On the public citation graph

https://doi.org/10.2139/ssrn.4677489

0 signed · 79 inferred · view as graph

Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.

Is this your work? Sign in with ORCID and put your name on the claims that are yours.
Claim with ORCID
Reference health. See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.
See reference health

What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/anie.200501023openalex-extracted
Protein Posttranslational Modifications: The Chemistry of Proteome Diversifications
inferredcites →https://doi.org/10.1002/j.1460-2075.1988.tb02783.xopenalex-extracted
At least 60 ADP‐ribosylated variant histones are present in nuclei from dimethylsulfate‐treated and untreated cells.
inferredcites →https://doi.org/10.1002/pmic.201400217openalex-extracted
Proteomics approaches to identify mono‐(ADP‐ribosyl)ated and poly(ADP‐ribosyl)ated proteins
inferredcites →https://doi.org/10.1006/excr.2001.5263openalex-extracted
Importance of Poly(ADP-Ribose) Glycohydrolase in the Control of Poly(ADP-Ribose) Metabolism
inferredcites →https://doi.org/10.1007/978-1-0716-2891-1_15openalex-extracted
Characterizing ADP-Ribosylation Sites Using Af1521 Enrichment Coupled to ETD-Based Mass Spectrometry
inferredcites →https://doi.org/10.1007/978-1-4939-6993-7_11openalex-extracted
Proteome-Wide Identification of In Vivo ADP-Ribose Acceptor Sites by Liquid Chromatography–Tandem Mass Spectrometry
inferredcites →https://doi.org/10.1016/0167-4889(89)90234-6openalex-extracted
Hydrogen peroxide insult in cultured mammalian cells: relationships between DNA single-strand breakage, poly(ADP-ribose) metabolism and cell killing
inferredcites →https://doi.org/10.1016/0968-0004(94)90280-1openalex-extracted
Poly(ADP-ribose) polymerase: a molecular nick-sensor
inferredcites →https://doi.org/10.1016/j.ccell.2018.05.008openalex-extracted
Selective Loss of PARG Restores PARylation and Counteracts PARP Inhibitor-Mediated Synthetic Lethality
inferredcites →https://doi.org/10.1016/j.ccr.2006.10.008openalex-extracted
A collection of breast cancer cell lines for the study of functionally distinct cancer subtypes
inferredcites →https://doi.org/10.1016/j.cell.2010.12.001openalex-extracted
A Tissue-Specific Atlas of Mouse Protein Phosphorylation and Expression
inferredcites →https://doi.org/10.1016/j.cell.2012.05.036openalex-extracted
Systematic Functional Prioritization of Protein Posttranslational Modifications
inferredcites →https://doi.org/10.1016/j.cell.2023.08.030openalex-extracted
ADP-ribosylation from molecular mechanisms to therapeutic implications
inferredcites →https://doi.org/10.1016/j.celrep.2017.10.106openalex-extracted
A Cell-Line-Specific Atlas of PARP-Mediated Protein Asp/Glu-ADP-Ribosylation in Breast Cancer
inferredcites →https://doi.org/10.1016/j.celrep.2018.07.083openalex-extracted
Systems-wide Analysis of Serine ADP-Ribosylation Reveals Widespread Occurrence and Site-Specific Overlap with Phosphorylation
inferredcites →https://doi.org/10.1016/j.celrep.2018.08.092openalex-extracted
Interplay of Histone Marks with Serine ADP-Ribosylation
inferredcites →https://doi.org/10.1016/j.cels.2017.05.009openalex-extracted
An Optimized Shotgun Strategy for the Rapid Generation of Comprehensive Human Proteomes
inferredcites →https://doi.org/10.1016/j.euo.2020.07.005openalex-extracted
When and How to Use PARP Inhibitors in Prostate Cancer: A Systematic Review of the Literature with an Update on On-Going Trials
inferredcites →https://doi.org/10.1016/j.jmb.2011.01.034openalex-extracted
The DNA-Binding Domain of Human PARP-1 Interacts with DNA Single-Strand Breaks as a Monomer through Its Second Zinc Finger
inferredcites →https://doi.org/10.1016/j.molcel.2011.08.025openalex-extracted
Systematic and Quantitative Assessment of the Ubiquitin-Modified Proteome
inferredcites →https://doi.org/10.1016/j.molcel.2013.08.026openalex-extracted
Proteome-wide Identification of Poly(ADP-Ribosyl)ation Targets in Different Genotoxic Stress Responses
inferredcites →https://doi.org/10.1016/j.molcel.2016.03.008openalex-extracted
HPF1/C4orf27 Is a PARP-1-Interacting Protein that Regulates PARP-1 ADP-Ribosylation Activity
inferredcites →https://doi.org/10.1016/j.molcel.2017.01.003openalex-extracted
Serine ADP-Ribosylation Depends on HPF1
inferredcites →https://doi.org/10.1016/s0021-9258(17)30177-1openalex-extracted
ADP ribosylation of rat liver lysine-rich histone in vitro.
inferredcites →https://doi.org/10.1016/s0092-8674(00)00034-9openalex-extracted
