| Delineation of ADPRHL2 Variants: Report of Two New Patients with Review of the Literature. | Delineation of ADPRHL2 Variants: Report of Two New Patients with Review of the Literature.
Öz Yıldız S, Yalnızoğlu D, Şimsek Kiper PÖ, Göçmen R, Soğukpınar M, Utine GE, Haliloğlu G. | 07/12/2024 |
| The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome. | The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome.
Hendriks IA, Buch-Larsen SC, Prokhorova E, Elsborg JD, Rebak AKLFS, Zhu K, Ahel D, Lukas C, Ahel I, Nielsen ML., Free PMC Article | 11/6/2021 |
| Structural and biochemical analysis of human ADP-ribosyl-acceptor hydrolase 3 reveals the basis of metal selectivity and different roles for the two magnesium ions. | Structural and biochemical analysis of human ADP-ribosyl-acceptor hydrolase 3 reveals the basis of metal selectivity and different roles for the two magnesium ions.
Pourfarjam Y, Ma Z, Kurinov I, Moss J, Kim IK., Free PMC Article | 08/21/2021 |
| Unrestrained poly-ADP-ribosylation provides insights into chromatin regulation and human disease. | Unrestrained poly-ADP-ribosylation provides insights into chromatin regulation and human disease.
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, Mangerich A, Ahel D, Baets J, O'Sullivan RJ, Ahel I., Free PMC Article | 07/24/2021 |
| AI26 inhibits the ADP-ribosylhydrolase ARH3 and suppresses DNA damage repair. | AI26 inhibits the ADP-ribosylhydrolase ARH3 and suppresses DNA damage repair.
Liu X, Xie R, Yu LL, Chen SH, Yang X, Singh AK, Li H, Wu C, Yu X., Free PMC Article | 02/6/2021 |
| Pathogenic ARH3 mutations result in ADP-ribose chromatin scars during DNA strand break repair. | Pathogenic ARH3 mutations result in ADP-ribose chromatin scars during DNA strand break repair.
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., Free PMC Article | 09/12/2020 |
| Study identified a family with an ARH3 gene mutation that resulted in a truncated, inactive protein. The 8-year-old proband exhibited a progressive neurodegeneration phenotype. Parthanatos was observed in neurons of the patient's deceased sibling, and an older sibling exhibited a mild behavioral phenotype. Patient's fibroblasts were more sensitive to H2O2 stress-induced poly(ADP-ribose) accumulation and cell death. | PARP1 inhibition alleviates injury in ARH3-deficient mice and human cells.
Mashimo M, Bu X, Aoyama K, Kato J, Ishiwata-Endo H, Stevens LA, Kasamatsu A, Wolfe LA, Toro C, Adams D, Markello T, Gahl WA, Moss J., Free PMC Article | 05/16/2020 |
| Here, the authors show that serine ADP-ribosylation represents the major fraction of ADP-ribosylation synthesized after DNA damage in mammalian cells and that globally serine ADP-ribosylation is dependent on HPF1, PARP1 and ARH3. In the absence of HPF1, glutamate/aspartate becomes the main target residues for ADP-ribosylation. | Serine is the major residue for ADP-ribosylation upon DNA damage.
Palazzo L, Leidecker O, Prokhorova E, Dauben H, Matic I, Ahel I., Free PMC Article | 07/20/2019 |
| ADPRHL2 was virtually absent in available affected individuals' fibroblasts. | Bi-allelic ADPRHL2 Mutations Cause Neurodegeneration with Developmental Delay, Ataxia, and Axonal Neuropathy.
