On the public citation graph
A Cell-Line-Specific Atlas of PARP-Mediated Protein Asp/Glu-ADP-Ribosylation in Breast Cancer
0 signed · 127 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.
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known work and none has been retracted — and get a dated CiteStamped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.
What this work says
Outgoing claims: the papers this work cites, builds on, or argues with.
inferredcites →https://doi.org/10.1007/s00439-008-0529-1openalex-snapshot
Hereditary breast cancer: new genetic developments, new therapeutic avenues
inferredcites →https://doi.org/10.1007/s10549-009-0363-8openalex-snapshot
Expression of estrogenicity genes in a lineage cell culture model of human breast cancer progression
inferredcites →https://doi.org/10.1016/0006-291x(87)90543-2openalex-snapshot
Molecular cloning of cDNA for human poly(ADP-ribose) polymerase and expression of its gene during HL-60 cell differentiation
inferredcites →https://doi.org/10.1016/0006-291x(87)90921-1openalex-snapshot
Nucleotide sequence of a full-length cDNA for human fibroblast poly(ADP-ribose) polymerase
inferredcites →https://doi.org/10.1016/j.bbagrm.2011.12.001openalex-snapshot
mRNA export and the TREX complex
inferredcites →https://doi.org/10.1016/j.cell.2006.09.048openalex-snapshot
GATA-3 Maintains the Differentiation of the Luminal Cell Fate in the Mammary Gland
inferredcites →https://doi.org/10.1016/j.cell.2010.12.001openalex-snapshot
A Tissue-Specific Atlas of Mouse Protein Phosphorylation and Expression
inferredcites →https://doi.org/10.1016/j.celrep.2014.08.009openalex-snapshot
Basal Activity of a PARP1-NuA4 Complex Varies Dramatically across Cancer Cell Lines
inferredcites →https://doi.org/10.1016/j.molcel.2010.06.017openalex-snapshot
The PARP Side of the Nucleus: Molecular Actions, Physiological Outcomes, and Clinical Targets
inferredcites →https://doi.org/10.1016/j.molcel.2015.01.037openalex-snapshot
RNA Regulation by Poly(ADP-Ribose) Polymerases
inferredcites →https://doi.org/10.1016/j.molcel.2015.06.012openalex-snapshot
The Promise of Proteomics for the Study of ADP-Ribosylation
inferredcites →https://doi.org/10.1016/j.molcel.2016.03.008openalex-snapshot
HPF1/C4orf27 Is a PARP-1-Interacting Protein that Regulates PARP-1 ADP-Ribosylation Activity
inferredcites →https://doi.org/10.1016/s0021-9258(18)68594-1openalex-snapshot
Immunoquantitation and size determination of intrinsic poly(ADP-ribose) polymerase from acid precipitates. An analysis of the in vivo status in mammalian species and in lower eukaryotes.
inferredcites →https://doi.org/10.1016/s0378-1119(98)00529-0openalex-snapshot
Poly(ADP-ribose) polymerase interacts with novel Drosophila ribosomal proteins, L22 and L23a, with unique histone-like amino-terminal extensions
inferredcites →https://doi.org/10.1021/acs.jproteome.5b00819openalex-snapshot
Quantitative Secretomic Analysis Identifies Extracellular Protein Factors That Modulate the Metastatic Phenotype of Non-Small Cell Lung Cancer
inferredcites →https://doi.org/10.1021/acs.jproteome.7b00140openalex-snapshot
Global Phosphoproteomic Analysis of Insulin/Akt/mTORC1/S6K Signaling in Rat Hepatocytes
inferredcites →https://doi.org/10.1021/pr401032qopenalex-snapshot
Phosphoproteomic Approach to Characterize Protein Mono- and Poly(ADP-ribosyl)ation Sites from Cells
inferredcites →https://doi.org/10.1038/283593a0openalex-snapshot
(ADP-ribose)n participates in DNA excision repair
inferredcites →https://doi.org/10.1038/35030160openalex-snapshot
The protein Aly links pre-messenger-RNA splicing to nuclear export in metazoans
inferredcites →https://doi.org/10.1038/nature03443openalex-snapshot
Specific killing of BRCA2-deficient tumours with inhibitors of poly(ADP-ribose) polymerase
inferredcites →https://doi.org/10.1038/nature03445openalex-snapshot
Targeting the DNA repair defect in BRCA mutant cells as a therapeutic strategy
inferredcites →https://doi.org/10.1038/nature14427openalex-snapshot
Structure of the human 80S ribosome
inferredcites →https://doi.org/10.1038/nbt.2121openalex-snapshot
