Publications by category
Journal articles
Madern JM, Voorneveld J, Rack JGM, Kistemaker HAV, Ahel I, van der Marel GA, Codée JDC, Filippov DV (2023). 4-Thioribose Analogues of Adenosine Diphosphate Ribose (ADPr) Peptides. Organic Letters, 25(27), 4980-4984.
Suskiewicz MJ, Prokhorova E, Rack JGM, Ahel I (2023). ADP-ribosylation from molecular mechanisms to therapeutic implications.
Cell,
186(21), 4475-4495.
Abstract:
ADP-ribosylation from molecular mechanisms to therapeutic implications
ADP-ribosylation is a ubiquitous modification of biomolecules, including proteins and nucleic acids, that regulates various cellular functions in all kingdoms of life. The recent emergence of new technologies to study ADP-ribosylation has reshaped our understanding of the molecular mechanisms that govern the establishment, removal, and recognition of this modification, as well as its impact on cellular and organismal function. These advances have also revealed the intricate involvement of ADP-ribosylation in human physiology and pathology and the enormous potential that their manipulation holds for therapy. In this review, we present the state-of-the-art findings covering the work in structural biology, biochemistry, cell biology, and clinical aspects of ADP-ribosylation.
Abstract.
Tashiro K, Wijngaarden S, Mohapatra J, Rack JGM, Ahel I, Filippov DV, Liszczak G (2023). Chemoenzymatic and Synthetic Approaches to Investigate Aspartate- and Glutamate-ADP-Ribosylation. Journal of the American Chemical Society, 145(25), 14000-14009.
Minnee H, Chung H, Rack JGM, van der Marel GA, Overkleeft HS, Codée JDC, Ahel I, Filippov DV (2023). Four of a Kind: a Complete Collection of ADP-Ribosylated Histidine Isosteres Using Cu(I)- and Ru(II)-Catalyzed Click Chemistry. The Journal of Organic Chemistry, 88(15), 10801-10809.
Schuller M, Raggiaschi R, Mikolcevic P, Rack JGM, Ariza A, Zhang Y, Ledermann R, Tang C, Mikoc A, Ahel I, et al (2023). Molecular basis for the reversible ADP-ribosylation of guanosine bases. Molecular Cell, 83(13), 2303-2315.e6.
Đukić N, Strømland Ø, Elsborg JD, Munnur D, Zhu K, Schuller M, Chatrin C, Kar P, Duma L, Suyari O, et al (2023). PARP14 is a PARP with both ADP-ribosyl transferase and hydrolase activities.
Sci Adv,
9(37).
Abstract:
PARP14 is a PARP with both ADP-ribosyl transferase and hydrolase activities.
PARP14 is a mono-ADP-ribosyl transferase involved in the control of immunity, transcription, and DNA replication stress management. However, little is known about the ADP-ribosylation activity of PARP14, including its substrate specificity or how PARP14-dependent ADP-ribosylation is reversed. We show that PARP14 is a dual-function enzyme with both ADP-ribosyl transferase and hydrolase activity acting on both protein and nucleic acid substrates. In particular, we show that the PARP14 macrodomain 1 is an active ADP-ribosyl hydrolase. We also demonstrate hydrolytic activity for the first macrodomain of PARP9. We reveal that expression of a PARP14 mutant with the inactivated macrodomain 1 results in a marked increase in mono(ADP-ribosyl)ation of proteins in human cells, including PARP14 itself and antiviral PARP13, and displays specific cellular phenotypes. Moreover, we demonstrate that the closely related hydrolytically active macrodomain of SARS2 Nsp3, Mac1, efficiently reverses PARP14 ADP-ribosylation in vitro and in cells, supporting the evolution of viral macrodomains to counteract PARP14-mediated antiviral response.
Abstract.
Author URL.
Fontana P, Buch-Larsen SC, Suyari O, Smith R, Suskiewicz MJ, Schützenhofer K, Ariza A, Rack JGM, Nielsen ML, Ahel I, et al (2023). Serine ADP-ribosylation in Drosophila provides insights into the evolution of reversible ADP-ribosylation signalling.