Mitotic Phosphorylation of Histone H3 Is Governed by Ipl1/aurora Kinase and Glc7/PP1 Phosphatase in Budding Yeast and Nematodes
inferredcites →https://doi.org/10.1021/acs.analchem.6b03365openalex-extracted
Combining Higher-Energy Collision Dissociation and Electron-Transfer/Higher-Energy Collision Dissociation Fragmentation in a Product-Dependent Manner Confidently Assigns Proteomewide ADP-Ribose Acceptor Sites
inferredcites →https://doi.org/10.1021/acs.chemrev.7b00122openalex-extracted
ADP-Ribosylation, a Multifaceted Posttranslational Modification Involved in the Control of Cell Physiology in Health and Disease
inferredcites →https://doi.org/10.1021/acs.jproteome.2c00651openalex-extracted
Cytoscape stringApp 2.0: Analysis and Visualization of Heterogeneous Biological Networks
inferredcites →https://doi.org/10.1038/bjc.2012.451openalex-extracted
Patterns of genomic loss of heterozygosity predict homologous recombination repair defects in epithelial ovarian cancer
inferredcites →https://doi.org/10.1038/nature03443openalex-extracted
Specific killing of BRCA2-deficient tumours with inhibitors of poly(ADP-ribose) polymerase
inferredcites →https://doi.org/10.1038/nature03445openalex-extracted
Targeting the DNA repair defect in BRCA mutant cells as a therapeutic strategy
inferredcites →https://doi.org/10.1038/nbt1252openalex-extracted
Post-translational modifications in the context of therapeutic proteins
inferredcites →https://doi.org/10.1038/nchembio.2180openalex-extracted
Serine is a new target residue for endogenous ADP-ribosylation on histones
inferredcites →https://doi.org/10.1038/ncomms12917openalex-extracted
Proteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue
inferredcites →https://doi.org/10.1038/nm.4292openalex-extracted
HRDetect is a predictor of BRCA1 and BRCA2 deficiency based on mutational signatures
inferredcites →https://doi.org/10.1038/nmeth.2603openalex-extracted
Site-specific characterization of the Asp- and Glu-ADP-ribosylated proteome
inferredcites →https://doi.org/10.1038/nmeth.3901openalex-extracted
The Perseus computational platform for comprehensive analysis of (prote)omics data
inferredcites →https://doi.org/10.1038/nmeth1109-786openalex-extracted
Improved visualization of protein consensus sequences by iceLogo
inferredcites →https://doi.org/10.1038/nrm.2017.53openalex-extracted
The multifaceted roles of PARP1 in DNA repair and chromatin remodelling
inferredcites →https://doi.org/10.1038/nrm1963openalex-extracted
Poly(ADP-ribose): novel functions for an old molecule
inferredcites →https://doi.org/10.1038/nsmb.3366openalex-extracted
Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation
inferredcites →https://doi.org/10.1038/s41391-020-0233-3openalex-extracted
PARP inhibitors as a new therapeutic option in metastatic prostate cancer: a systematic review
inferredcites →https://doi.org/10.1038/s41467-021-26172-4openalex-extracted
The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome
inferredcites →https://doi.org/10.1038/s41467-023-38793-yopenalex-extracted
Serine ADP-ribosylation in Drosophila provides insights into the evolution of reversible ADP-ribosylation signalling
inferredcites →https://doi.org/10.1038/s41523-018-0066-6openalex-extracted
Migrating the SNP array-based homologous recombination deficiency measures to next generation sequencing data of breast cancer
inferredcites →https://doi.org/10.1038/s41571-021-00532-xopenalex-extracted
Understanding and overcoming resistance to PARP inhibitors in cancer therapy
inferredcites →https://doi.org/10.1038/s41587-019-0344-3openalex-extracted
The functional landscape of the human phosphoproteome
inferredcites →https://doi.org/10.1038/s41589-018-0097-1openalex-extracted
Acetylation blocks DNA damage–induced chromatin ADP-ribosylation
inferredcites →https://doi.org/10.1038/sj.emboj.7600664openalex-extracted
The macro domain is an ADP‐ribose binding module
inferredcites →https://doi.org/10.1038/sj.onc.1202932openalex-extracted
Loss of USF transcriptional activity in breast cancer cell lines
inferredcites →https://doi.org/10.1074/jbc.m110.202507openalex-extracted
Crystal Structures of Poly(ADP-ribose) Polymerase-1 (PARP-1) Zinc Fingers Bound to DNA
inferredcites →https://doi.org/10.1074/jbc.m111.246116openalex-extracted
The E-box Binding Factors Max/Mnt, MITF, and USF1 Act Coordinately with FoxO to Regulate Expression of Proapoptotic and Cell Cycle Control Genes by Phosphatidylinositol 3-Kinase/Akt/Glycogen Synthase Kinase 3 Signaling
inferredcites →https://doi.org/10.1074/jbc.m706734200openalex-extracted
