Relevant bibliographies by topics / PARP1

Academic literature on the topic 'PARP1'

Author: Grafiati
Published: 4 June 2021
Last updated: 10 March 2023

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'PARP1.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Journal articles on the topic "PARP1":

1

Kamata, Teddy, Chun-Song Yang, Tiffany A. Melhuish, Henry F. Frierson Jr., David Wotton, and Bryce M. Paschal. "Post-Transcriptional Regulation of PARP7 Protein Stability Is Controlled by Androgen Signaling." Cells 10, no. 2 (February 9, 2021): 363. http://dx.doi.org/10.3390/cells10020363.

Full text
APA, Harvard, Vancouver, ISO, and other styles
Abstract:
Poly-ADP-ribose polymerases (PARPs) are enzymes that catalyze ADP-ribosylation and play critical roles in normal and disease settings. The PARP family member, PARP7, is a mono-ADP-ribosyltransferase that has been suggested to play a tumor suppressive role in breast, ovarian, and colorectal cancer. Here, we have investigated how androgen signaling regulates PARP7 homeostasis in prostate cancer cells, where PARP7 is a direct target gene of AR. We found that the PARP7 protein is extremely short-lived, with a half-life of 4.5 min. We show that in addition to its transcriptional regulation by AR, PARP7 is subject to androgen-dependent post-transcriptional regulation that increases its half-life to 25.6 min. This contrasts with PARP1, PARP2, PARP9, and PARP14, which do not display rapid turnover and are not regulated by androgen signaling. Androgen- and AR-dependent stabilization of PARP7 leads to accumulation in the nucleus, which we suggest is a major site of action. Mutations in the catalytic domain, the Cys3His1 zinc finger, and WWE (tryptophan–tryptophan–glutamate) domains in PARP7 each reduce the degradation rate of PARP7, suggesting the overall structure of the protein is tuned for its rapid turnover. Our finding that PARP7 is regulated by AR signaling both transcriptionally and post-transcriptionally in prostate cancer cells suggests the dosage of PARP7 protein is subject to tight regulation.
2

Demény, Máté A., and László Virág. "The PARP Enzyme Family and the Hallmarks of Cancer Part 1. Cell Intrinsic Hallmarks." Cancers 13, no. 9 (April 23, 2021): 2042. http://dx.doi.org/10.3390/cancers13092042.

Full text
APA, Harvard, Vancouver, ISO, and other styles
Abstract:
The 17-member poly (ADP-ribose) polymerase enzyme family, also known as the ADP-ribosyl transferase diphtheria toxin-like (ARTD) enzyme family, contains DNA damage-responsive and nonresponsive members. Only PARP1, 2, 5a, and 5b are capable of modifying their targets with poly ADP-ribose (PAR) polymers; the other PARP family members function as mono-ADP-ribosyl transferases. In the last decade, PARP1 has taken center stage in oncology treatments. New PARP inhibitors (PARPi) have been introduced for the targeted treatment of breast cancer 1 or 2 (BRCA1/2)-deficient ovarian and breast cancers, and this novel therapy represents the prototype of the synthetic lethality paradigm. Much less attention has been paid to other PARPs and their potential roles in cancer biology. In this review, we summarize the roles played by all PARP enzyme family members in six intrinsic hallmarks of cancer: uncontrolled proliferation, evasion of growth suppressors, cell death resistance, genome instability, reprogrammed energy metabolism, and escape from replicative senescence. In a companion paper, we will discuss the roles of PARP enzymes in cancer hallmarks related to cancer-host interactions, including angiogenesis, invasion and metastasis, evasion of the anticancer immune response, and tumor-promoting inflammation. While PARP1 is clearly involved in all ten cancer hallmarks, an increasing body of evidence supports the role of other PARPs in modifying these cancer hallmarks (e.g., PARP5a and 5b in replicative immortality and PARP2 in cancer metabolism). We also highlight controversies, open questions, and discuss prospects of recent developments related to the wide range of roles played by PARPs in cancer biology. Some of the summarized findings may explain resistance to PARPi therapy or highlight novel biological roles of PARPs that can be therapeutically exploited in novel anticancer treatment paradigms.
3

Xu, Xi, Jian Wang, Tong Tong, Shao-Fen Lin, Congmin Liu, and Dunhua Zhou. "Evaluation of Poly(ADP-ribose) Polymerase Inhibitor, Pamiparib (BGB-290) in Treating Acute Myeloid Leukemia and the Characterization of Its Nanocarrier." Journal of Biomedical Nanotechnology 17, no. 11 (November 1, 2021): 2165–75. http://dx.doi.org/10.1166/jbn.2021.3182.

Full text
APA, Harvard, Vancouver, ISO, and other styles
Abstract:
Despite the continuous improvement of leukemia treatment in the clinic, the overall 5-year disease-free survival of acute myeloid leukemia (AML) is only approximately 30%–60% due to relapse and the refractoriness of AML after traditional chemotherapy. Inhibition of poly(ADP-ribose) polymerase (PARP), a member of the DNA damage repair complex, has a strong antitumor effect in solid tumors. However, the role of PARP in AML remains unclear. We found that high levels of PARP1 and PARP2 were positively related to chemotherapy resistance and poor prognosis in patients with AML. Doxorubicin (DOX)-resistant AML cells highly expressed PAPR1 and PARP2. Knockdown of PARP1 and PARP2, or pharmaceutical inhibition of PARP by the PARP inhibitor (PARPi) BGB-290, significantly enhanced the cytotoxicity of DOX in AML cells due to increased DNA damage. PLGA-loading BGB-290 was properly self-assembled into stable BGB-290@PLGA nanoparticles (NPs), which is uniform particle size and good stability. BGB-290@PLGA is easily uptake by AML cell lines and stays for a long time. Combined with DOX, BGB-290@PLGA can significantly improve the chemosensitivity of AML cell lines. Furthermore, BGB-290 and DOX combination treatment dramatically repressed the onset of leukemia and prolonged the survival of THP-1 xenografted mice. Overall, this study demonstrated that PARPi with traditional chemotherapy could be an efficient therapeutic strategy for AML.
4

Gennari, A., M. Sormani, L. Varesco, P. Pronzato, V. Viassolo, V. Mirisola, U. Pfeffer, and P. Bruzzi. "Prognostic significance of BRCA1, PARP1, and PARP2 in sporadic breast cancer." Journal of Clinical Oncology 27, no. 15_suppl (May 20, 2009): e22114-e22114. http://dx.doi.org/10.1200/jco.2009.27.15_suppl.e22114.

