| Year |
Citation |
Score |
| 2024 |
Zhang Z, Fu J, Rack JGM, Li C, Voorneveld J, Filippov DV, Ahel I, Luo ZQ, Das C. Legionella metaeffector MavL reverses ubiquitin ADP-ribosylation via a conserved arginine-specific macrodomain. Nature Communications. 15: 2452. PMID 38503748 DOI: 10.1038/s41467-024-46649-2 |
0.381 |
|
| 2023 |
Zhu K, Suskiewicz MJ, Chatrin C, Strømland Ø, Dorsey BW, Aucagne V, Ahel D, Ahel I. DELTEX E3 ligases ubiquitylate ADP-ribosyl modification on nucleic acids. Nucleic Acids Research. PMID 38000390 DOI: 10.1093/nar/gkad1119 |
0.79 |
|
| 2023 |
Suskiewicz MJ, Prokhorova E, Rack JGM, Ahel I. ADP-ribosylation from molecular mechanisms to therapeutic implications. Cell. 186: 4475-4495. PMID 37832523 DOI: 10.1016/j.cell.2023.08.030 |
0.761 |
|
| 2023 |
Đukić N, Strømland Ø, Elsborg JD, Munnur D, Zhu K, Schuller M, Chatrin C, Kar P, Duma L, Suyari O, Rack JGM, Baretić D, Crudgington DRK, Groslambert J, Fowler G, ... ... Ahel I, et al. PARP14 is a PARP with both ADP-ribosyl transferase and hydrolase activities. Science Advances. 9: eadi2687. PMID 37703374 DOI: 10.1126/sciadv.adi2687 |
0.827 |
|
| 2023 |
Groslambert J, Prokhorova E, Wondisford AR, Tromans-Coia C, Giansanti C, Jansen J, Timinszky G, Dobbelstein M, Ahel D, O'Sullivan RJ, Ahel I. The interplay of TARG1 and PARG protects against genomic instability. Cell Reports. 42: 113113. PMID 37676774 DOI: 10.1016/j.celrep.2023.113113 |
0.817 |
|
| 2023 |
Schuller M, Raggiaschi R, Mikolcevic P, Rack JGM, Ariza A, Zhang Y, Ledermann R, Tang C, Mikoc A, Ahel I. Molecular basis for the reversible ADP-ribosylation of guanosine bases. Molecular Cell. 83: 2303-2315.e6. PMID 37390817 DOI: 10.1016/j.molcel.2023.06.013 |
0.784 |
|
| 2023 |
Suskiewicz MJ, Munnur D, Strømland Ø, Yang JC, Easton LE, Chatrin C, Zhu K, Baretić D, Goffinont S, Schuller M, Wu WF, Elkins JM, Ahel D, Sanyal S, Neuhaus D, ... Ahel I, et al. Updated protein domain annotation of the PARP protein family sheds new light on biological function. Nucleic Acids Research. PMID 37326024 DOI: 10.1093/nar/gkad514 |
0.801 |
|
| 2023 |
Fontana P, Buch-Larsen SC, Suyari O, Smith R, Suskiewicz MJ, Schützenhofer K, Ariza A, Rack JGM, Nielsen ML, Ahel I. Serine ADP-ribosylation in Drosophila provides insights into the evolution of reversible ADP-ribosylation signalling. Nature Communications. 14: 3200. PMID 37268618 DOI: 10.1038/s41467-023-38793-y |
0.8 |
|
| 2023 |
Duma L, Ahel I. The function and regulation of ADP-ribosylation in the DNA damage response. Biochemical Society Transactions. PMID 37171085 DOI: 10.1042/BST20220749 |
0.431 |
|
| 2023 |
Longarini EJ, Dauben H, Locatelli C, Wondisford AR, Smith R, Muench C, Kolvenbach A, Lynskey ML, Pope A, Bonfiglio JJ, Jurado EP, Fajka-Boja R, Colby T, Schuller M, Ahel I, et al. Modular antibodies reveal DNA damage-induced mono-ADP-ribosylation as a second wave of PARP1 signaling. Molecular Cell. PMID 37116497 DOI: 10.1016/j.molcel.2023.03.027 |
0.766 |
|
| 2023 |
Smith R, Zentout S, Rother M, Bigot N, Chapuis C, Mihuț A, Zobel FF, Ahel I, van Attikum H, Timinszky G, Huet S. HPF1-dependent histone ADP-ribosylation triggers chromatin relaxation to promote the recruitment of repair factors at sites of DNA damage. Nature Structural & Molecular Biology. PMID 37106138 DOI: 10.1038/s41594-023-00977-x |
0.431 |
|
| 2023 |
Schuller M, Zarganes-Tzitzikas T, Bennett J, De Cesco S, Fearon D, von Delft F, Fedorov O, Brennan PE, Ahel I. Discovery and Development Strategies for SARS-CoV-2 NSP3 Macrodomain Inhibitors. Pathogens (Basel, Switzerland). 12. PMID 36839595 DOI: 10.3390/pathogens12020324 |
0.718 |
|
| 2023 |
Gahbauer S, Correy GJ, Schuller M, Ferla MP, Doruk YU, Rachman M, Wu T, Diolaiti M, Wang S, Neitz RJ, Fearon D, Radchenko DS, Moroz YS, Irwin JJ, Renslo AR, ... ... Ahel I, et al. Iterative computational design and crystallographic screening identifies potent inhibitors targeting the Nsp3 macrodomain of SARS-CoV-2. Proceedings of the National Academy of Sciences of the United States of America. 120: e2212931120. PMID 36598939 DOI: 10.1073/pnas.2212931120 |
