate filament assembly.

Zhou X, Lin Y, Kato M, Mori E, Liszczak G, Sutherland L, Sysoev VO, Murray DT, Tycko R, McKnight SL, 2021 Feb Proc Natl Acad Sci U S A 8 118

Serine ADP-ribosylation marks nucleosomes for ALC1-dependent chromatin remodeling.

Mohapatra J, Tashiro K, Beckner RL, Sierra J, Kilgore JA, Williams NS, Liszczak G, 2021 Dec Elife 10

Acetylation blocks DNA damage-induced chromatin ADP-ribosylation.

Liszczak G, Diehl KL, Dann GP, Muir TW 2018 Sep Nat. Chem. Biol. 9 14 837-840

Genomic targeting of epigenetic probes using a chemically tailored Cas9 system.

Liszczak GP, Brown ZZ, Kim SH, Oslund RC, David Y, Muir TW 2017 Jan Proc. Natl. Acad. Sci. U.S.A. 4 114 681-686

ISWI chromatin remodellers sense nucleosome modifications to determine substrate preference.

Dann GP, Liszczak GP, Bagert JD, Müller MM, Nguyen UTT, Wojcik F, Brown ZZ, Bos J, Panchenko T, Pihl R, Pollock SB, Diehl KL, Allis CD, Muir TW 2017 08 Nature 7669 548 607-611

A two-state activation mechanism controls the histone methyltransferase Suv39h1.

Müller MM, Fierz B, Bittova L, Liszczak G, Muir TW 2016 Mar Nat. Chem. Biol. 3 12 188-93

Molecular Basis for Cohesin Acetylation by Establishment of Sister Chromatid Cohesion N-Acetyltransferase ESCO1.

Rivera-Colón Y, Maguire A, Liszczak GP, Olia AS, Marmorstein R 2016 Dec J. Biol. Chem. 51 291 26468-26477

The molecular basis for histone H4- and H2A-specific amino-terminal acetylation by NatD.

Magin RS, Liszczak GP, Marmorstein R 2015 Feb Structure 2 23 332-41

Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-acetylation defects.

Myklebust LM, Van Damme P, Støve SI, Dörfel MJ, Abboud A, Kalvik TV, Grauffel C, Jonckheere V, Wu Y, Swensen J, Kaasa H, Liszczak G, Marmorstein R, Reuter N, Lyon GJ, Gevaert K, Arnesen T 2015 Apr Hum. Mol. Genet. 7 24 1956-76

Implications for the evolution of eukaryotic amino-terminal acetyltransferase (NAT) enzymes from the structure of an archaeal ortholog.

Liszczak G, Marmorstein R 2013 Sep Proc. Natl. Acad. Sci. U.S.A. 36 110 14652-7

Molecular basis for N-terminal acetylation by the heterodimeric NatA complex.

Liszczak G, Goldberg JM, Foyn H, Petersson EJ, Arnesen T, Marmorstein R 2013 Sep Nat. Struct. Mol. Biol. 9 20 1098-105

Specificity and versatility of substrate binding sites in four catalytic domains of human N-terminal acetyltransferases.

Grauffel C, Abboud A, Liszczak G, Marmorstein R, Arnesen T, Reuter N 2012 PLoS ONE 12 7 e52642

Structure of a ternary Naa50p (NAT5/SAN) N-terminal acetyltransferase complex reveals the molecular basis for substrate-specific acetylation.

Liszczak G, Arnesen T, Marmorstein R 2011 Oct J. Biol. Chem. 42 286 37002-10

Virtual ligand screening of the p300/CBP histone acetyltransferase: identification of a selective small molecule inhibitor.

Bowers EM, Yan G, Mukherjee C, Orry A, Wang L, Holbert MA, Crump NT, Hazzalin CA, Liszczak G, Yuan H, Larocca C, Saldanha SA, Abagyan R, Sun Y, Meyers DJ, Marmorstein R, Mahadevan LC, Alani RM, Cole PA 2010 May Chem. Biol. 5 17 471-82