Nature Communications,
14(1).
Abstract:
Serine ADP-ribosylation in Drosophila provides insights into the evolution of reversible ADP-ribosylation signalling
AbstractIn the mammalian DNA damage response, ADP-ribosylation signalling is of crucial importance to mark sites of DNA damage as well as recruit and regulate repairs factors. Specifically, the PARP1:HPF1 complex recognises damaged DNA and catalyses the formation of serine-linked ADP-ribosylation marks (mono-Ser-ADPr), which are extended into ADP-ribose polymers (poly-Ser-ADPr) by PARP1 alone. Poly-Ser-ADPr is reversed by PARG, while the terminal mono-Ser-ADPr is removed by ARH3. Despite its significance and apparent evolutionary conservation, little is known about ADP-ribosylation signalling in non-mammalian Animalia. The presence of HPF1, but absence of ARH3, in some insect genomes, including Drosophila species, raises questions regarding the existence and reversal of serine-ADP-ribosylation in these species. Here we show by quantitative proteomics that Ser-ADPr is the major form of ADP-ribosylation in the DNA damage response of Drosophila melanogaster and is dependent on the dParp1:dHpf1 complex. Moreover, our structural and biochemical investigations uncover the mechanism of mono-Ser-ADPr removal by Drosophila Parg. Collectively, our data reveal PARP:HPF1-mediated Ser-ADPr as a defining feature of the DDR in Animalia. The striking conservation within this kingdom suggests that organisms that carry only a core set of ADP-ribosyl metabolising enzymes, such as Drosophila, are valuable model organisms to study the physiological role of Ser-ADPr signalling.
Abstract.
Minnee H, Rack JGM, van der Marel GA, Overkleeft HS, Codée JDC, Ahel I, Filippov DV (2023). Solid‐Phase Synthesis and Biological Evaluation of Peptides ADP‐Ribosylated at Histidine.
Angewandte ChemieAbstract:
Solid‐Phase Synthesis and Biological Evaluation of Peptides ADP‐Ribosylated at Histidine
AbstractThe transfer of an adenosine diphosphate (ADP) ribose moiety to a nucleophilic side chain by consumption of nicotinamide adenine dinucleotide is referred to as ADP‐ribosylation, which allows for the spatiotemporal regulation of vital processes such as apoptosis and DNA repair. Recent mass‐spectrometry based analyses of the “ADP‐ribosylome” have identified histidine as ADP‐ribose acceptor site. In order to study this modification, a fully synthetic strategy towards α‐configured N(τ)‐ and N(π)‐ADP‐ribosylated histidine‐containing peptides has been developed. Ribofuranosylated histidine building blocks were obtained via Mukaiyama‐type glycosylation and the building blocks were integrated into an ADP‐ribosylome derived peptide sequence using fluorenylmethyloxycarbonyl (Fmoc)‐based solid‐phase peptide synthesis. On‐resin installation of the ADP moiety was achieved using phosphoramidite chemistry, and global deprotection provided the desired ADP‐ribosylated oligopeptides. The stability under various chemical conditions and resistance against (ADP‐ribosyl) hydrolase‐mediated degradation has been investigated to reveal that the constructs are stable under various chemical conditions and non‐degradable by any of the known ADP‐ribosylhydrolases.
Abstract.
Minnee H, Rack JGM, van der Marel GA, Overkleeft HS, Codée JDC, Ahel I, Filippov D (2023). Solid‐Phase Synthesis and Biological Evaluation of Peptides ADP‐ribosylated at Histidine. Angewandte Chemie International Edition
Hlousek-Kasun A, Mikolcevic P, Rack JGM, Tromans-Coia C, Schuller M, Jankevicius G, Matkovic M, Bertosa B, Ahel I, Mikoc A, et al (2022). <i>Streptomyces</i><i> coelicolor</i> macrodomain hydrolase SCO6735 cleaves thymidine-linked ADP-ribosylation of DNA.