0.729 |
|
| 2022 |
Rack JGM, Ahel I. A Simple Method to Study ADP-Ribosylation Reversal: From Function to Drug Discovery. Methods in Molecular Biology (Clifton, N.J.). 2609: 111-132. PMID 36515833 DOI: 10.1007/978-1-0716-2891-1_8 |
0.316 |
|
| 2022 |
Mosler T, Baymaz HI, Gräf JF, Mikicic I, Blattner G, Bartlett E, Ostermaier M, Piccinno R, Yang J, Voigt A, Gatti M, Pellegrino S, Altmeyer M, Luck K, Ahel I, et al. PARP1 proximity proteomics reveals interaction partners at stressed replication forks. Nucleic Acids Research. PMID 36350633 DOI: 10.1093/nar/gkac948 |
0.387 |
|
| 2022 |
Zhu K, Suskiewicz MJ, Hloušek-Kasun A, Meudal H, Mikoč A, Aucagne V, Ahel D, Ahel I. DELTEX E3 ligases ubiquitylate ADP-ribosyl modification on protein substrates. Science Advances. 8: eadd4253. PMID 36197986 DOI: 10.1126/sciadv.add4253 |
0.794 |
|
| 2022 |
Hloušek-Kasun A, Mikolčević P, Rack JGM, Tromans-Coia C, Schuller M, Jankevicius G, Matković M, Bertoša B, Ahel I, Mikoč A. macrodomain hydrolase SCO6735 cleaves thymidine-linked ADP-ribosylation of DNA. Computational and Structural Biotechnology Journal. 20: 4337-4350. PMID 36051881 DOI: 10.1016/j.csbj.2022.08.002 |
0.85 |
|
| 2022 |
Gahbauer S, Correy GJ, Schuller M, Ferla MP, Doruk YU, Rachman M, Wu T, Diolaiti M, Wang S, Neitz RJ, Fearon D, Radchenko D, Moroz Y, Irwin JJ, Renslo AR, ... ... Ahel I, et al. Structure-based inhibitor optimization for the Nsp3 Macrodomain of SARS-CoV-2. Biorxiv : the Preprint Server For Biology. PMID 35794891 DOI: 10.1101/2022.06.27.497816 |
0.715 |
|
| 2022 |
Schuller M, Ahel I. Beyond protein modification: the rise of non-canonical ADP-ribosylation. The Biochemical Journal. 479: 463-477. PMID 35175282 DOI: 10.1042/BCJ20210280 |
0.76 |
|
| 2021 |
Schützenhofer K, Rack JGM, Ahel I. The Making and Breaking of Serine-ADP-Ribosylation in the DNA Damage Response. Frontiers in Cell and Developmental Biology. 9: 745922. PMID 34869334 DOI: 10.3389/fcell.2021.745922 |
0.446 |
|
| 2021 |
Hendriks IA, Buch-Larsen SC, Prokhorova E, Elsborg JD, Rebak AKLFS, Zhu K, Ahel D, Lukas C, Ahel I, Nielsen ML. The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome. Nature Communications. 12: 5893. PMID 34625544 DOI: 10.1038/s41467-021-26172-4 |
0.825 |
|
| 2021 |
Kong L, Feng B, Yan Y, Zhang C, Kim JH, Xu L, Rack JGM, Wang Y, Jang JC, Ahel I, Shan L, He P. Noncanonical mono(ADP-ribosyl)ation of zinc finger SZF proteins counteracts ubiquitination for protein homeostasis in plant immunity. Molecular Cell. PMID 34592134 DOI: 10.1016/j.molcel.2021.09.006 |
0.335 |
|
| 2021 |
Tromans-Coia C, Sanchi A, Moeller GK, Timinszky G, Lopes M, Ahel I. TARG1 protects against toxic DNA ADP-ribosylation. Nucleic Acids Research. PMID 34508355 DOI: 10.1093/nar/gkab771 |
0.409 |
|
| 2021 |
Beijer D, Agnew T, Rack JGM, Prokhorova E, Deconinck T, Ceulemans B, Peric S, Milic Rasic V, De Jonghe P, Ahel I, Baets J. Biallelic mutations in complex neuropathy affect ADP ribosylation and DNA damage response. Life Science Alliance. 4. PMID 34479984 DOI: 10.26508/lsa.202101057 |
0.304 |
|
| 2021 |
Schuller M, Butler RE, Ariza A, Tromans-Coia C, Jankevicius G, Claridge TDW, Kendall SL, Goh S, Stewart GR, Ahel I. Molecular basis for DarT ADP-ribosylation of a DNA base. Nature. PMID 34408320 DOI: 10.1038/s41586-021-03825-4 |
0.853 |
|
| 2021 |
Palazzo L, Suskiewicz MJ, Ahel I. Serine ADP-ribosylation in DNA-damage response regulation. Current Opinion in Genetics & Development. 71: 106-113. PMID 34340015 DOI: 10.1016/j.gde.2021.07.005 |
0.811 |
|
| 2021 |
Lüscher B, Ahel I, Altmeyer M, Ashworth A, Bai P, Chang P, Cohen M, Corda D, Dantzer F, Daugherty MD, Dawson TM, Dawson VL, Deindl S, Fehr AR, Feijs KLH, et al. ADP-ribosyltransferases, an update on function and nomenclature. The Febs Journal. PMID 34323016 DOI: 10.1111/febs.16142 |
0.72 |
|
| 2021 |