Family-wide chemical profiling and structural analysis of PARP and tankyrase inhibitors
inferredcites →https://doi.org/10.1038/ncb1530openalex-snapshot
Gata-3 is an essential regulator of mammary-gland morphogenesis and luminal-cell differentiation
inferredcites →https://doi.org/10.1038/nchembio.2180openalex-snapshot
Serine is a new target residue for endogenous ADP-ribosylation on histones
inferredcites →https://doi.org/10.1038/ncomms12917openalex-snapshot
Proteome-wide identification of the endogenous ADP-ribosylome of mammalian cells and tissue
inferredcites →https://doi.org/10.1038/nmeth.2603openalex-snapshot
Site-specific characterization of the Asp- and Glu-ADP-ribosylated proteome
inferredcites →https://doi.org/10.1038/nprot.2008.211openalex-snapshot
Systematic and integrative analysis of large gene lists using DAVID bioinformatics resources
inferredcites →https://doi.org/10.1038/nrm3376openalex-snapshot
New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs
inferredcites →https://doi.org/10.1038/onc.2014.295openalex-snapshot
The role of poly(ADP-ribosyl)ation in DNA damage response and cancer chemotherapy
inferredcites →https://doi.org/10.1038/sj.emboj.7600070openalex-snapshot
Human Fip1 is a subunit of CPSF that binds to U‐rich RNA elements and stimulates poly(A) polymerase
inferredcites →https://doi.org/10.1042/0264-6021:3420249openalex-snapshot
Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
inferredcites →https://doi.org/10.1042/bj3420249openalex-snapshot
Poly(ADP-ribosyl)ation reactions in the regulation of nuclear functions
inferredcites →https://doi.org/10.1056/nejmoa0900212openalex-snapshot
Inhibition of Poly(ADP-Ribose) Polymerase in Tumors from BRCA Mutation Carriers
inferredcites →https://doi.org/10.1073/pnas.84.5.1224openalex-snapshot
Cloning and expression of cDNA for human poly(ADP-ribose) polymerase.
inferredcites →https://doi.org/10.1074/mcp.m111.009654openalex-snapshot
Correct Interpretation of Comprehensive Phosphorylation Dynamics Requires Normalization by Protein Expression Changes
inferredcites →https://doi.org/10.1074/mcp.m900375-mcp200openalex-snapshot
A Dual Pressure Linear Ion Trap Orbitrap Instrument with Very High Sequencing Speed
inferredcites →https://doi.org/10.1074/mcp.o116.065623openalex-snapshot
New Quantitative Mass Spectrometry Approaches Reveal Different ADP-ribosylation Phases Dependent On the Levels of Oxidative Stress
inferredcites →https://doi.org/10.1093/nar/gkr965openalex-snapshot
AnimalTFDB: a comprehensive animal transcription factor database
inferredcites →https://doi.org/10.1093/nar/gku1003openalex-snapshot
STRING v10: protein–protein interaction networks, integrated over the tree of life
inferredcites →https://doi.org/10.1093/nar/gkv1344openalex-snapshot
The Pfam protein families database: towards a more sustainable future
inferredcites →https://doi.org/10.1093/nar/gkx565openalex-snapshot
The role of poly ADP-ribosylation in the first wave of DNA damage response
inferredcites →https://doi.org/10.1097/ppo.0b013e3181d24ff7openalex-snapshot
Triple-Negative Breast Cancer
inferredcites →https://doi.org/10.1101/gad.552910openalex-snapshot
Cooperative interaction between retinoic acid receptor-α and estrogen receptor in breast cancer
inferredcites →https://doi.org/10.1101/gr.1239303openalex-snapshot
Cytoscape: A Software Environment for Integrated Models of Biomolecular Interaction Networks
inferredcites →https://doi.org/10.1101/gr.139469.112openalex-snapshot
GATA3 acts upstream of FOXA1 in mediating ESR1 binding by shaping enhancer accessibility
inferredcites →https://doi.org/10.1126/science.aaf7865openalex-snapshot
Chemical genetic discovery of PARP targets reveals a role for PARP-1 in transcription elongation
inferredcites →https://doi.org/10.1126/science.aam7344openalex-snapshot
PARP inhibitors: Synthetic lethality in the clinic
inferredcites →https://doi.org/10.1128/mcb.19.4.2644openalex-snapshot
Inhibition of Nuclear Receptor Signalling by Poly(ADP-Ribose) Polymerase
inferredcites →https://doi.org/10.1128/mmbr.00040-05openalex-snapshot
Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going?