COMPUTATIONAL AND STRUCTURAL BIOTECHNOLOGY JOURNAL,
20, 4337-4350.
Author URL.
Minnee H, Rack JGM, van der Marel GA, Overkleeft HS, Codee JDC, Ahel I, Filippov DV (2022). Mimetics of ADP-Ribosylated Histidine through Copper(I)-Catalyzed Click Chemistry.
ORGANIC LETTERS,
24(21), 3776-3780.
Author URL.
Beijer D, Agnew T, Rack JGM, Prokhorova E, Deconinck T, Ceulemans B, Peric S, Rasic VM, De Jonghe P, Ahel I, et al (2021). Biallelic <i>ADPRHL2</i> mutations in complex neuropathy affect ADP ribosylation and DNA damage response.
LIFE SCIENCE ALLIANCE,
4(11).
Author URL.
Schuller M, Correy GJ, Gahbauer S, Fearon D, Wu T, Diaz RE, Young ID, Martins LC, Smith DH, Schulze-Gahmen U, et al (2021). Fragment binding to the Nsp3 macrodomain of SARS-CoV-2 identified through crystallographic screening and computational docking.
SCIENCE ADVANCES,
7(16).
Author URL.
Rack JGM, Liu Q, Zorzini V, Voorneveld J, Ariza A, Ebrahimi KH, Reber JM, Krassnig SC, Ahel D, van der Marel GA, et al (2021). Mechanistic insights into the three steps of poly(ADP-ribosylation) reversal.
NATURE COMMUNICATIONS,
12(1).
Author URL.
Gorbunova V, Buschbeck M, Cambronne XA, Chellappa K, Corda D, Du J, Freichel M, Gigas J, Green AE, Gu F, et al (2021). Meeting Report the 2021 FASEB science research conference on NAD metabolism and signaling.
AGING-US,
13(23), 24924-24930.
Author URL.
Voorneveld J, Rack JGM, van Gijlswijk L, Meeuwenoord NJ, Liu Q, Overkleeft HS, van Der Marel GA, Ahel I, Filippov DV (2021). Molecular Tools for the Study of ADP-Ribosylation: a Unified and Versatile Method to Synthesise Native Mono-ADP-Ribosylated Peptides.
CHEMISTRY-A EUROPEAN JOURNAL,
27(41), 10621-10627.
Author URL.
Kong L, Feng B, Yan Y, Zhang C, Kim JH, Xu L, Rack JGM, Wang Y, Jang J-C, Ahel I, et al (2021). Noncanonical mono(ADP-ribosyl)ation of zinc finger SZF proteins counteracts ubiquitination for protein homeostasis in plant immunity.
MOLECULAR CELL,
81(22), 4591-+.
Author URL.
Gorbunova V, Buschbeck M, Cambronne XA, Chellappa K, Corda D, Du J, Freichel M, Gigas J, Green AE, Gu F, et al (2021). The 2021 FASEB science research conference on NAD metabolism and signaling. Aging, 13(23), 24924-24930.
Schuetzenhofer K, Rack JGM, Ahel I (2021). The Making and Breaking of Serine-ADP-Ribosylation in the DNA Damage Response.
FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY,
9 Author URL.
Rack JGM, Palazzo L, Ahel I (2020). (ADP-ribosyl)hydrolases: structure, function, and biology.
GENES & DEVELOPMENT,
34(5-6), 263-284.
Author URL.
Rack JGM, Zorzini V, Zhu Z, Schuller M, Ahel D, Ahel I (2020). Viral macrodomains: a structural and evolutionary assessment of the pharmacological potential.
OPEN BIOLOGY,
10(11).
Author URL.
Munnur D, Bartlett E, Mikolcevic P, Kirby IT, Rack JGM, Mikoc A, Cohen MS, Ahel I (2019). Reversible ADP-ribosylation of RNA.
NUCLEIC ACIDS RESEARCH,
47(11), 5658-5669.
Author URL.
Rack JGM, Ariza A, Drown BS, Henfrey C, Bartlett E, Shirai T, Hergenrother PJ, Ahel I (2018). (ADP-ribosyl)hydrolases: Structural Basis for Differential Substrate Recognition and Inhibition.