Rack JGM, Liu Q, Zorzini V, Voorneveld J, Ariza A, Honarmand Ebrahimi K, Reber JM, Krassnig SC, Ahel D, van der Marel GA, Mangerich A, McCullagh JSO, Filippov DV, Ahel I. Mechanistic insights into the three steps of poly(ADP-ribosylation) reversal. Nature Communications. 12: 4581. PMID 34321462 DOI: 10.1038/s41467-021-24723-3 |
0.819 |
|
| 2021 |
Prokhorova E, Zobel F, Smith R, Zentout S, Gibbs-Seymour I, Schützenhofer K, Peters A, Groslambert J, Zorzini V, Agnew T, Brognard J, Nielsen ML, Ahel D, Huet S, Suskiewicz MJ, ... Ahel I, et al. Serine-linked PARP1 auto-modification controls PARP inhibitor response. Nature Communications. 12: 4055. PMID 34210965 DOI: 10.1038/s41467-021-24361-9 |
0.815 |
|
| 2021 |
Groslambert J, Prokhorova E, Ahel I. ADP-ribosylation of DNA and RNA. Dna Repair. 105: 103144. PMID 34116477 DOI: 10.1016/j.dnarep.2021.103144 |
0.408 |
|
| 2021 |
Bajusz D, Wade WS, Satała G, Bojarski AJ, Ilaš J, Ebner J, Grebien F, Papp H, Jakab F, Douangamath A, Fearon D, von Delft F, Schuller M, Ahel I, Wakefield A, et al. Exploring protein hotspots by optimized fragment pharmacophores. Nature Communications. 12: 3201. PMID 34045440 DOI: 10.1038/s41467-021-23443-y |
0.694 |
|
| 2021 |
Prokhorova E, Agnew T, Wondisford AR, Tellier M, Kaminski N, Beijer D, Holder J, Groslambert J, Suskiewicz MJ, Zhu K, Reber JM, Krassnig SC, Palazzo L, Murphy S, Nielsen ML, ... ... Ahel I, et al. Unrestrained poly-ADP-ribosylation provides insights into chromatin regulation and human disease. Molecular Cell. PMID 34019811 DOI: 10.1016/j.molcel.2021.04.028 |
0.811 |
|
| 2021 |
Schuller M, Correy GJ, Gahbauer S, Fearon D, Wu T, Díaz RE, Young ID, Carvalho Martins L, Smith DH, Schulze-Gahmen U, Owens TW, Deshpande I, Merz GE, Thwin AC, Biel JT, ... ... Ahel I, et al. Fragment binding to the Nsp3 macrodomain of SARS-CoV-2 identified through crystallographic screening and computational docking. Science Advances. 7. PMID 33853786 DOI: 10.1126/sciadv.abf8711 |
0.719 |
|
| 2021 |
Voorneveld J, Rack J, van Gijlswijk L, Meeuwenoord N, Liu Q, Overkleeft H, van der Marel G, Ahel I, Filippov D. Molecular Tools for the Study of ADP-ribosylation: A Unified and Versatile Method to Synthesise Native Mono-ADP-ribosylated Peptides. Chemistry (Weinheim An Der Bergstrasse, Germany). PMID 33769608 DOI: 10.1002/chem.202100337 |
0.354 |
|
| 2020 |
Genois MM, Gagné JP, Yasuhara T, Jackson J, Saxena S, Langelier MF, Ahel I, Bedford MT, Pascal JM, Vindigni A, Poirier GG, Zou L. CARM1 regulates replication fork speed and stress response by stimulating PARP1. Molecular Cell. PMID 33412112 DOI: 10.1016/j.molcel.2020.12.010 |
0.311 |
|
| 2020 |
Hewitt G, Borel V, Segura-Bayona S, Takaki T, Ruis P, Bellelli R, Lehmann LC, Sommerova L, Vancevska A, Tomas-Loba A, Zhu K, Cooper C, Fugger K, Patel H, Goldstone R, ... ... Ahel I, et al. Defective ALC1 nucleosome remodeling confers PARPi sensitization and synthetic lethality with HRD. Molecular Cell. PMID 33333017 DOI: 10.1016/j.molcel.2020.12.006 |
0.823 |
|
| 2020 |
Schuller M, Correy GJ, Gahbauer S, Fearon D, Wu T, Díaz RE, Young ID, Martins LC, Smith DH, Schulze-Gahmen U, Owens TW, Deshpande I, Merz GE, Thwin AC, Biel JT, ... ... Ahel I, et al. Fragment Binding to the Nsp3 Macrodomain of SARS-CoV-2 Identified Through Crystallographic Screening and Computational Docking. Biorxiv : the Preprint Server For Biology. PMID 33269349 DOI: 10.1101/2020.11.24.393405 |
0.717 |
|
| 2020 |
Rack JGM, Zorzini V, Zhu Z, Schuller M, Ahel D, Ahel I. Viral macrodomains: a structural and evolutionary assessment of the pharmacological potential. Open Biology. 10: 200237. PMID 33202171 DOI: 10.1098/rsob.200237 |
0.786 |
|
| 2020 |
Bilokapic S, Suskiewicz MJ, Ahel I, Halic M. Bridging of DNA breaks activates PARP2-HPF1 to modify chromatin. Nature. 585: 609-613. PMID 32939087 DOI: 10.1038/S41586-020-2725-7 |
0.831 |
|
| 2020 |
Suskiewicz MJ, Palazzo L, Hughes R, Ahel I. Progress and outlook in studying the substrate specificities of PARPs and related enzymes. The Febs Journal. PMID 32785980 DOI: 10.1111/Febs.15518 |