Full text
APA, Harvard, Vancouver, ISO, and other styles
Abstract:
e22114 Background: Breast cancer susceptibility gene (BRCA1) is a tumor suppressor gene whose mutation is associated with the development of hereditary breast cancer. In sporadic tumors, loss of BRCA1, resulting from reduced expression or incorrect subcellular localization, has been suggested to be associated with prognosis. Cells with BRCA1 loss of function are deficient in DNA double strand break repair thus activating poly(ADP-ribose) polymerases (PARPs) whose catalytic activity is immediately stimulated by DNA strand-breaks. The aim of this study was to evaluate the prognostic value of BRCA1 and PARPs (PARP1 and 2) in sporadic breast cancer. Methods: We merged two previously published Affymetrix gene expression datasets: GSE 1456 (159 patients, median follow up 7 years) and GSE 2494 (249 patients, median follow up 10 years). Microarray data preprocessing was carried out using Bioconductor software (gcrma procedure). Expression of BRCA1, PARP1 and PARP2 mRNA were evaluated as continuous variables. Kaplan Meier survival curves and Cox regression analysis (stratified by database) were used to assess the prognostic capability of the identified biomarkers. Results: High mRNA expression of BRCA1, PARP1 and PARP2 was correlated with an adverse prognosis. Relapse Free Survival (RFS) Hazard Ratio was 1.6 (95% CI, 1.2 to 2.1) for BRCA1 (p = 0.002), 1.7 (95% CI, 1.2 to 2.4) for PARP1 (p = 0.002) and 1.7 (95% CI, 1.3 to 2.3) for PARP2 (p = 0.001). By multivariate analysis all 3 genes resulted independently correlated with RFS. When interaction with systemic adjuvant therapy (107 patients treated) was tested, BRCA1 mRNA expression was strongly associated with treatment: HR 2.3 (95% CI, 1.4 to 3.7, p 0.001); p for interaction = 0.06. Conclusions: This study shows that BRCA1, PARP1 and PARP2 are all significantly associated with prognosis in sporadic breast cancer. No significant financial relationships to disclose.
5

Maluchenko, Natalya, Darya Koshkina, Anna Korovina, Vasily Studitsky, and Alexey Feofanov. "Interactions of PARP1 Inhibitors with PARP1-Nucleosome Complexes." Cells 11, no. 21 (October 23, 2022): 3343. http://dx.doi.org/10.3390/cells11213343.

Full text
APA, Harvard, Vancouver, ISO, and other styles
Abstract:
Inhibitors (PARPi) of poly(ADP-ribose-)polymerase-1 (PARP1) are used in antitumor therapy; their cytotoxicity correlates with the efficiency of PARP1 trapping in cell chromatin. Previous studies have demonstrated the PARPi-induced trapping of PARP1 on DNA, although details of the mechanism remain controversial. Here, the interactions of PARP1-nucleosome complexes with PARPi, olaparib (Ola), talazoparib (Tala), and veliparib (Veli) were studied. PARPi trap PARP1 on nucleosomes without affecting the structure of PARP1-nucleosome complexes. The efficiency of PARP1 trapping on nucleosomes increases in the order of Tala>Ola>>Veli, recapitulating the relative trapping efficiencies of PARPi in cells, but different from the relative potency of PARPi to inhibit the catalytic activity of PARP1. The efficiency of PARP1 trapping on nucleosomes correlates with the level of inhibition of auto-PARylation, which otherwise promotes the dissociation of PARP1-nucleosome complexes. The trapping efficiencies of Tala and Ola (but not Veli) are additionally modulated by the enhanced PARP1 binding to nucleosomes. The dissociation of PARP1-nucleosome complexes occurs without a loss of histones and leads to the restoration of the intact structure of nucleosomal DNA. The data suggest that the chromatin structure can considerably affect the efficiency of the PARPi action.
6

Vasil’eva, Inna, Nina Moor, Rashid Anarbaev, Mikhail Kutuzov, and Olga Lavrik. "Functional Roles of PARP2 in Assembling Protein–Protein Complexes Involved in Base Excision DNA Repair." International Journal of Molecular Sciences 22, no. 9 (April 28, 2021): 4679. http://dx.doi.org/10.3390/ijms22094679.