CELL CHEMICAL BIOLOGY,
25(12), 1533-+.
Author URL.
Drown BS, Shirai T, Rack JGM, Ahel I, Hergenrother PJ (2018). Monitoring Poly(ADP-ribosyl)glycohydrolase Activity with a Continuous Fluorescent Substrate.
CELL CHEMICAL BIOLOGY,
25(12), 1562-+.
Author URL.
Voorneveld J, Rack JGM, Ahel I, Overkleeft HS, van der Marel GA, Filippov DV (2018). Synthetic α- and β-Ser-ADP-ribosylated Peptides Reveal α-Ser-ADPr as the Native Epimer.
ORGANIC LETTERS,
20(13), 4140-4143.
Author URL.
Gibbs-Seymour I, Fontana P, Rack JGM, Ahel I (2016). HPF1/C4orf27 is a PARP-1-Interacting Protein that Regulates PARP-1 ADP-Ribosylation Activity.
MOLECULAR CELL,
62(3), 432-442.
Author URL.
Rack JGM, Morra R, Barkauskaite E, Kraehenbuehl R, Ariza A, Qu Y, Ortmayer M, Leidecker O, Cameron DR, Matic I, et al (2015). Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens.
MOLECULAR CELL,
59(2), 309-320.
Author URL.
Rack JGM, Lutter T, Kjæreng Bjerga GE, Guder C, Ehrhardt C, Värv S, Ziegler M, Aasland R (2015). The PHD finger of p300 influences its ability to acetylate histone and non-histone targets.
Journal of Molecular Biology,
426(24), 3960-3972.
Abstract:
The PHD finger of p300 influences its ability to acetylate histone and non-histone targets
In enzymes that regulate chromatin structure, the combinatorial occurrence of modules that alter and recognise histone modifications is a recurrent feature. In this study, we explored the functional relationship between the acetyltransferase domain and the adjacent bromodomain/PHD finger (bromo/PHD) region of the transcriptional coactivator p300. We found that the bromo/PHD region of p300 can bind to the acetylated catalytic domain in vitro and augment the catalytic activity of the enzyme. Deletion of the PHD finger, but not the bromodomain, impaired the ability of the enzyme to acetylate histones in vivo, whilst it enhanced p300 self-acetylation. A point mutation in the p300 PHD finger that is related to the Rubinstein-Taybi syndrome resulted in increased self-acetylation but retained the ability to acetylate histones. Hence, the PHD finger appears to negatively regulate self-acetylation. Furthermore, our data suggest that the PHD finger has a role in the recruitment of p300 to chromatin.
Abstract.
Rack JGM, VanLinden MR, Lutter T, Aasland R, Ziegler M (2014). Constitutive Nuclear Localization of an Alternatively Spliced Sirtuin-2 Isoform.
JOURNAL OF MOLECULAR BIOLOGY,
426(8), 1677-1691.
Author URL.
Dolle C, Rack JGM, Ziegler M (2013). NAD and ADP-ribose metabolism in mitochondria.
FEBS JOURNAL,
280(15), 3530-3541.
Author URL.
Chapters
Rack JGM, Ahel I (2023). A Simple Method to Study ADP-Ribosylation Reversal: from Function to Drug Discovery. In (Ed)
Methods in Molecular Biology, 111-132.
Abstract:
A Simple Method to Study ADP-Ribosylation Reversal: from Function to Drug Discovery
Abstract.
Rack JGM, Perina D, Ahel I (2016). Macrodomains: Structure, Function, Evolution, and Catalytic Activities. In (Ed)
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 85, 431-454.
Author URL.
Publications by year
2023
Madern JM, Voorneveld J, Rack JGM, Kistemaker HAV, Ahel I, van der Marel GA, Codée JDC, Filippov DV (2023). 4-Thioribose Analogues of Adenosine Diphosphate Ribose (ADPr) Peptides. Organic Letters, 25(27), 4980-4984.