0.811 |
|
| 2020 |
Hanzlikova H, Prokhorova E, Krejcikova K, Cihlarova Z, Kalasova I, Kubovciak J, Sachova J, Hailstone R, Brazina J, Ghosh S, Cirak S, Gleeson JG, Ahel I, Caldecott KW. Pathogenic ARH3 mutations result in ADP-ribose chromatin scars during DNA strand break repair. Nature Communications. 11: 3391. PMID 32636369 DOI: 10.1038/S41467-020-17069-9 |
0.501 |
|
| 2020 |
Rack JGM, Palazzo L, Ahel I. (ADP-ribosyl)hydrolases: structure, function, and biology. Genes & Development. 34: 263-284. PMID 32029451 DOI: 10.1101/Gad.334631.119 |
0.41 |
|
| 2020 |
Suskiewicz MJ, Zobel F, Ogden TEH, Fontana P, Ariza A, Yang JC, Zhu K, Bracken L, Hawthorne WJ, Ahel D, Neuhaus D, Ahel I. HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation. Nature. PMID 32028527 DOI: 10.1038/S41586-020-2013-6 |
0.839 |
|
| 2020 |
Lawarée E, Jankevicius G, Cooper C, Ahel I, Uphoff S, Tang CM. DNA ADP-Ribosylation Stalls Replication and Is Reversed by RecF-Mediated Homologous Recombination and Nucleotide Excision Repair. Cell Reports. 30: 1373-1384.e4. PMID 32023456 DOI: 10.1016/J.Celrep.2020.01.014 |
0.798 |
|
| 2019 |
Munnur D, Bartlett E, Mikolčević P, Kirby IT, Matthias Rack JG, Mikoč A, Cohen MS, Ahel I. Reversible ADP-ribosylation of RNA. Nucleic Acids Research. 47: 5658-5669. PMID 31216043 DOI: 10.1093/Nar/Gkz305 |
0.481 |
|
| 2019 |
Palazzo L, Mikolčević P, Mikoč A, Ahel I. ADP-ribosylation signalling and human disease. Open Biology. 9: 190041. PMID 30991935 DOI: 10.1098/Rsob.190041 |
0.412 |
|
| 2019 |
Munnur D, Somers J, Skalka G, Weston R, Jukes-Jones R, Bhogadia M, Dominguez C, Cain K, Ahel I, Malewicz M. NR4A Nuclear Receptors Target Poly-ADP-Ribosylated DNA-PKcs Protein to Promote DNA Repair. Cell Reports. 26: 2028-2036.e6. PMID 30784586 DOI: 10.1016/J.Celrep.2019.01.083 |
0.492 |
|
| 2018 |
Rack JGM, Ariza A, Drown BS, Henfrey C, Bartlett E, Shirai T, Hergenrother PJ, Ahel I. (ADP-ribosyl)hydrolases: Structural Basis for Differential Substrate Recognition and Inhibition. Cell Chemical Biology. 25: 1533-1546.e12. PMID 30472116 DOI: 10.2210/Pdb6Hh4/Pdb |
0.459 |
|
| 2018 |
Palazzo L, Ahel I. PARPs in genome stability and signal transduction: implications for cancer therapy. Biochemical Society Transactions. 46: 1681-1695. PMID 30420415 DOI: 10.1042/Bst20180418 |
0.5 |
|
| 2018 |
Drown BS, Shirai T, Rack JGM, Ahel I, Hergenrother PJ. Monitoring Poly(ADP-ribosyl)glycohydrolase Activity with a Continuous Fluorescent Substrate. Cell Chemical Biology. PMID 30318463 DOI: 10.1016/J.Chembiol.2018.09.008 |
0.428 |
|
| 2018 |
Bartlett E, Bonfiglio JJ, Prokhorova E, Colby T, Zobel F, Ahel I, Matic I. Interplay of Histone Marks with Serine ADP-Ribosylation. Cell Reports. 24: 3488-3502.e5. PMID 30257210 DOI: 10.1016/J.Celrep.2018.08.092 |
0.431 |
|
| 2018 |
Posavec Marjanovic M, Jankevicius G, Ahel I. Hydrolysis of ADP-Ribosylation by Macrodomains. Methods in Molecular Biology (Clifton, N.J.). 1813: 215-223. PMID 30097870 DOI: 10.1007/978-1-4939-8588-3_14 |
0.814 |
|
| 2018 |
Kwasna D, Abdul Rehman SA, Natarajan J, Matthews S, Madden R, De Cesare V, Weidlich S, Virdee S, Ahel I, Gibbs-Seymour I, Kulathu Y. Discovery and Characterization of ZUFSP/ZUP1, a Distinct Deubiquitinase Class Important for Genome Stability. Molecular Cell. PMID 29576527 DOI: 10.1016/J.Molcel.2018.02.023 |
0.827 |
|
| 2018 |
Palazzo L, Leidecker O, Prokhorova E, Dauben H, Matic I, Ahel I. Serine is the major residue for ADP-ribosylation upon DNA damage. Elife. 7. PMID 29480802 DOI: 10.7554/Elife.34334 |
0.553 |
|
| 2018 |
Agnew T, Munnur D, Crawford K, Palazzo L, Mikoč A, Ahel I. MacroD1 Is a Promiscuous ADP-Ribosyl Hydrolase Localized to Mitochondria. Frontiers in Microbiology. 9: 20. PMID 29410655 DOI: 10.3389/Fmicb.2018.00020 |
0.49 |
|
| 2018 |
Palazzo L, Leidecker O, Prokhorova E, Dauben H, Matic I, Ahel I. Author response: Serine is the major residue for ADP-ribosylation upon DNA damage Elife. DOI: 10.7554/Elife.34334.011 |