Full text
APA, Harvard, Vancouver, ISO, and other styles
Abstract:
Poly(ADP-ribose) polymerase 2 (PARP2) participates in base excision repair (BER) alongside PARP1, but its functions are still under study. Here, we characterize binding affinities of PARP2 for other BER proteins (PARP1, APE1, Polβ, and XRCC1) and oligomerization states of the homo- and hetero-associated complexes using fluorescence-based and light scattering techniques. To compare PARP2 and PARP1 in the efficiency of PAR synthesis, in the absence and presence of protein partners, the size of PARP2 PARylated in various reaction conditions was measured. Unlike PARP1, PARP2 forms more dynamic complexes with common protein partners, and their stability is effectively modulated by DNA intermediates. Apparent binding affinity constants determined for homo- and hetero-oligomerized PARP1 and PARP2 provide evidence that the major form of PARP2 at excessive PARP1 level is their heterocomplex. Autoregulation of PAR elongation at high PARP and NAD+ concentrations is stronger for PARP2 than for PARP1, and the activity of PARP2 is more effectively inhibited by XRCC1. Moreover, the activity of both PARP1 and PARP2 is suppressed upon their heteroPARylation. Taken together, our findings suggest that PARP2 can function differently in BER, promoting XRCC1-dependent repair (similarly to PARP1) or an alternative XRCC1-independent mechanism via hetero-oligomerization with PARP1.
7

Mueller, Nancy, Stephen Luen, Roger Stupp, Anthony Chalmers, Baisong Huang, Massimo Squatrito, Barry Davies, Petra Hamerlik, and Timothy Yap. "CTNI-03. A PHASE I/IIA, OPEN-LABEL STUDY OF THE BRAIN-PENETRANT PARP1-SELECTIVE INHIBITOR AZD9574 AS MONOTHERAPY AND IN COMBINATION IN PATIENTS WITH ADVANCED SOLID MALIGNANCIES (CERTIS1)." Neuro-Oncology 24, Supplement_7 (November 1, 2022): vii70. http://dx.doi.org/10.1093/neuonc/noac209.270.

Full text
APA, Harvard, Vancouver, ISO, and other styles
Abstract:
Abstract BACKGROUND Currently approved Poly ADP-Ribose Polymerase (PARP) inhibitors (PARPi) selectively inhibit and trap both PARP1 and PARP2 (PARP1/2) at sites of single strand (ss) deoxyribonucleic acid (DNA) (ssDNA) damage, preventing ssDNA repair and leading to replication-dependent DNA double strand breaks. Recent data suggest that only inhibition of PARP1 is required for anti-proliferative effects, while PARP2 functions in the survival of haematopoietic stem and progenitor cells. These observations suggest that the inhibition and trapping of PARP 2 is not needed for anti-cancer effects, and may be a major driver of haematological toxicity observed. AZD9574 is a novel brain-penetrant PARPi that potently and selectively inhibits and traps PARP1, with the goal of delivering efficacious, less toxic, and more combinable PARPi. Furthermore, owing to its central nervous system penetration capability, AZD9574 may provide a new treatment option for patients with CNS malignancies or patients with brain metastases characterized by homologous recombination deficiency (HRD). METHODS This is a first-in-human modular study primarily designed to evaluate the safety and tolerability of AZD9574 as monotherapy and in combination with anti-cancer agents at increasing dose levels in patients with advanced solid malignancies, followed by expansion cohorts in specific indications. The study will also characterize the pharmacokinetics of AZD9574 and explore potential biological activity by assessing pharmacodynamic and exploratory biomarkers and anti-tumour activity. Module 1 will enrol patients with advanced breast, ovarian, pancreatic or prostate tumours harbouring homologous recombination deficiencies. Module 2 will enrol patients with isocitrate dehydrogenase (IDH)1/2 mutated glioma.
8

Kam, Caleb M., Amanda L. Tauber, Stephan M. Levonis, and Stephanie S. Schweiker. "Design, synthesis and evaluation of potential inhibitors for poly(ADP-ribose) polymerase members 1 and 14." Future Medicinal Chemistry 12, no. 24 (December 2020): 2179–90. http://dx.doi.org/10.4155/fmc-2020-0218.

Full text
APA, Harvard, Vancouver, ISO, and other styles
Abstract:
Poly(ADP-ribose) polymerase (PARP) members PARP1 and PARP14 belong to an 18-member superfamily of post-translational modifying enzymes. A library of 9 novel non-NAD analog amine compounds was designed, synthesized and evaluated for inhibitory activity against PARP1 and PARP14. Both in silico studies and in vitro assays identified compound 2 as a potential PARP1 inhibitor, inhibiting activity by 93 ± 2% (PARP14 inhibition: 0 ± 6%), and 7 as a potential PARP14 inhibitor, inhibiting activity by 91 ± 2% (PARP1 inhibition: 18 ± 4%), at 10-μm concentration. Key in silico interactions with TYR907 in PARP1 and TYR1620 and TYR1646 in PARP14 have been identified. Compound 2 and compound 7 have been identified as potential leads for the development of selective PARP inhibitors.
9

Nguyen, Nghia T., Anna Pacelli, Michael Nader, and Susanne Kossatz. "DNA Repair Enzyme Poly(ADP-Ribose) Polymerase 1/2 (PARP1/2)-Targeted Nuclear Imaging and Radiotherapy." Cancers 14, no. 5 (February 23, 2022): 1129. http://dx.doi.org/10.3390/cancers14051129.

Full text
APA, Harvard, Vancouver, ISO, and other styles
Abstract:
Since it was discovered that many tumor types are vulnerable to inhibition of the DNA repair machinery, research towards efficient and selective inhibitors has accelerated. Amongst other enzymes, poly(ADP-ribose)-polymerase 1 (PARP1) was identified as a key player in this process, which resulted in the development of selective PARP inhibitors (PARPi) as anti-cancer drugs. Most small molecule PARPi’s exhibit high affinity for both PARP1 and PARP2. PARPi are under clinical investigation for mono- and combination therapy in several cancer types and five PARPi are now clinically approved. In parallel, radiolabeled PARPi have emerged for non-invasive imaging of PARP1 expression. PARP imaging agents have been suggested as companion diagnostics, patient selection, and treatment monitoring tools to improve the outcome of PARPi therapy, but also as stand-alone diagnostics. We give a comprehensive overview over the preclinical development of PARP imaging agents, which are mostly based on the PARPi olaparib, rucaparib, and recently also talazoparib. We also report on the current status of clinical translation, which involves a growing number of early phase trials. Additionally, this work provides an insight into promising approaches of PARP-targeted radiotherapy based on Auger and α-emitting isotopes. Furthermore, the review covers synthetic strategies for PARP-targeted imaging and therapy agents that are compatible with large scale production and clinical translation.
10

Jamal, Kunzah, Anna Staniszewska, Jacob Gordon, Shenghua Wen, Frank McGrath, Gregory Dowdell, Dominic Kabbabe, et al. "Abstract 2609: AZD9574 is a novel, brain penetrant PARP-1 selective inhibitor with activity in an orthotopic, intracranial xenograft model with aberrant DNA repair." Cancer Research 82, no. 12_Supplement (June 15, 2022): 2609. http://dx.doi.org/10.1158/1538-7445.am2022-2609.