Rack JGM, Ahel I (2023). A Simple Method to Study ADP-Ribosylation Reversal: from Function to Drug Discovery. In (Ed)
Methods in Molecular Biology, 111-132.
Abstract:
A Simple Method to Study ADP-Ribosylation Reversal: from Function to Drug Discovery
Abstract.
Suskiewicz MJ, Prokhorova E, Rack JGM, Ahel I (2023). ADP-ribosylation from molecular mechanisms to therapeutic implications.
Cell,
186(21), 4475-4495.
Abstract:
ADP-ribosylation from molecular mechanisms to therapeutic implications
ADP-ribosylation is a ubiquitous modification of biomolecules, including proteins and nucleic acids, that regulates various cellular functions in all kingdoms of life. The recent emergence of new technologies to study ADP-ribosylation has reshaped our understanding of the molecular mechanisms that govern the establishment, removal, and recognition of this modification, as well as its impact on cellular and organismal function. These advances have also revealed the intricate involvement of ADP-ribosylation in human physiology and pathology and the enormous potential that their manipulation holds for therapy. In this review, we present the state-of-the-art findings covering the work in structural biology, biochemistry, cell biology, and clinical aspects of ADP-ribosylation.
Abstract.
Tashiro K, Wijngaarden S, Mohapatra J, Rack JGM, Ahel I, Filippov DV, Liszczak G (2023). Chemoenzymatic and Synthetic Approaches to Investigate Aspartate- and Glutamate-ADP-Ribosylation. Journal of the American Chemical Society, 145(25), 14000-14009.
Minnee H, Chung H, Rack JGM, van der Marel GA, Overkleeft HS, Codée JDC, Ahel I, Filippov DV (2023). Four of a Kind: a Complete Collection of ADP-Ribosylated Histidine Isosteres Using Cu(I)- and Ru(II)-Catalyzed Click Chemistry. The Journal of Organic Chemistry, 88(15), 10801-10809.
Schuller M, Raggiaschi R, Mikolcevic P, Rack JGM, Ariza A, Zhang Y, Ledermann R, Tang C, Mikoc A, Ahel I, et al (2023). Molecular basis for the reversible ADP-ribosylation of guanosine bases. Molecular Cell, 83(13), 2303-2315.e6.
Đukić N, Strømland Ø, Munnur D, Zhu K, Schuller M, Chatrin C, Kar P, Rack JGM, Baretić D, Schüler H, et al (2023). PARP14 is a PARP with both ADP-ribosyl transferase and hydrolase activities.
Đukić N, Strømland Ø, Elsborg JD, Munnur D, Zhu K, Schuller M, Chatrin C, Kar P, Duma L, Suyari O, et al (2023). PARP14 is a PARP with both ADP-ribosyl transferase and hydrolase activities.
Sci Adv,
9(37).
Abstract:
PARP14 is a PARP with both ADP-ribosyl transferase and hydrolase activities.
PARP14 is a mono-ADP-ribosyl transferase involved in the control of immunity, transcription, and DNA replication stress management. However, little is known about the ADP-ribosylation activity of PARP14, including its substrate specificity or how PARP14-dependent ADP-ribosylation is reversed. We show that PARP14 is a dual-function enzyme with both ADP-ribosyl transferase and hydrolase activity acting on both protein and nucleic acid substrates. In particular, we show that the PARP14 macrodomain 1 is an active ADP-ribosyl hydrolase. We also demonstrate hydrolytic activity for the first macrodomain of PARP9. We reveal that expression of a PARP14 mutant with the inactivated macrodomain 1 results in a marked increase in mono(ADP-ribosyl)ation of proteins in human cells, including PARP14 itself and antiviral PARP13, and displays specific cellular phenotypes. Moreover, we demonstrate that the closely related hydrolytically active macrodomain of SARS2 Nsp3, Mac1, efficiently reverses PARP14 ADP-ribosylation in vitro and in cells, supporting the evolution of viral macrodomains to counteract PARP14-mediated antiviral response.
Abstract.
Author URL.