0.442 |
|
| 2017 |
Fehr AR, Jankevicius G, Ahel I, Perlman S. Viral Macrodomains: Unique Mediators of Viral Replication and Pathogenesis. Trends in Microbiology. PMID 29268982 DOI: 10.1016/J.Tim.2017.11.011 |
0.791 |
|
| 2017 |
Crawford K, Bonfiglio JJ, Mikoč A, Matic I, Ahel I. Specificity of reversible ADP-ribosylation and regulation of cellular processes. Critical Reviews in Biochemistry and Molecular Biology. 1-19. PMID 29098880 DOI: 10.1080/10409238.2017.1394265 |
0.357 |
|
| 2017 |
Munnur D, Ahel I. Reversible mono-ADP-ribosylation of DNA breaks. The Febs Journal. 284: 4002-4016. PMID 29054115 DOI: 10.1111/Febs.14297 |
0.531 |
|
| 2017 |
Schuller M, Riedel K, Gibbs-Seymour I, Uth K, Sieg C, Gehring AP, Ahel I, Bracher F, Kessler BM, Elkins JM, Knapp S. Discovery of a selective allosteric inhibitor targeting macrodomain 2 of poly-adenosine-diphosphate-ribose polymerases 14. Acs Chemical Biology. PMID 28991428 DOI: 10.1021/Acschembio.7B00445 |
0.811 |
|
| 2017 |
Marjanović MP, Hurtado-Bagès S, Lassi M, Valero V, Malinverni R, Delage H, Navarro M, Corujo D, Guberovic I, Douet J, Gama-Perez P, Garcia-Roves PM, Ahel I, Ladurner AG, Yanes O, et al. MacroH2A1.1 regulates mitochondrial respiration by limiting nuclear NAD(+) consumption. Nature Structural & Molecular Biology. PMID 28991266 DOI: 10.1038/Nsmb.3481 |
0.646 |
|
| 2017 |
Palazzo L, James DI, Waddell ID, Ahel I. Studying Catabolism of Protein ADP-Ribosylation. Methods in Molecular Biology (Clifton, N.J.). 1608: 415-430. PMID 28695524 DOI: 10.1007/978-1-4939-6993-7_26 |
0.509 |
|
| 2017 |
Fontana P, Bonfiglio JJ, Palazzo L, Bartlett E, Matic I, Ahel I. Serine ADP-ribosylation reversal by the hydrolase ARH3. Elife. 6. PMID 28650317 DOI: 10.7554/Elife.28533 |
0.556 |
|
| 2017 |
Palazzo L, Mikoč A, Ahel I. ADP-ribosylation: new facets of an ancient modification. The Febs Journal. 284: 2932-2946. PMID 28383827 DOI: 10.1111/Febs.14078 |
0.482 |
|
| 2017 |
Bonfiglio JJ, Fontana P, Zhang Q, Colby T, Gibbs-Seymour I, Atanassov I, Bartlett E, Zaja R, Ahel I, Matic I. Serine ADP-Ribosylation Depends on HPF1. Molecular Cell. PMID 28190768 DOI: 10.1016/J.Molcel.2017.01.003 |
0.837 |
|
| 2016 |
Fehr AR, Channappanavar R, Jankevicius G, Fett C, Zhao J, Athmer J, Meyerholz DK, Ahel I, Perlman S. The Conserved Coronavirus Macrodomain Promotes Virulence and Suppresses the Innate Immune Response during Severe Acute Respiratory Syndrome Coronavirus Infection. Mbio. 7. PMID 27965448 DOI: 10.1128/Mbio.01721-16 |
0.751 |
|
| 2016 |
Jankevicius G, Ariza A, Ahel M, Ahel I. The Toxin-Antitoxin System DarTG Catalyzes Reversible ADP-Ribosylation of DNA. Molecular Cell. 64: 1109-1116. PMID 27939941 DOI: 10.1016/J.Molcel.2016.11.014 |
0.811 |
|
| 2016 |
Leidecker O, Bonfiglio JJ, Colby T, Zhang Q, Atanassov I, Zaja R, Palazzo L, Stockum A, Ahel I, Matic I. Serine is a new target residue for endogenous ADP-ribosylation on histones. Nature Chemical Biology. PMID 27723750 DOI: 10.1038/Nchembio.2180 |
0.482 |
|
| 2016 |
Posavec Marjanović M, Crawford K, Ahel I. PARP, transcription and chromatin modeling. Seminars in Cell & Developmental Biology. PMID 27677453 DOI: 10.1016/J.Semcdb.2016.09.014 |
0.389 |
|
| 2016 |
Lalić J, Posavec Marjanović M, Palazzo L, Perina D, Sabljić I, Žaja R, Colby T, Pleše B, Halasz M, Jankevicius G, Bucca G, Ahel M, Matić I, Ćetković H, Luić M, ... ... Ahel I, et al. Disruption of macrodomain protein SCO6735 increases antibiotic production in Streptomyces coelicolor. The Journal of Biological Chemistry. PMID 27634042 DOI: 10.1074/Jbc.M116.721894 |
0.798 |
|
| 2016 |
Gunn AR, Banos-Pinero B, Paschke P, Sanchez-Pulido L, Ariza A, Day J, Emrich M, Leys D, Ponting CP, Ahel I, Lakin ND. The role of ADP-ribosylation in regulating DNA interstrand crosslink repair. Journal of Cell Science. PMID 27587838 DOI: 10.1242/Jcs.193375 |
0.534 |
|
| 2016 |