inferredcites →https://doi.org/10.1186/1477-5956-8-22openalex-snapshot
Investigation of PARP-1, PARP-2, and PARG interactomes by affinity-purification mass spectrometry
inferredcites →https://doi.org/10.1210/me.2005-0040openalex-snapshot
Functional Genomics Identifies a Mechanism for Estrogen Activation of the Retinoic Acid Receptor α1 Gene in Breast Cancer Cells
inferredcites →https://doi.org/10.1371/journal.pgen.1002442openalex-snapshot
Poly(ADP-Ribose) Polymerase 1 (PARP-1) Regulates Ribosomal Biogenesis in Drosophila Nucleoli
inferredcites →https://doi.org/10.1371/journal.pone.0006146openalex-snapshot
Molecular Profiling of Breast Cancer Cell Lines Defines Relevant Tumor Models and Provides a Resource for Cancer Gene Discovery
inferredcites →https://doi.org/10.1515/bchm2.1976.357.1.527openalex-snapshot
Poly(Adenosine Diphosphate Ribose) is Covalently Linked to Nuclear Proteins by Two Types of Bonds
inferredcites →https://doi.org/10.2741/3329openalex-snapshot
Poly (ADP-ribose) glycohydrolase (PARG) and its therapeutic potential
inferredcites →https://doi.org/10.4161/cc.10.9.15486openalex-snapshot
Aldehyde dehydrogenase: Its role as a cancer stem cell marker comes down to the specific isoform
What points at this work
Incoming claims: where this work appears in other papers’ reference lists and arguments.
inferred← citeshttps://doi.org/10.1002/9781118970195.ch14openalex-snapshot
Site‐Specific Characterization of Asp ‐ and Glu ‐ ADP ‐Ribosylation by Quantitative Mass Spectrometry
inferred← citeshttps://doi.org/10.1002/ddr.70346openalex-snapshot
Structure‐Based Design, Synthesis, and Biological Evaluation of Oxadiazole–Morpholine Hybrids as Potent PARP‐1 Inhibitors Inducing Apoptosis in Breast Cancer Cells
inferred← citeshttps://doi.org/10.1002/mas.21811openalex-snapshot
Uncommon posttranslational modifications in proteomics: ADP‐ribosylation, tyrosine nitration, and tyrosine sulfation
inferred← citeshttps://doi.org/10.1002/pmic.202200083openalex-snapshot
Impact of Asp/Glu‐ADP‐ribosylation on protein‐protein interaction and protein function
inferred← citeshttps://doi.org/10.1002/wrna.1571openalex-snapshot
Connections between 3′ end processing and DNA damage response: Ten years later
inferred← citeshttps://doi.org/10.1007/s10549-023-07150-4openalex-snapshot
Olaparib enhances sensitization of BRCA-proficient breast cancer cells to x-rays and protons
inferred← citeshttps://doi.org/10.1016/b978-0-443-19001-8.00007-6openalex-snapshot
Regulation of chromatin structure and function by adenosine diphosphate (ADP)-ribosylation
inferred← citeshttps://doi.org/10.1016/bs.mie.2019.06.024openalex-snapshot
Site-specific analysis of the Asp- and Glu-ADP-ribosylated proteome by quantitative mass spectrometry
inferred← citeshttps://doi.org/10.1016/j.arr.2024.102206openalex-snapshot
PARP1 at the crossroad of cellular senescence and nucleolar processes
inferred← citeshttps://doi.org/10.1016/j.bcp.2019.03.037openalex-snapshot
Human alcohol dehydrogenase 1 is an acceptor protein for polyADP-ribosylation
inferred← citeshttps://doi.org/10.1016/j.bcp.2022.115329openalex-snapshot
A PARP1 PROTAC as a novel strategy against PARP inhibitor resistance via promotion of ferroptosis in p53-positive breast cancer
inferred← citeshttps://doi.org/10.1016/j.cbs.2026.100005openalex-snapshot