Fontana P, Buch-Larsen SC, Suyari O, Smith R, Suskiewicz MJ, Schützenhofer K, Ariza A, Rack JGM, Nielsen ML, Ahel I, et al (2023). Serine ADP-ribosylation in Drosophila provides insights into the evolution of reversible ADP-ribosylation signalling.
Nature Communications,
14(1).
Abstract:
Serine ADP-ribosylation in Drosophila provides insights into the evolution of reversible ADP-ribosylation signalling
AbstractIn the mammalian DNA damage response, ADP-ribosylation signalling is of crucial importance to mark sites of DNA damage as well as recruit and regulate repairs factors. Specifically, the PARP1:HPF1 complex recognises damaged DNA and catalyses the formation of serine-linked ADP-ribosylation marks (mono-Ser-ADPr), which are extended into ADP-ribose polymers (poly-Ser-ADPr) by PARP1 alone. Poly-Ser-ADPr is reversed by PARG, while the terminal mono-Ser-ADPr is removed by ARH3. Despite its significance and apparent evolutionary conservation, little is known about ADP-ribosylation signalling in non-mammalian Animalia. The presence of HPF1, but absence of ARH3, in some insect genomes, including Drosophila species, raises questions regarding the existence and reversal of serine-ADP-ribosylation in these species. Here we show by quantitative proteomics that Ser-ADPr is the major form of ADP-ribosylation in the DNA damage response of Drosophila melanogaster and is dependent on the dParp1:dHpf1 complex. Moreover, our structural and biochemical investigations uncover the mechanism of mono-Ser-ADPr removal by Drosophila Parg. Collectively, our data reveal PARP:HPF1-mediated Ser-ADPr as a defining feature of the DDR in Animalia. The striking conservation within this kingdom suggests that organisms that carry only a core set of ADP-ribosyl metabolising enzymes, such as Drosophila, are valuable model organisms to study the physiological role of Ser-ADPr signalling.
Abstract.
Minnee H, Rack JGM, van der Marel GA, Overkleeft HS, Codée JDC, Ahel I, Filippov DV (2023). Solid‐Phase Synthesis and Biological Evaluation of Peptides ADP‐Ribosylated at Histidine.
Angewandte ChemieAbstract:
Solid‐Phase Synthesis and Biological Evaluation of Peptides ADP‐Ribosylated at Histidine
AbstractThe transfer of an adenosine diphosphate (ADP) ribose moiety to a nucleophilic side chain by consumption of nicotinamide adenine dinucleotide is referred to as ADP‐ribosylation, which allows for the spatiotemporal regulation of vital processes such as apoptosis and DNA repair. Recent mass‐spectrometry based analyses of the “ADP‐ribosylome” have identified histidine as ADP‐ribose acceptor site. In order to study this modification, a fully synthetic strategy towards α‐configured N(τ)‐ and N(π)‐ADP‐ribosylated histidine‐containing peptides has been developed. Ribofuranosylated histidine building blocks were obtained via Mukaiyama‐type glycosylation and the building blocks were integrated into an ADP‐ribosylome derived peptide sequence using fluorenylmethyloxycarbonyl (Fmoc)‐based solid‐phase peptide synthesis. On‐resin installation of the ADP moiety was achieved using phosphoramidite chemistry, and global deprotection provided the desired ADP‐ribosylated oligopeptides. The stability under various chemical conditions and resistance against (ADP‐ribosyl) hydrolase‐mediated degradation has been investigated to reveal that the constructs are stable under various chemical conditions and non‐degradable by any of the known ADP‐ribosylhydrolases.
Abstract.
Minnee H, Rack JGM, van der Marel GA, Overkleeft HS, Codée JDC, Ahel I, Filippov D (2023). Solid‐Phase Synthesis and Biological Evaluation of Peptides ADP‐ribosylated at Histidine. Angewandte Chemie International Edition
2022
Hlousek-Kasun A, Mikolcevic P, Rack JGM, Tromans-Coia C, Schuller M, Jankevicius G, Matkovic M, Bertosa B, Ahel I, Mikoc A, et al (2022). <i>Streptomyces</i><i> coelicolor</i> macrodomain hydrolase SCO6735 cleaves thymidine-linked ADP-ribosylation of DNA.