Staples CJ, Barone G, Myers KN, Ganesh A, Gibbs-Seymour I, Patil AA, Beveridge RD, Daye C, Beniston R, Maslen S, Ahel I, Skehel JM, Collis SJ. MRNIP/C5orf45 Interacts with the MRN Complex and Contributes to the DNA Damage Response. Cell Reports. PMID 27568553 DOI: 10.1016/J.Celrep.2016.07.087 |
0.825 |
|
| 2016 |
Li C, Debing Y, Jankevicius G, Neyts J, Ahel I, Coutard B, Canard B. Viral Macro Domains Reverse Protein ADP-ribosylation. Journal of Virology. PMID 27440879 DOI: 10.1128/Jvi.00705-16 |
0.783 |
|
| 2016 |
Palazzo L, Daniels CM, Nettleship JE, Rahman N, McPherson RL, Ong SE, Kato K, Nureki O, Leung AK, Ahel I. ENPP1 processes protein ADP-ribosylation in vitro. The Febs Journal. PMID 27406238 DOI: 10.1111/Febs.13811 |
0.501 |
|
| 2016 |
Gibbs-Seymour I, Fontana P, Rack JGM, Ahel I. HPF1/C4orf27 Is a PARP-1-Interacting Protein that Regulates PARP-1 ADP-Ribosylation Activity. Molecular Cell. 62: 432-442. PMID 27067600 DOI: 10.1016/J.Molcel.2016.03.008 |
0.846 |
|
| 2016 |
Rack JG, Perina D, Ahel I. Macrodomains: Structure, Function, Evolution, and Catalytic Activities. Annual Review of Biochemistry. 85: 431-54. PMID 26844395 DOI: 10.1146/Annurev-Biochem-060815-014935 |
0.486 |
|
| 2016 |
Carter-O'Connell I, Jin H, Morgan RK, Zaja R, David LL, Ahel I, Cohen MS. Identifying Family-Member-Specific Targets of Mono-ARTDs by Using a Chemical Genetics Approach. Cell Reports. PMID 26774478 DOI: 10.1016/J.Celrep.2015.12.045 |
0.388 |
|
| 2015 |
Rack JG, Morra R, Barkauskaite E, Kraehenbuehl R, Ariza A, Qu Y, Ortmayer M, Leidecker O, Cameron DR, Matic I, Peleg AY, Leys D, Traven A, Ahel I. Identification of a Class of Protein ADP-Ribosylating Sirtuins in Microbial Pathogens. Molecular Cell. 59: 309-20. PMID 26166706 DOI: 10.1016/J.Molcel.2015.06.013 |
0.417 |
|
| 2015 |
Barkauskaite E, Jankevicius G, Ahel I. Structures and Mechanisms of Enzymes Employed in the Synthesis and Degradation of PARP-Dependent Protein ADP-Ribosylation. Molecular Cell. 58: 935-46. PMID 26091342 DOI: 10.1016/J.Molcel.2015.05.007 |
0.819 |
|
| 2015 |
Palazzo L, Thomas B, Jemth AS, Colby T, Leidecker O, Feijs KL, Zaja R, Loseva O, Puigvert JC, Matic I, Helleday T, Ahel I. Processing of protein ADP-ribosylation by Nudix hydrolases. The Biochemical Journal. 468: 293-301. PMID 25789582 DOI: 10.1042/Bj20141554 |
0.498 |
|
| 2015 |
Lambrecht MJ, Brichacek M, Barkauskaite E, Ariza A, Ahel I, Hergenrother PJ. Synthesis of dimeric ADP-ribose and its structure with human poly(ADP-ribose) glycohydrolase. Journal of the American Chemical Society. 137: 3558-64. PMID 25706250 DOI: 10.1021/Ja512528P |
0.481 |
|
| 2014 |
Vyas S, Matic I, Uchima L, Rood J, Zaja R, Hay RT, Ahel I, Chang P. Family-wide analysis of poly(ADP-ribose) polymerase activity. Nature Communications. 5: 4426. PMID 25043379 DOI: 10.1038/Ncomms5426 |
0.442 |
|
| 2014 |
Perina D, Mikoč A, Ahel J, Ćetković H, Žaja R, Ahel I. Distribution of protein poly(ADP-ribosyl)ation systems across all domains of life. Dna Repair. 23: 4-16. PMID 24865146 DOI: 10.1016/J.Dnarep.2014.05.003 |
0.47 |
|
| 2014 |
Tallis M, Morra R, Barkauskaite E, Ahel I. Poly(ADP-ribosyl)ation in regulation of chromatin structure and the DNA damage response Chromosoma. 123: 79-90. PMID 24162931 DOI: 10.1007/S00412-013-0442-9 |
0.526 |
|
| 2013 |
Barkauskaite E, Brassington A, Tan ES, Warwicker J, Dunstan MS, Banos B, Lafite P, Ahel M, Mitchison TJ, Ahel I, Leys D. Visualization of poly(ADP-ribose) bound to PARG reveals inherent balance between exo- and endo-glycohydrolase activities. Nature Communications. 4: 2164. PMID 23917065 DOI: 10.1038/Ncomms3164 |
0.407 |
|
| 2013 |
Barkauskaite E, Jankevicius G, Ladurner AG, Ahel I, Timinszky G. The recognition and removal of cellular poly(ADP-ribose) signals. The Febs Journal. 280: 3491-507. PMID 23711178 DOI: 10.1111/Febs.12358 |
0.828 |
|
| 2013 |