Metabolic Fuel, Molecular Code: How Cancer Rewires Metabolite-Driven Post-Translational Modifications to Shape Tumor Fate
inferred← citeshttps://doi.org/10.1016/j.celrep.2018.07.083openalex-snapshot
Systems-wide Analysis of Serine ADP-Ribosylation Reveals Widespread Occurrence and Site-Specific Overlap with Phosphorylation
inferred← citeshttps://doi.org/10.1016/j.celrep.2019.04.031openalex-snapshot
PARP-1 Activation Directs FUS to DNA Damage Sites to Form PARG-Reversible Compartments Enriched in Damaged DNA
inferred← citeshttps://doi.org/10.1016/j.celrep.2024.114433openalex-snapshot
ADP-ribosylome analysis reveals homogeneous DNA-damage-induced serine ADP-ribosylation across wild-type and BRCA-mutant breast cancer cell lines
inferred← citeshttps://doi.org/10.1016/j.chembiol.2018.09.008openalex-snapshot
Monitoring Poly(ADP-ribosyl)glycohydrolase Activity with a Continuous Fluorescent Substrate
inferred← citeshttps://doi.org/10.1016/j.dnarep.2019.02.002openalex-snapshot
The role of dePARylation in DNA damage repair and cancer suppression
inferred← citeshttps://doi.org/10.1016/j.dnarep.2025.103824openalex-snapshot
Targeting dePARylation in cancer therapy
inferred← citeshttps://doi.org/10.1016/j.dnarep.2025.103863openalex-snapshot
PARPs and ADP-ribosyl hydrolases in cancer therapy: From drug targets to biomarkers
inferred← citeshttps://doi.org/10.1016/j.mcpro.2026.101666openalex-snapshot
Optimized detection of acidic ADP-ribosylation by PARP14 in vitro using multi-modal mass spectrometry reveals putative autoregulatory patches
inferred← citeshttps://doi.org/10.1016/j.molcel.2018.12.022openalex-snapshot
ELTA: Enzymatic Labeling of Terminal ADP-Ribose
inferred← citeshttps://doi.org/10.1016/j.molcel.2019.06.020openalex-snapshot
Activation of PARP-1 by snoRNAs Controls Ribosome Biogenesis and Cell Growth via the RNA Helicase DDX21
inferred← citeshttps://doi.org/10.1016/j.molcel.2021.08.037openalex-snapshot
Reading ADP-ribosylation signaling using chemical biology and interaction proteomics
inferred← citeshttps://doi.org/10.1016/j.molcel.2023.04.009openalex-snapshot
PARPs and ADP-ribosylation: Deciphering the complexity with molecular tools
inferred← citeshttps://doi.org/10.1016/j.molcel.2024.10.024openalex-snapshot
PARP enzyme de novo synthesis of protein-free poly(ADP-ribose)
inferred← citeshttps://doi.org/10.1016/j.procbio.2023.06.012openalex-snapshot
Highly efficient and simultaneous production of thirteen taxanes from Taxus × media and mining of their new bioactivity
inferred← citeshttps://doi.org/10.1021/acs.biochem.7b01022openalex-snapshot
Proteomic Analysis of the Downstream Signaling Network of PARP1
inferred← citeshttps://doi.org/10.1021/acs.jproteome.8b00146openalex-snapshot
Hydrofluoric Acid-Based Derivatization Strategy To Profile PARP-1 ADP-Ribosylation by LC–MS/MS
inferred← citeshttps://doi.org/10.1021/acs.jproteome.8b00895openalex-snapshot
A Study into the ADP-Ribosylome of IFN-γ-Stimulated THP-1 Human Macrophage-like Cells Identifies ARTD8/PARP14 and ARTD9/PARP9 ADP-Ribosylation
inferred← citeshttps://doi.org/10.1021/acs.jproteome.9b00696openalex-snapshot
Ion-Pairing with Triethylammonium Acetate Improves Solid-Phase Extraction of ADP-Ribosylated Peptides
inferred← citeshttps://doi.org/10.1021/acschembio.1c00542openalex-snapshot