COMPUTATIONAL AND STRUCTURAL BIOTECHNOLOGY JOURNAL,
20, 4337-4350.
Author URL.
Minnee H, Rack JGM, van der Marel GA, Overkleeft HS, Codee JDC, Ahel I, Filippov DV (2022). Mimetics of ADP-Ribosylated Histidine through Copper(I)-Catalyzed Click Chemistry.
ORGANIC LETTERS,
24(21), 3776-3780.
Author URL.
2021
Beijer D, Agnew T, Rack JGM, Prokhorova E, Deconinck T, Ceulemans B, Peric S, Rasic VM, De Jonghe P, Ahel I, et al (2021). Biallelic <i>ADPRHL2</i> mutations in complex neuropathy affect ADP ribosylation and DNA damage response.
LIFE SCIENCE ALLIANCE,
4(11).
Author URL.
Schuller M, Correy GJ, Gahbauer S, Fearon D, Wu T, Diaz RE, Young ID, Martins LC, Smith DH, Schulze-Gahmen U, et al (2021). Fragment binding to the Nsp3 macrodomain of SARS-CoV-2 identified through crystallographic screening and computational docking.
SCIENCE ADVANCES,
7(16).
Author URL.
Rack JGM, Liu Q, Zorzini V, Voorneveld J, Ariza A, Ebrahimi KH, Reber JM, Krassnig SC, Ahel D, van der Marel GA, et al (2021). Mechanistic insights into the three steps of poly(ADP-ribosylation) reversal.
NATURE COMMUNICATIONS,
12(1).
Author URL.
Gorbunova V, Buschbeck M, Cambronne XA, Chellappa K, Corda D, Du J, Freichel M, Gigas J, Green AE, Gu F, et al (2021). Meeting Report the 2021 FASEB science research conference on NAD metabolism and signaling.
AGING-US,
13(23), 24924-24930.
Author URL.
Voorneveld J, Rack JGM, van Gijlswijk L, Meeuwenoord NJ, Liu Q, Overkleeft HS, van Der Marel GA, Ahel I, Filippov DV (2021). Molecular Tools for the Study of ADP-Ribosylation: a Unified and Versatile Method to Synthesise Native Mono-ADP-Ribosylated Peptides.
CHEMISTRY-A EUROPEAN JOURNAL,
27(41), 10621-10627.
Author URL.
Kong L, Feng B, Yan Y, Zhang C, Kim JH, Xu L, Rack JGM, Wang Y, Jang J-C, Ahel I, et al (2021). Noncanonical mono(ADP-ribosyl)ation of zinc finger SZF proteins counteracts ubiquitination for protein homeostasis in plant immunity.
MOLECULAR CELL,
81(22), 4591-+.
Author URL.
Gorbunova V, Buschbeck M, Cambronne XA, Chellappa K, Corda D, Du J, Freichel M, Gigas J, Green AE, Gu F, et al (2021). The 2021 FASEB science research conference on NAD metabolism and signaling. Aging, 13(23), 24924-24930.
Schuetzenhofer K, Rack JGM, Ahel I (2021). The Making and Breaking of Serine-ADP-Ribosylation in the DNA Damage Response.
FRONTIERS IN CELL AND DEVELOPMENTAL BIOLOGY,
9 Author URL.
2020
Rack JGM, Palazzo L, Ahel I (2020). (ADP-ribosyl)hydrolases: structure, function, and biology.
GENES & DEVELOPMENT,
34(5-6), 263-284.
Author URL.
Schuller M, Correy GJ, Gahbauer S, Fearon D, Wu T, Díaz RE, Young ID, Martins LC, Smith DH, Schulze-Gahmen U, et al (2020). Fragment Binding to the Nsp3 Macrodomain of SARS-CoV-2 Identified Through Crystallographic Screening and Computational Docking. , 1(12-02).