Full text
APA, Harvard, Vancouver, ISO, and other styles
Abstract:
Abstract The Poly (ADP-ribose) polymerase (PARP) family has numerous essential functions in cellular processes such as transcription, chromatin remodelling, DNA damage response and repair as well as apoptosis. PARP inhibition blocks base excision repair and results in conversion of SSBs to DNA double-strand break (DSBs). DSBs are the most deleterious form of DNA damage that can be generated by exogenous DNA damaging agents or endogenous replication stress. DSBs can be repaired by homologous recombination repair (HRR) or non-homologous end joining (NHEJ). The physiological importance of HRR is underscored by the observation of genomic instability in HRR-deficient (HRD+) cells and, importantly, the association of cancer predisposition and developmental defects with mutations in HRR genes. PARP1 and PARP2 are required for SSB repair, while PARP1 is also involved in the repair of DNA double-strand breaks (DSBs) and replication fork damage. Recent reports suggest the PARP1 inhibition is sufficient to elicit an anti-proliferative effect and that PARP2 is essential for the survival of hematopoietic stem and progenitor cells in animal models.AZD9574 is a novel brain penetrant PARP1 inhibitor that acts by selectively inhibiting and trapping PARP1 at the sites of SSBs. AZD9574 exhibited >8000-fold selectivity for PARP1 compared to PARP2 and other members of the PARP family (PARP2, PARP3, PARP5a and PARP6) in biochemical assays. While AZD9574 inhibited PARP1 enzymatic activity in all tested cell lines irrespective of the HRR status (IC50 range between 0.3 - 2 nM), colony formation assay in isogenic cell lines pairs confirmed higher potency and selectivity towards HRD+ models (DLD1 BRCA2-/-; SKOV-3 BRCA2-/- and SKOV-3 PALB2-/-). For example, AZD9574 IC50 in the BRCA2-/- DLD1 cells was 1.38 nM compared to IC50 > 40 µM BRCA2wt cells, which corresponds to a ~20,000-fold greater efficacy in the BRCA2-/-cells (ratio of AZD9574 IC50 in BRCA2wt divided by BRCA2-/-) compared to the wild type parental line. In vivo, AZD9574 demonstrated dose-dependent efficacy in a BRCA1 mutant MDA-MB-436 subcutaneous xenograft model. Anti-tumour effects of AZD9574 were manifested by pronounced growth regressions that were durable after treatment withdrawal. An intracranial xenograft model of breast cancer brain metastases was developed to assess the efficacy of AZD9574 in the context of blood-brain barrier penetrance. Treatment of animals with established intracranial lesions using a dose of 3 mg/kg AZD9574 showed sustained tumour growth suppression resulting in a significantly extended survival of tumour-bearing mice. Collectively, we believe that our data support the development of AZD9574 as a potential therapy for patients with HRD+ breast cancer whose disease has spread to the brain. Citation Format: Kunzah Jamal, Anna Staniszewska, Jacob Gordon, Shenghua Wen, Frank McGrath, Gregory Dowdell, Dominic Kabbabe, Giuditta illuzzi, Matthew Griffin, Barry R. Davies, Petra Hamerlik. AZD9574 is a novel, brain penetrant PARP-1 selective inhibitor with activity in an orthotopic, intracranial xenograft model with aberrant DNA repair [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2022; 2022 Apr 8-13. Philadelphia (PA): AACR; Cancer Res 2022;82(12_Suppl):Abstract nr 2609.
More sources
You might also be interested in the extended bibliographies on the topic 'PARP1' for particular source types:
Journal articles Dissertations / Theses Books

Dissertations / Theses on the topic "PARP1":

1

Roper, Stephen James. "PARP1 and PARP7 safeguard the lineage-specificity and pluripotency of ES cells." Thesis, University of Cambridge, 2011. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.609467.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Gajewski, Sabine [Verfasser], and A. [Akademischer Betreuer] Hartwig. "Generierung einer PARP1-Knockout Zelllinie zur Charakterisierung der Rolle von PARP1 in der DNA-Schadensantwort / Sabine Gajewski ; Betreuer: A. Hartwig." Karlsruhe : KIT-Bibliothek, 2021. http://d-nb.info/1234063735/34.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Dulak-Lis, Maria Gabriela. "PARP1, TRPM2 and redox signalling in hypertension-associated vascular dysfunction." Thesis, University of Glasgow, 2018. http://theses.gla.ac.uk/30660/.