Rapid Analysis of ADP-Ribosylation Dynamics and Site-Specificity Using TLC-MALDI
inferred← citeshttps://doi.org/10.1021/acschembio.5c00817openalex-snapshot
A Large-Scale Method to Measure the Stoichiometries of Protein Poly-ADP-Ribosylation
inferred← citeshttps://doi.org/10.1038/s41422-021-00597-4openalex-snapshot
Pre-ribosomal RNA reorganizes DNA damage repair factors in nucleus during meiotic prophase and DNA damage response
inferred← citeshttps://doi.org/10.1038/s41467-019-08859-xopenalex-snapshot
Emerging roles of eraser enzymes in the dynamic control of protein ADP-ribosylation
inferred← citeshttps://doi.org/10.1038/s41467-021-26172-4openalex-snapshot
The regulatory landscape of the human HPF1- and ARH3-dependent ADP-ribosylome
inferred← citeshttps://doi.org/10.1038/s41467-024-48314-0openalex-snapshot
Preserving ester-linked modifications reveals glutamate and aspartate mono-ADP-ribosylation by PARP1 and its reversal by PARG
inferred← citeshttps://doi.org/10.1038/s41467-026-73677-xopenalex-snapshot
Deciphering cytokine-driven ADP-ribosylation signaling networks via Af1521-based mass spectrometry analysis of labile Glu/Asp-linkages
inferred← citeshttps://doi.org/10.1038/s41589-019-0379-2openalex-snapshot
Uncoupling of PARP1 trapping and inhibition using selective PARP1 degradation
inferred← citeshttps://doi.org/10.1038/s41598-018-25137-wopenalex-snapshot
Nucleolar-nucleoplasmic shuttling of TARG1 and its control by DNA damage-induced poly-ADP-ribosylation and by nucleolar transcription
inferred← citeshttps://doi.org/10.1042/bst20180418openalex-snapshot
PARPs in genome stability and signal transduction: implications for cancer therapy
inferred← citeshttps://doi.org/10.1074/jbc.ra120.012801openalex-snapshot
AI26 inhibits the ADP-ribosylhydrolase ARH3 and suppresses DNA damage repair
inferred← citeshttps://doi.org/10.1083/jcb.202401101openalex-snapshot
RACK1 MARylation regulates translation and stress granules in ovarian cancer cells
inferred← citeshttps://doi.org/10.1093/nar/gkad440openalex-snapshot
Pyruvate Kinase M (PKM) binds ribosomes in a poly-ADP ribosylation dependent manner to induce translational stalling
inferred← citeshttps://doi.org/10.1093/nar/gkaf1090openalex-snapshot
Nuclear poly(A)-binding protein and nucleolin utilize their RNA recognition motifs to read PAR chains
inferred← citeshttps://doi.org/10.1093/nar/gkag183openalex-snapshot
HPF1 regulates the formation of FUS-dependent compartments by PARP1 and PARP2 activation on damaged DNA
inferred← citeshttps://doi.org/10.1093/narcan/zcad043openalex-snapshot
The dynamic process of covalent and non-covalent PARylation in the maintenance of genome integrity: a focus on PARP inhibitors
inferred← citeshttps://doi.org/10.1093/toxsci/kfz131openalex-snapshot
Toxicoproteomic Analysis of Poly(ADP-Ribose)-Associated Proteins Induced by Oxidative Stress in Human Proximal Tubule Cells
inferred← citeshttps://doi.org/10.1101/2021.11.15.468561openalex-snapshot
pGlycoQuant with a deep residual network for precise and minuscule-missing-value quantitative glycoproteomics enabling the functional exploration of site-specific glycosylation
inferred← citeshttps://doi.org/10.1101/2023.12.15.571635openalex-snapshot