Danhauser K, Alhaddad B, Makowski C, Piekutowska-Abramczuk D, Syrbe S, Gomez-Ospina N, Manning MA, Kostera-Pruszczyk A, Krahn-Peper C, Berutti R, Kovács-Nagy R, Gusic M, Graf E, Laugwitz L, Röblitz M, Wroblewski A, Hartmann H, Das AM, Bültmann E, Fang F, Xu M, Schatz UA, Karall D, Zellner H, Haberlandt E, Feichtinger RG, Mayr JA, Meitinger T, Prokisch H, Strom TM, Płoski R, Hoffmann GF, Pronicki M, Bonnen PE, Morlot S, Haack TB., Free PMC Article | 05/18/2019 |
| study provides structural and functional insights into the molecular mechanism by which ARH3 hydrolyzes the ADP-ribosyl group from serine and contributes to DNA damage repair | Structure-function analyses reveal the mechanism of the ARH3-dependent hydrolysis of ADP-ribosylation.
Wang M, Yuan Z, Xie R, Ma Y, Liu X, Yu X., Free PMC Article | 04/13/2019 |
| Study results establish ARH3 as a serine mono-ADP-ribosylhydrolase and as an important regulator of the basal and stress-induced ADP-ribosylome. | Proteomic analyses identify ARH3 as a serine mono-ADP-ribosylhydrolase.
Abplanalp J, Leutert M, Frugier E, Nowak K, Feurer R, Kato J, Kistemaker HVA, Filippov DV, Moss J, Caflisch A, Hottiger MO., Free PMC Article | 10/6/2018 |
| By screening for the hydrolase that is responsible for the reversal of Ser-ADP ribosilation, the authors identified ARH3/ADPRHL2 as capable of efficiently and specifically removing Ser-ADP ribosilation of histones and other proteins. | Serine ADP-ribosylation reversal by the hydrolase ARH3.
Fontana P, Bonfiglio JJ, Palazzo L, Bartlett E, Matic I, Ahel I., Free PMC Article | 05/5/2018 |
| ADP-ribosylhydrolase 3 (ARH3), not poly(ADP-ribose) glycohydrolase (PARG) isoforms, is responsible for degradation of mitochondrial matrix-associated poly(ADP-ribose). | ADP-ribosylhydrolase 3 (ARH3), not poly(ADP-ribose) glycohydrolase (PARG) isoforms, is responsible for degradation of mitochondrial matrix-associated poly(ADP-ribose).
Niere M, Mashimo M, Agledal L, Dölle C, Kasamatsu A, Kato J, Moss J, Ziegler M., Free PMC Article | 07/14/2012 |
| poly(ADP-ribose) glycohydrolase ARH3 hydrolyzed O-acetyl-ADP-ribose to produce ADP-ribose in a time- and Mg(2+)-dependent reaction and thus could participate in two signaling pathways | The 39-kDa poly(ADP-ribose) glycohydrolase ARH3 hydrolyzes O-acetyl-ADP-ribose, a product of the Sir2 family of acetyl-histone deacetylases.
Ono T, Kasamatsu A, Oka S, Moss J., Free PMC Article | 01/21/2010 |
| ARH3 has poly(ADP-ribose) glycohydrolase activity but is structurally unrelated to poly(ADP-ribose) glycohydrolase | Identification and characterization of a mammalian 39-kDa poly(ADP-ribose) glycohydrolase.
Oka S, Kato J, Moss J. | 01/21/2010 |
| cloning, recombinant production, purification and crystallization of ARH3 consisting of 347 amino-acid residues | Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of human ARH3, the first eukaryotic protein-ADP-ribosylhydrolase.
Kernstock S, Koch-Nolte F, Mueller-Dieckmann J, Weiss MS, Mueller-Dieckmann C., Free PMC Article | 01/21/2010 |
| The molecular architecture of human ARH3 constitutes the archetype of an all-alpha-helical protein fold and suggests reversibility mechanisms of protein ADP-ribosylation. | The structure of human ADP-ribosylhydrolase 3 (ARH3) provides insights into the reversibility of protein ADP-ribosylation.
Mueller-Dieckmann C, Kernstock S, Lisurek M, von Kries JP, Haag F, Weiss MS, Koch-Nolte F., Free PMC Article | 01/21/2010 |