Full text
APA, Harvard, Vancouver, ISO, and other styles
Abstract:
While oxidative stress and dysregulation of Ca2+ homeostasis in vascular signalling are hallmarks of hypertension-associated vascular injury, downstream molecular mechanisms that govern reactive oxygen species (ROS)-dependent regulation of ion channels in hypertension are complex and have not yet been fully elucidated. Activation of poly(ADPribose)-polymerase 1 (PARP1) in response to oxidative stress and DNA damage leads to subsequent activation of transient receptor potential melastatin 2 (TRPM2), an ion channel that regulates Na+ and Ca2+ influx. Considering that ROS generation and Ca2+ influx are increased in hypertension we hypothesised that redox regulation of PARP1-TRPM2 may play a role in vascular injury and target organ-damage associated with hypertension. The proof of concept was tested in a TRPM2-overexpressing human embryonic kidney cell line and the relationship between ROS, PARP1 and TRPM2 was studied in vitro, in human vascular smooth muscle cells and endothelial cells. The regulatory role of PARP1 and TRPM2 on vascular function was assessed in isolated resistance arteries from LinA3 mice, a transgenic model expressing human renin gene resulting in chronic hypertension. Finally, the effects of pharmacological inhibition of PARP1 on blood pressure, target organ damage and cellular signalling were evaluated in vivo in hypertensive LinA3 mice. To our knowledge, findings from this study provide the first evidence in clinically-relevant models, that the redox-sensitive PARP1-TRPM2 pathway regulates vascular contraction in the context of hypertension. This is supported by the following findings: i) The in vitro studies demonstrated that PARP1 and TRPM2 facilitate Ang II and oxidant-dependent activation of a pro-contractile protein MLC20 and partially reduce the anti-contractile activity of MYPT1. ii) The ex vivo experiments on mesenteric resistance arteries from LinA3 mice confirmed that the PARP1-TRPM2 pathway exacerbates vascular hypercontractility of the arteries isolated from hypertensive mice. iii) In vivo inhibition of PARP1 had significant effects on renal and cardiac Akt/PKB-dependent signalling, leading to upregulation of prosurvival and anti-apoptotic proteins, effects that were independent of blood pressure lowering. Overall, the studies presented in this thesis highlight a novel pathway linking ROS to vascular signalling pathways through PARP1 and TRPM2. Dysregulation of this system, in the context of oxidative stress in hypertension, may play a role in hypertension-associated vascular injury and target organ damage. While the present studies have opened the field, further investigations to unambiguously prove the importance of the ROS-PARP1-TRPM2-Ca2+ axis in hypertension are required.
4

Lacy, Jessica. "Imaging of PARP1/2-Overexpressing Cancers with Novel AZD2281-Derived Probes." Thesis, Harvard University, 2014. http://etds.lib.harvard.edu/hms/admin/view/58.

Full text
APA, Harvard, Vancouver, ISO, and other styles
Abstract:
Poly(ADP-ribose)polymerase-1 and -2 (PARP1/2) are nuclear proteins involved in DNA repair. Tumors with defects in homologous recombination, including BRCA1- and BRCA2-deficient cancers, have been shown to be sensitive to PARP inhibition. The Weissleder group has synthesized fluorescent and radioactive derivatives of the PARP1/2 inhibitor AZD2281. We hypothesized that fluorescent and radioactive AZD2281-based imaging agents would quantify PARP1/2 expression in vitro and in vivo. To test this hypothesis, a panel of pancreatic ductal adenocarcinoma and ovarian carcinoma cell lines were characterized by immunocytochemistry for PARP1/2 expression. AZD2281-derived fluorescence signal correlated with anti-PARP antibody fluorescence signal strength in vitro. Four cell lines representing a range of PARP1/2 expression levels were then xenografted into Nu/Nu mice. Mice bearing four tumor types each were imaged with AZD2281-derived imaging agents, sacrificed, and their tumors excised for stand-alone imaging and Western blot. AZD2281-derived signal correlated with tumor PARP1/2 expression determined by Western blot, indicating that PARP1/2 expression level is a determinant of fluorescent signal strength and SUVs of AZD2281-derived agents in vivo. These data indicate that AZD2281-derived agents are useful tools for quantifying intracellular PARP1/2 both in vitro and in vivo, which could one day enable prospective identification of tumors likely to respond to PARP inhibitors.
5

Rank, Lisa [Verfasser]. "Cellular characterization of PARP1 variants with altered enzymatic activities / Lisa Rank." Konstanz : KOPS Universität Konstanz, 2019. http://d-nb.info/1216039968/34.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Mouly, Laetitia. "Rôle de la GTPase Rho RND1 dans la réponse cellulaire à la camptothécine, inhibiteur de la topoisomérase I." Thesis, Toulouse 3, 2018. http://www.theses.fr/2018TOU30030/document.