Sharifi R, Morra R, Appel CD, Tallis M, Chioza B, Jankevicius G, Simpson MA, Matic I, Ozkan E, Golia B, Schellenberg MJ, Weston R, Williams JG, Rossi MN, Galehdari H, ... ... Ahel I, et al. Deficiency of terminal ADP-ribose protein glycohydrolase TARG1/C6orf130 in neurodegenerative disease. The Embo Journal. 32: 1225-37. PMID 23481255 DOI: 10.1038/Emboj.2013.51 |
0.816 |
|
| 2012 |
Zaja R, Mikoč A, Barkauskaite E, Ahel I. Molecular Insights into Poly(ADP-ribose) Recognition and Processing. Biomolecules. 3: 1-17. PMID 24970154 DOI: 10.3390/biom3010001 |
0.425 |
|
| 2012 |
Dunstan MS, Barkauskaite E, Lafite P, Knezevic CE, Brassington A, Ahel M, Hergenrother PJ, Leys D, Ahel I. Structure and mechanism of a canonical poly(ADP-ribose) glycohydrolase. Nature Communications. 3: 878. PMID 22673905 DOI: 10.1038/Ncomms1889 |
0.504 |
|
| 2011 |
Tumbale P, Appel CD, Kraehenbuehl R, Robertson PD, Williams JS, Krahn J, Ahel I, Williams RS. Structure of an aprataxin-DNA complex with insights into AOA1 neurodegenerative disease. Nature Structural & Molecular Biology. 18: 1189-95. PMID 21984210 DOI: 10.1038/nsmb.2146 |
0.371 |
|
| 2011 |
Slade D, Dunstan MS, Barkauskaite E, Weston R, Lafite P, Dixon N, Ahel M, Leys D, Ahel I. The structure and catalytic mechanism of a poly(ADP-ribose) glycohydrolase. Nature. 477: 616-20. PMID 21892188 DOI: 10.1038/Nature10404 |
0.537 |
|
| 2011 |
Peterson FC, Chen D, Lytle BL, Rossi MN, Ahel I, Denu JM, Volkman BF. Orphan macrodomain protein (human C6orf130) is an O-acyl-ADP-ribose deacylase: solution structure and catalytic properties. The Journal of Biological Chemistry. 286: 35955-65. PMID 21849506 DOI: 10.1074/Jbc.M111.276238 |
0.432 |
|
| 2011 |
Chen D, Vollmar M, Rossi MN, Phillips C, Kraehenbuehl R, Slade D, Mehrotra PV, von Delft F, Crosthwaite SK, Gileadi O, Denu JM, Ahel I. Identification of macrodomain proteins as novel O-acetyl-ADP-ribose deacetylases. The Journal of Biological Chemistry. 286: 13261-71. PMID 21257746 DOI: 10.1074/Jbc.M110.206771 |
0.433 |
|
| 2011 |
Mehrotra PV, Ahel D, Ryan DP, Weston R, Wiechens N, Kraehenbuehl R, Owen-Hughes T, Ahel I. DNA repair factor APLF is a histone chaperone. Molecular Cell. 41: 46-55. PMID 21211722 DOI: 10.1016/J.Molcel.2010.12.008 |
0.837 |
|
| 2010 |
Eustermann S, Brockmann C, Mehrotra PV, Yang JC, Loakes D, West SC, Ahel I, Neuhaus D. Solution structures of the two PBZ domains from human APLF and their interaction with poly(ADP-ribose). Nature Structural & Molecular Biology. 17: 241-3. PMID 20098424 DOI: 10.1038/Nsmb.1747 |
0.627 |
|
| 2009 |
Ahel D, Horejsí Z, Wiechens N, Polo SE, Garcia-Wilson E, Ahel I, Flynn H, Skehel M, West SC, Jackson SP, Owen-Hughes T, Boulton SJ. Poly(ADP-ribose)-dependent regulation of DNA repair by the chromatin remodeling enzyme ALC1. Science (New York, N.Y.). 325: 1240-3. PMID 19661379 DOI: 10.1126/Science.1177321 |
0.838 |
|
| 2008 |
Rass U, Ahel I, West SC. Molecular mechanism of DNA deadenylation by the neurological disease protein aprataxin. The Journal of Biological Chemistry. 283: 33994-4001. PMID 18836178 DOI: 10.1074/Jbc.M807124200 |
0.668 |
|
| 2008 |
Ahel I, Ahel D, Matsusaka T, Clark AJ, Pines J, Boulton SJ, West SC. Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins. Nature. 451: 81-5. PMID 18172500 DOI: 10.1038/Nature06420 |
0.843 |
|
| 2007 |
Rass U, Ahel I, West SC. Defective DNA repair and neurodegenerative disease. Cell. 130: 991-1004. PMID 17889645 DOI: 10.1016/J.Cell.2007.08.043 |
0.585 |
|
| 2007 |
Rass U, Ahel I, West SC. Actions of aprataxin in multiple DNA repair pathways. The Journal of Biological Chemistry. 282: 9469-74. PMID 17276982 DOI: 10.1074/Jbc.M611489200 |
0.653 |
|
| 2006 |
Ahel I, Rass U, El-Khamisy SF, Katyal S, Clements PM, McKinnon PJ, Caldecott KW, West SC. The neurodegenerative disease protein aprataxin resolves abortive DNA ligation intermediates. Nature. 443: 713-6. PMID 16964241 DOI: 10.1038/Nature05164 |
0.647 |
|
| 2005 |
Ahel I, Mikoc A, Gamulin V. recA gene expression in a streptomycete is mediated by the unusual C-terminus of RecA protein. Fems Microbiology Letters. 248: 119-24. PMID 15953699 DOI: 10.1016/J.Femsle.2005.05.030 |