Rack JGM, Zorzini V, Zhu Z, Schuller M, Ahel D, Ahel I (2020). Viral macrodomains: a structural and evolutionary assessment of the pharmacological potential.
OPEN BIOLOGY,
10(11).
Author URL.
2019
Munnur D, Bartlett E, Mikolcevic P, Kirby IT, Rack JGM, Mikoc A, Cohen MS, Ahel I (2019). Reversible ADP-ribosylation of RNA.
NUCLEIC ACIDS RESEARCH,
47(11), 5658-5669.
Author URL.
2018
Rack JGM, Ariza A, Drown BS, Henfrey C, Bartlett E, Shirai T, Hergenrother PJ, Ahel I (2018). (ADP-ribosyl)hydrolases: Structural Basis for Differential Substrate Recognition and Inhibition.
CELL CHEMICAL BIOLOGY,
25(12), 1533-+.
Author URL.
Drown BS, Shirai T, Rack JGM, Ahel I, Hergenrother PJ (2018). Monitoring Poly(ADP-ribosyl)glycohydrolase Activity with a Continuous Fluorescent Substrate.
CELL CHEMICAL BIOLOGY,
25(12), 1562-+.
Author URL.
Voorneveld J, Rack JGM, Ahel I, Overkleeft HS, van der Marel GA, Filippov DV (2018). Synthetic α- and β-Ser-ADP-ribosylated Peptides Reveal α-Ser-ADPr as the Native Epimer.
ORGANIC LETTERS,
20(13), 4140-4143.
Author URL.
2016
Gibbs-Seymour I, Fontana P, Rack JGM, Ahel I (2016). HPF1/C4orf27 is a PARP-1-Interacting Protein that Regulates PARP-1 ADP-Ribosylation Activity.
MOLECULAR CELL,
62(3), 432-442.
Author URL.
Rack JGM, Perina D, Ahel I (2016). Macrodomains: Structure, Function, Evolution, and Catalytic Activities. In (Ed)
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 85, 431-454.
Author URL.
2015
Rack JGM, Morra R, Barkauskaite E, Kraehenbuehl R, Ariza A, Qu Y, Ortmayer M, Leidecker O, Cameron DR, Matic I, et al (2015). Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens.
MOLECULAR CELL,
59(2), 309-320.
Author URL.
Rack JGM, Lutter T, Kjæreng Bjerga GE, Guder C, Ehrhardt C, Värv S, Ziegler M, Aasland R (2015). The PHD finger of p300 influences its ability to acetylate histone and non-histone targets.
Journal of Molecular Biology,
426(24), 3960-3972.
Abstract:
The PHD finger of p300 influences its ability to acetylate histone and non-histone targets
In enzymes that regulate chromatin structure, the combinatorial occurrence of modules that alter and recognise histone modifications is a recurrent feature. In this study, we explored the functional relationship between the acetyltransferase domain and the adjacent bromodomain/PHD finger (bromo/PHD) region of the transcriptional coactivator p300. We found that the bromo/PHD region of p300 can bind to the acetylated catalytic domain in vitro and augment the catalytic activity of the enzyme. Deletion of the PHD finger, but not the bromodomain, impaired the ability of the enzyme to acetylate histones in vivo, whilst it enhanced p300 self-acetylation. A point mutation in the p300 PHD finger that is related to the Rubinstein-Taybi syndrome resulted in increased self-acetylation but retained the ability to acetylate histones. Hence, the PHD finger appears to negatively regulate self-acetylation. Furthermore, our data suggest that the PHD finger has a role in the recruitment of p300 to chromatin.
Abstract.
2014
Rack JGM, VanLinden MR, Lutter T, Aasland R, Ziegler M (2014). Constitutive Nuclear Localization of an Alternatively Spliced Sirtuin-2 Isoform.
JOURNAL OF MOLECULAR BIOLOGY,
426(8), 1677-1691.
Author URL.
2013
Dolle C, Rack JGM, Ziegler M (2013). NAD and ADP-ribose metabolism in mitochondria.
FEBS JOURNAL,
280(15), 3530-3541.
Author URL.