Full text
APA, Harvard, Vancouver, ISO, and other styles
Abstract:
La famille des GTPases Rho, comprenant 20 membres, contrôle la dynamique du cytosquelette d'actine et différents processus cellulaires comme la migration. En plus de leurs rôles bien établis, certaines GTPases Rho, notamment RhoB et Rac1, ont émergé en tant que gènes de réponse précoce aux dommages à l'ADN. En effet, RhoB est induite en réponse à divers stress génotoxiques, y compris la camptothécine (CPT), les UV et le cisplatine, et protège principalement les cellules de l'apoptose. Le rôle des autres GTPases Rho en réponse précoce aux génotoxiques reste largement méconnu. Dans ce projet, nous avons utilisé la camptothécine, un inhibiteur de la topoisomérase I (TOP1), qui stabilise sélectivement les complexes de clivage TOP1-ADN (TOP1cc) sur la chromatine, afin de cribler les GTPases Rho induites de façon précoce par les dommages à l'ADN. En plus de RhoB, nous avons identifié RND1 comme un gène rapidement induit par la CPT. L'induction de RND1 est réversible et étroitement corrélée à la présence de TOP1cc induit par la CPT. En accord avec ces observations, les rayons UV et le péroxyde d'hydrogène, qui stabilisent indirectement les TOP1cc, induisent également RND1. La CPT augmente la transcription de RND1 indépendamment de l'activité de son promoteur minimal. De plus, la CPT augmente l'activité de la poly ADP-ribose polymérase (PARP1), dont l'inhibition prévient la transcription de RND1. La surexpression de RND1 augmente également l'expression de PARP1, suggérant une régulation positive entre PARP1 et RND1 en réponse aux TOP1cc. Ainsi, nous proposons qu'en réponse à la CPT, les TOP1cc activent PARP1, qui à son tour favorise la transcription de RND1, initiant ainsi une boucle de rétrocontrôle positive. Enfin, nous avons montré que RND1 protège les cellules contre l'apoptose induite par la CPT et entraîne leur résistance à la CPT. L'ensemble de ces résultats ont permis d'identifier RND1 comme nouvelle GTPase Rho impliquée dans la réponse au stress et proposent un nouveau mécanisme de régulation de la transcription des gènes en réponse aux TOP1cc via l'activation de PARP1. Ces résultats suggèrent par ailleurs qu'inhiber la signalisation de RND1 pourrait sensibiliser les cellules tumorales aux dérivés cliniques de la CPT
Rho GTPase family comprises 20 members that regulate key cellular functions such as actin cytoskeleton organization and migration. Beside their canonical functions, certain Rho GTPases, including RhoB and Rac1, emerged as early DNA damage-inducible genes. Indeed, RhoB is readily induced in response to various genotoxic stress, including camptothecin (CPT), UV and cisplatin, and primarily protect cells against apoptotic cell death. Whether other Rho GTPases also respond early to genotoxics is largely unknown. In this project, we used camptothecin, a topoisomerase I (TOP1) inhibitor that selectively stabilized TOP1-DNA cleavage complexes (TOP1cc) onto chromatin, to screen for early DNA damage-inducible Rho GTPases. Besides RhoB, we identified RND1 as a gene rapidly induced by CPT. RND1 induction is reversible and closely associated with the presence of TOP1cc induced by CPT. Consistently, UV light and hydrogen peroxide, which indirectly stabilized TOP1cc, induce RND1 as well. CPT increases minimal promoter-independent RND1 transcription. Additionally, CPT increases poly ADP-ribose polymerase (PARP1) activity, whose inhibition prevents RND1 transcription. Overexpression of RND1 also increases PARP1 expression, suggesting a positive regulation between PARP1 and RND1 in response to TOP1cc. Thus, we propose that in response to CPT, TOP1cc activate PARP1, which in turn promotes RND1 transcription resulting in a positive feedback loop. Finally, we found that RND1 protects cells against CPT-induced apoptosis and leads to resistance to CPT. Together, these results highlight RND1 as a new Rho GTPase involved in the response to stress and propose a new mechanism for TOP1cc-induced gene transcription through PARP1 activation. These findings further suggest that inhibiting RND1 signaling could sensitize tumor cells to CPT derivatives
7

Shaikh, Aamir. "Levels of PARP1-immunoreactivity in the Human Brain in Major Depressive Disorder." Digital Commons @ East Tennessee State University, 2020. https://dc.etsu.edu/honors/547.

Full text
APA, Harvard, Vancouver, ISO, and other styles
Abstract:
MDD is a severe and debilitating disorder that is associated with a growing global economic burden due to reduced workplace productivity along with increased healthcare resource utilization. Furthermore, depression markedly enhances the risk for suicide, mortality that is especially worrisome given that 30% of depressed individuals have an inadequate response to current antidepressants. This inadequacy of antidepressants necessitates the discovery of a better understanding of the pathobiology of MDD. Most current antidepressants work through monoamine neurotransmitters, and their relative efficacy in depression led to the now dated monoamine-deficiency hypothesis. The limited usefulness of antidepressants has led to a reinvigorated search for other pathologies in depression that might yield clues for the development of better drug treatments. In this regard, a strong association has been found between oxidative stress and MDD. Our lab recently found increased DNA oxidation and elevated poly(ADP)ribose polymerase (PARP1) gene expression in the brain from donors that had MDD at the time of death. Besides DNA damage repair, PARP1 mediates several downstream inflammatory effects that may contribute to pathology in MDD. In fact, our lab has demonstrated that PARP-1 inhibition produces antidepressant-like effects in rodents, suggesting that PARP-1 inhibitors hold promise as a novel antidepressant drug. While our lab had previously demonstrated elevated PARP1 gene expression in the frontal cortex in MDD, whether PARP1 protein levels were also increased in depression had not been verified. My thesis research was performed to determine whether PARP1 protein expression was also elevated in the brain in MDD. I studied primarily the hippocampus because it is part of the limbic (mediating emotion) system of the brain and because previous research has shown numerous other pathologies in the hippocampus. My study was carried out simultaneously as others in our lab were measuring PARP1 protein levels in frontal cortex in MDD. This latter work was important since the lab’s previous work had observed elevated PARP1 gene expression in the frontal cortex, rather than in the hippocampus which was not previously studied. Hippocampal and frontal cortical brain sections were cut from frozen blocks of both MDD and psychiatrically normal control brain donors for these studies. PARP1 protein levels were estimated by assisted-imaging software. The findings herein demonstrate that levels of PARP1 immunoreactivity are significantly elevated in the frontal cortex of MDD donors as compared to control donors. However, there was no change in PARP1 immunoreactivity in the hippocampus in MDD.
8

Abens, Ryan. "GENE EXPRESSION OF CYTOKINES AND OXIDATIVE STRESS MARKERS IN CTRP3 TRANSGENIC MICE WITH CHRONIC ETHANOL EXPOSURE." Digital Commons @ East Tennessee State University, 2019. https://dc.etsu.edu/asrf/2019/schedule/2.