A Site-Specific Analysis of the ADP-Ribosylome Unveils Homogeneous DNA Damage-Induced Serine ADP-Ribosylation Across Wild-Type and BRCA-Mutant Breast Cancer Cell Lines
inferred← citeshttps://doi.org/10.1101/2025.03.27.645734openalex-snapshot
A large-scale method to measure the absolute stoichiometries of protein Poly-ADP-Ribosylation
inferred← citeshttps://doi.org/10.1101/2025.09.15.676193openalex-snapshot
Interplay between human ribosomal proteins, PARP1, PARP2, HPF1 and histones
inferred← citeshttps://doi.org/10.1101/gad.334433.119openalex-snapshot
PARPs and ADP-ribosylation in RNA biology: from RNA expression and processing to protein translation and proteostasis
inferred← citeshttps://doi.org/10.1126/sciadv.adg7752openalex-snapshot
Nimbolide targets RNF114 to induce the trapping of PARP1 and synthetic lethality in BRCA -mutated cancer
inferred← citeshttps://doi.org/10.1146/annurev-cancerbio-042324-103725openalex-snapshot
Mechanism of Action of PARP Inhibitors
inferred← citeshttps://doi.org/10.1158/1541-7786.mcr-21-0103openalex-snapshot
PARP-1 Regulates Estrogen-Dependent Gene Expression in Estrogen Receptor α–Positive Breast Cancer Cells
inferred← citeshttps://doi.org/10.1158/1541-7786.mcr-25-1068openalex-snapshot
Mapping the Subtype-Specific PARP1 ADP-Ribosylated Proteome in Breast Cancer Cells
inferred← citeshttps://doi.org/10.1158/2326-6066.cir-18-0071openalex-snapshot
PARP1 Suppresses the Transcription of PD-L1 by Poly(ADP-Ribosyl)ating STAT3
inferred← citeshttps://doi.org/10.1186/s13058-025-02085-8openalex-snapshot
Retinoic acid-induced 2 deficiency impairs genomic stability in breast cancer
inferred← citeshttps://doi.org/10.1186/s13578-022-00756-zopenalex-snapshot
Unconventional protein post-translational modifications: the helmsmen in breast cancer
inferred← citeshttps://doi.org/10.21203/rs.3.rs-3908810/v1openalex-snapshot
Retinoic Acid-Induced 2 Contributes to Proficient Homologous Recombination and Maintains Genomic Stability in Breast Cancer
inferred← citeshttps://doi.org/10.26508/lsa.202403026openalex-snapshot
PARP10 is critical for stress granule initiation
inferred← citeshttps://doi.org/10.2967/jnumed.124.268254openalex-snapshot
Kinetic Analysis and Metabolism of Poly(Adenosine Diphosphate–Ribose) Polymerase-1–Targeted18F-Fluorthanatrace PET in Breast Cancer
inferred← citeshttps://doi.org/10.3389/fcell.2022.831741openalex-snapshot
The C-Terminal Domain of Y-Box Binding Protein 1 Exhibits Structure-Specific Binding to Poly(ADP-Ribose), Which Regulates PARP1 Activity
inferred← citeshttps://doi.org/10.3389/fcell.2022.864101openalex-snapshot
Research Progress on Mono-ADP-Ribosyltransferases in Human Cell Biology
inferred← citeshttps://doi.org/10.3389/fgene.2021.746380openalex-snapshot
Encounters in Three Dimensions: How Nuclear Topology Shapes Genome Integrity
inferred← citeshttps://doi.org/10.3389/fonc.2021.785102openalex-snapshot
Comparison of the Efficacy and Safety of PARP Inhibitors as a Monotherapy for Platinum-Sensitive Recurrent Ovarian Cancer: A Network Meta-Analysis
inferred← citeshttps://doi.org/10.70675/bdd8c1b6z3cfcz4fd8z9277z39ed8983ee72openalex-snapshot
The link between PARP1-mediated signaling and RNA-binding protein FUS in response to DNA damage
inferred← citeshttps://doi.org/10.7554/elife.34334openalex-snapshot
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.