PARP1-dependent Kinetics of Recruitment of MRE11 and NBS1 Proteins to Multiple DNA Damage Sites
inferredcites →https://doi.org/10.1074/mcp.m113.031591openalex-extracted
Accurate Proteome-wide Label-free Quantification by Delayed Normalization and Maximal Peptide Ratio Extraction, Termed MaxLFQ
inferredcites →https://doi.org/10.1074/mcp.tir119.001315openalex-extracted
An Advanced Strategy for Comprehensive Profiling of ADP-ribosylation Sites Using Mass Spectrometry-based Proteomics*
inferredcites →https://doi.org/10.1093/bioinformatics/btac757openalex-extracted
GSEApy: a comprehensive package for performing gene set enrichment analysis in Python
inferredcites →https://doi.org/10.1093/nar/gkw1246openalex-extracted
Overlapping roles for PARP1 and PARP2 in the recruitment of endogenous XRCC1 and PNKP into oxidized chromatin
inferredcites →https://doi.org/10.1093/nar/gkx446openalex-extracted
Mass spectrometry for serine ADP-ribosylation? Think o-glycosylation!
inferredcites →https://doi.org/10.1101/2023.09.04.556166openalex-extracted
Mitotic chromatin marking governs asymmetric segregation of DNA damage
inferredcites →https://doi.org/10.1101/gad.183509.111openalex-extracted
On PAR with PARP: cellular stress signaling through poly(ADP-ribose) and PARP-1
inferredcites →https://doi.org/10.1101/gr.080259.108openalex-extracted
A sequence-level map of chromosomal breakpoints in the MCF-7 breast cancer cell line yields insights into the evolution of a cancer genome
inferredcites →https://doi.org/10.1111/febs.16142openalex-extracted
ADP‐ribosyltransferases, an update on function and nomenclature
inferredcites →https://doi.org/10.1111/j.1432-1033.1985.tb08650.xopenalex-extracted
Sequential ADP‐ribosylation pattern of nucleosomal histones
inferredcites →https://doi.org/10.1126/science.1175371openalex-extracted
Lysine Acetylation Targets Protein Complexes and Co-Regulates Major Cellular Functions
inferredcites →https://doi.org/10.1126/science.1216338openalex-extracted
Structural Basis for DNA Damage–Dependent Poly(ADP-ribosyl)ation by Human PARP-1
inferredcites →https://doi.org/10.1126/science.aaf2144openalex-extracted
Evolution of protein phosphorylation across 18 fungal species
inferredcites →https://doi.org/10.1126/scisignal.aaf7329openalex-extracted
Proteome-wide analysis of arginine monomethylation reveals widespread occurrence in human cells
inferredcites →https://doi.org/10.1158/0008-5472.can-12-1470openalex-extracted
Ploidy and Large-Scale Genomic Instability Consistently Identify Basal-like Breast Carcinomas with BRCA1/2 Inactivation
inferredcites →https://doi.org/10.1158/1078-0432.ccr-15-2477openalex-extracted
Homologous Recombination Deficiency (HRD) Score Predicts Response to Platinum-Containing Neoadjuvant Chemotherapy in Patients with Triple-Negative Breast Cancer
inferredcites →https://doi.org/10.1158/1078-0432.ccr-19-2135openalex-extracted
Detection of Molecular Signatures of Homologous Recombination Deficiency in Prostate Cancer with or without BRCA1/2 Mutations
inferredcites →https://doi.org/10.1158/2159-8290.cd-11-0206openalex-extracted
Telomeric Allelic Imbalance Indicates Defective DNA Repair and Sensitivity to DNA-Damaging Agents
inferredcites →https://doi.org/10.1186/1471-2105-14-128openalex-extracted
Enrichr: interactive and collaborative HTML5 gene list enrichment analysis tool
inferredcites →https://doi.org/10.1242/dmm.023762openalex-extracted
Drosophilatools and assays for the study of human diseases
inferredcites →https://doi.org/10.3389/fphar.2015.00003openalex-extracted
Protein kinases as switches for the function of upstream stimulatory factors: implications for tissue injury and cancer
inferredcites →https://doi.org/10.3390/cancers13050946openalex-extracted
Modification of Homologous Recombination Deficiency Score Threshold and Association with Long-Term Survival in Epithelial Ovarian Cancer
inferredcites →https://doi.org/10.3390/jcm9040940openalex-extracted
Response of Breast Cancer Cells to PARP Inhibitors Is Independent of BRCA Status
inferredcites →https://doi.org/10.3892/ijo.2015.3003openalex-extracted
The PARP inhibitor AZD2281 (Olaparib) induces autophagy/mitophagy in BRCA1 and BRCA2 mutant breast cancer cells
inferredcites →https://doi.org/10.7554/elife.28533openalex-extracted
Serine ADP-ribosylation reversal by the hydrolase ARH3
inferredcites →https://doi.org/10.7554/elife.34334openalex-extracted
Serine is the major residue for ADP-ribosylation upon DNA damage
Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.