Full text
APA, Harvard, Vancouver, ISO, and other styles
Abstract:
Oxidative stress and inflammation are often linked to the prognosis of diseases caused by chronic alcohol consumption. Chronic alcohol consumption plays a key role in brain tissue damage, often leading to the development of cognitive disorders and loss of brain function. In addition to the direct effects of alcohol on brain function, consumption of alcohol can lead to psychosocial stressors such as legal, financial, and interpersonal problems. It has been found that mice that overexpress C1q/Tumor Necrosis Factor-related protein-3 (CTRP3) and exposed to ethanol daily do not die like the mice who did not overexpress CTRP3 and fed the same diet. Although the specific physiological functions regulated by the CTRP family are largely unknown, there is evidence showing that they have diverse biological effects on inflammation, metabolism, and survival signaling in several different types of tissue. Postmortem brain tissue samples were collected from mice that were exposed to ethanol with transgenic overexpression of CTRP3 and from wild type mice that were only exposed to ethanol. Interestingly, previous immunoblotting of the cerebellum and the hippocampus using collected tissue demonstrated that glia activation was present in the CTRP3 overexpressing mice but not in the wild-type ethanol fed mice. This finding suggests that glia cells are either dying in the ethanol fed wild type mice or that CTRP3 protects and prolongs activated glia cells. The current study will determine if markers of oxidative stress and cell viability are altered in the CTRP3 overexpressing mice when compared to wild-type mice at the molecular level. RNA isolation using the Directzol system and cDNA synthesis using punch dissected homogenate tissue collected from the hippocampus was used for this investigation. Gene expression of BDNF, SOD1 and PARP1 in mouse tissue was determined using quantitative PCR. Immunoblotting of a small number of hippocampal tissue using PARP1 was performed. The mice that were CTRP3 overexpressed and fed ethanol will likely exhibit altered gene expression of cytokines and increased oxidative stress gene expression in postmortem hippocampal brain tissue when compared to wild-type ethanol fed mice. The current studies could contribute to the body of knowledge for the development of novel therapies that may alleviate the neuro-inflammatory effects of alcohol use.
9

García, Parra Jetzabel 1983. "PARP1 expression in breast cancer and effects of its inhibition in preclinical models." Doctoral thesis, Universitat Pompeu Fabra, 2012. http://hdl.handle.net/10803/84173.

Full text
APA, Harvard, Vancouver, ISO, and other styles
Abstract:
Breast cancer is the main cause of cancer death in women. Improved treatments, prevention programs and earlier detection are reducing the rate of death; however, there is still a high percentage of mortality by this cancer. Identification of novel targets to predict response to specific treatments is a key goal for personalizing breast cancer therapy and to improve survival. Few years ago, PARP inhibitors appeared as a promising therapy, particularly in BRCA-mutated cancers. However, there was a clear need to conduct further preclinical and translational work to improve the rational development of PARP inhibition in breast cancer. In this work we described PARP1 expression in breast tumour samples and characterized the effects of its inhibition in preclinical models. We found that nuclear PARP1 protein overexpression was associated with malignant transformation and poor prognosis in breast cancer. PARP1 overexpression was more common in triple negative subtype, but was also detectable in small subsets of estrogen receptor positive and HER2 positive breast cancers. In preclinical models, PARP1 played distinct roles in different molecular subtypes of breast cancer. Moreover, we described that olaparib (novel PARP inhibitor) had antitumour effects in different breast cancer subtypes, and its combination with trastuzumab (anti-HER2 antibody) enhanced the antitumour effects of this therapy.
El càncer de mama és la principal causa de mort per càncer en dones. La millora dels tractaments i la detecció precoç estan reduint la taxa de mort, però segueix sent elevada. Identificar noves dianes per predir la resposta a tractaments és clau per millorar les teràpies contra aquest càncer i la supervivència. Els inhibidors de PARP van aparèixer com una teràpia prometedora, particularment en càncers BRCA-mutants, però, cal dur a terme més estudis preclínics i translacionals per fomentar un desenvolupament racional d’aquesta teràpia en càncer de mama. Aquest treball descriu l’expressió de PARP1 en mostres de tumors mamaris i caracteritza els efectes de la seva inhibició a models preclínics. Vam observar que la sobreexpressió nuclear de la proteïna PARP1 fou associada amb: la transformació maligna; mal pronòstic en càncer de mama; i fou més freqüent al subtipus triple-negatiu, però també es va detectar en un subgrup de càncers de mama receptors d’estrogen positius i HER2 positius. En models preclínics, PARP1 va exercir rols diferents als diferents subtipus de càncer de mama. Per altra banda, vam descriure que olaparib (inhibidor de PARP) té efectes antitumorals en els diversos subtipus, i combinat amb trastuzumab (anticòs anti-HER2) potencia els efectes antitumorals d’aquesta teràpia.
10

Ordway, Gregory A. "Potential Role of Brain Poly (ADP-ribose) Polymerase 1 (PARP1) in the Pathology of Major Depressive Disorder and Suicide." Digital Commons @ East Tennessee State University, 2019. https://dc.etsu.edu/etsu-works/8644.