0.373 |
|
| 2004 |
Ambrogelly A, Kamtekar S, Sauerwald A, Ruan B, Tumbula-Hansen D, Kennedy D, Ahel I, Söll D. Cys-tRNACys formation and cysteine biosynthesis in methanogenic archaea: two faces of the same problem? Cellular and Molecular Life Sciences. 61: 2437-2445. PMID 15526152 DOI: 10.1007/S00018-004-4194-9 |
0.612 |
|
| 2004 |
Gamulin V, Cetkovic H, Ahel I. Identification of a promoter motif regulating the major DNA damage response mechanism of Mycobacterium tuberculosis. Fems Microbiology Letters. 238: 57-63. PMID 15336403 DOI: 10.1016/J.Femsle.2004.07.017 |
0.461 |
|
| 2004 |
Korencic D, Ahel I, Schelert J, Sacher M, Ruan B, Stathopoulos C, Blum P, Ibba M, Söll D. A freestanding proofreading domain is required for protein synthesis quality control in Archaea. Proceedings of the National Academy of Sciences of the United States of America. 101: 10260-5. PMID 15240874 DOI: 10.1073/Pnas.0403926101 |
0.644 |
|
| 2003 |
Ahel I, Korencic D, Ibba M, Söll D. Trans-editing of mischarged tRNAs. Proceedings of the National Academy of Sciences of the United States of America. 100: 15422-7. PMID 14663147 DOI: 10.1073/Pnas.2136934100 |
0.664 |
|
| 2003 |
Salazar JC, Ahel I, Orellana O, Tumbula-Hansen D, Krieger R, Daniels L, Söll D. Coevolution of an aminoacyl-tRNA synthetase with its tRNA substrates. Proceedings of the National Academy of Sciences of the United States of America. 100: 13863-8. PMID 14615592 DOI: 10.1073/Pnas.1936123100 |
0.634 |
|
| 2003 |
Waters E, Hohn MJ, Ahel I, Graham DE, Adams MD, Barnstead M, Beeson KY, Bibbs L, Bolanos R, Keller M, Kretz K, Lin X, Mathur E, Ni J, Podar M, et al. The genome of Nanoarchaeum equitans: insights into early archaeal evolution and derived parasitism. Proceedings of the National Academy of Sciences of the United States of America. 100: 12984-8. PMID 14566062 DOI: 10.1073/Pnas.1735403100 |
0.622 |
|
| 2002 |
Ambrogelly A, Ahel I, Polycarpo C, Bunjun-Srihari S, Krett B, Jacquin-Becker C, Ruan B, Köhrer C, Stathopoulos C, RajBhandary UL, Söll D. Methanocaldococcus jannaschii prolyl-tRNA synthetase charges tRNA(Pro) with cysteine. The Journal of Biological Chemistry. 277: 34749-54. PMID 12130658 DOI: 10.1074/Jbc.M206929200 |
0.543 |
|
| 2002 |
Ahel I, Stathopoulos C, Ambrogelly A, Sauerwald A, Toogood H, Hartsch T, Söll D. Cysteine activation is an inherent in vitro property of prolyl-tRNA synthetases. The Journal of Biological Chemistry. 277: 34743-8. PMID 12130657 DOI: 10.1074/Jbc.M206928200 |
0.641 |
|
| 2002 |
Feng L, Stathopoulos C, Ahel I, Mitra A, Tumbula-Hansen D, Hartsch T, Söll D. Aminoacyl-tRNA formation in the extreme thermophile Thermus thermophilus Extremophiles. 6: 167-174. PMID 12013438 DOI: 10.1007/S007920100245 |
0.642 |
|
| 2002 |
Ahel I, Vujaklija D, Mikoc A, Gamulin V. Transcriptional analysis of the recA gene in Streptomyces rimosus: identification of the new type of promoter. Fems Microbiology Letters. 209: 133-7. PMID 12007666 DOI: 10.1111/J.1574-6968.2002.Tb11121.X |
0.358 |
|
| 2002 |
Jacquin-Becker C, Ahel I, Ambrogelly A, Ruan B, Söll D, Stathopoulos C. Cysteinyl-tRNA formation and prolyl-tRNA synthetase. Febs Letters. 514: 34-6. PMID 11904177 DOI: 10.1016/S0014-5793(02)02331-1 |
0.634 |
|
| 2001 |
Stathopoulos C, Ahel I, Ali K, Ambrogelly A, Becker H, Bunjun S, Feng L, Herring S, Jacquin-Becker C, Kobayashi H, Korencic D, Krett B, Mejlhede N, Min B, Nakano H, et al. Aminoacyl-tRNA synthesis: a postgenomic perspective. Cold Spring Harbor Symposia On Quantitative Biology. 66: 175-83. PMID 12762020 DOI: 10.1101/Sqb.2001.66.175 |
0.751 |
|
| 2001 |
Ruan B, Ahel I, Ambrogelly A, Becker HD, Bunjun S, Feng L, Tumbula-Hansen D, Ibba M, Korencic D, Kobayashi H, Jacquin-Becker C, Mejlhede N, Min B, Raczniak G, Rinehart J, et al. Genomics and the evolution of aminoacyl-tRNA synthesis. Acta Biochimica Polonica. 48: 313-21. PMID 11732603 DOI: 10.18388/Abp.2001_3917 |
0.785 |
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