Full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Books on the topic "PARP1":

1

Giammartino, Dafne Campigli Di. Elucidating the roles of PARP1 and RBBP6 in the regulation of pre-mRNA 3' end processing. [New York, N.Y.?]: [publisher not identified], 2014.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
2

McNaughton, Colin. Parp! London: Collins, 2001.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
3

Provan, Andrew B. MCQ's in medicine for MRCP Part1. Edinburgh: Churchill Livingstone, 1989.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
4

Curtin, Nicola J., and Ricky A. Sharma, eds. PARP Inhibitors for Cancer Therapy. Cham: Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-14151-0.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Karau, Paul, and Ian Pope. The Forest of Dean Branch Part1&2. 1-3 Hagbourne Rd Didcot Oxen OX11 8DP: Wild Swan Publications Ltd, 1992.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
6

Lacy, Jessica. Imaging of PARP1/2-Overexpressing Cancers with Novel AZD2281-Derived Probes. 2014.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
7

Henson, Mike, and Eugene & Eugene & Louise. Parp! Quarto Publishing Group UK, 2022.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
8

G, Jill. Sagittarius Part1. Independently Published, 2019.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
9

Talesh, Koroush Taheri, Flaviana Soares Rocha, Esshagh Lassemi, and Massoud Seifi. Oral Surgery Part1. DI Press, 2022.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
10

Mullenax, P. L. Brinewall Legacy Part1. Independently Published, 2017.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Book chapters on the topic "PARP1":

1

Kutuzov, M. M., E. A. Belousova, E. S. Ilina, and O. I. Lavrik. "Impact of PARP1, PARP2 & PARP3 on the Base Excision Repair of Nucleosomal DNA." In Advances in Experimental Medicine and Biology, 47–57. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-41283-8_4.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Lodhi, Niraj, and Alexei V. Tulin. "PARP1 Genomics: Chromatin Immunoprecipitation Approach Using Anti-PARP1 Antibody (ChIP and ChIP-seq)." In Methods in Molecular Biology, 191–208. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-270-0_12.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Lutfi, Nura, Carlos Martínez, and José Yélamos. "Studying the Immunomodulatory Functions of PARP1 and PARP2 in Mouse Models of Cancer." In Methods in Molecular Biology, 195–212. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2891-1_12.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Kotova, Elena, Aaron D. Pinnola, and Alexei V. Tulin. "Small-Molecule Collection and High-Throughput Colorimetric Assay to Identify PARP1 Inhibitors." In Methods in Molecular Biology, 491–516. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-270-0_29.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Bordet, Guillaume, and Alexei V. Tulin. "Using Drosophila Genetics to Identify Factors that Affect PARP1 Activity In Vivo." In Methods in Molecular Biology, 339–52. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2891-1_20.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Dhahri, Hejer, Elena Matveeva, and Yvonne Fondufe-Mittendorf. "Approach to Measuring the Effect of PARP1 on RNA Polymerase II Elongation Rates." In Methods in Molecular Biology, 315–28. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2891-1_18.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Rudolph, Johannes, and Karolin Luger. "Analyzing PARP1 Activity: Small Molecule Reactants and Attached Chains of Poly (ADP-Ribose)." In Methods in Molecular Biology, 61–73. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2891-1_4.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Bordet, Guillaume, Gbolahan Bamgbose, Sayem H. Bhuiyam, Sarah Johnson, and Alexei V. Tulin. "Chromatin Immunoprecipitation Approach to Determine How PARP1 Domains Affect Binding Pattern to Chromatin." In Methods in Molecular Biology, 297–313. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-2891-1_17.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Melikishvili, Manana, Elena Matveeva, and Yvonne Fondufe-Mittendorf. "Methodology to Identify Poly-ADP-Ribose Polymerase 1 (PARP1)–mRNA Targets by PAR-CLiP." In Methods in Molecular Biology, 211–28. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-6993-7_15.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Melikishvili, Manana, Elena Matveeva, and Yvonne Fondufe-Mittendorf. "Erratum to: Methodology to Identify Poly-ADP-Ribose Polymerase 1 (PARP1)–mRNA Targets by PAR-CLiP." In Methods in Molecular Biology, E1. New York, NY: Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-6993-7_30.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Conference papers on the topic "PARP1":

1

Pignochino, Ymera, Federica Capozzi, Lorenzo D’ambrosio, Carmine Dell’aglio, Marco Basiricò, Paola Boccone, Erica Palesandro, et al. "Abstract 3709: PARP1 expression (PARP1expr) drives synergy between PARP1 inhibitors (PARP1-Is) and trabectedin (TR)." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-3709.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Chen, Hua-Dong, Chuan-Huizi Chen, Yu-Ting Wang, Ne Guo, Yu-Nan Tian, Xia-Juan Huan, Shan-Shan Song, Jin-Xue He, and Ze-Hong Miao. "Abstract 2936: Increased PARP1-DNA binding due to autoPARylation inhibition of PARP1 on DNA rather than PARP1-DNA trapping is correlated with PARP1 inhibitor's cytotoxicity." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-2936.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Chen, Hua-Dong, Chuan-Huizi Chen, Yu-Ting Wang, Ne Guo, Yu-Nan Tian, Xia-Juan Huan, Shan-Shan Song, Jin-Xue He, and Ze-Hong Miao. "Abstract 2936: Increased PARP1-DNA binding due to autoPARylation inhibition of PARP1 on DNA rather than PARP1-DNA trapping is correlated with PARP1 inhibitor's cytotoxicity." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-2936.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Hopkins, Todd A., Yan Y. Shi, Enrico L. DiGiammarino, Sanjay C. Panchal, Gui-Dong G. Zhu, Thomas D. Penning, Eric F. Johnson, and David Maag. "Abstract 2850: Talazoparib (BMN-673) possesses greater PARP1 trapping activity than structurally distinct PARP inhibitors with identical PARP1 binding properties." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-2850.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

"PARP1 and PARP2 affinity to the lessions in the context of nucleosomes." In Bioinformatics of Genome Regulation and Structure/ Systems Biology. institute of cytology and genetics siberian branch of the russian academy of science, Novosibirsk State University, 2020. http://dx.doi.org/10.18699/bgrs/sb-2020-356.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

"YB-1 as modulator of PARP1 activity." In Bioinformatics of Genome Regulation and Structure/ Systems Biology. institute of cytology and genetics siberian branch of the russian academy of science, Novosibirsk State University, 2020. http://dx.doi.org/10.18699/bgrs/sb-2020-363.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

"HPF1 can promote opposite effects on different stages of PARP1 and PARP2 autoPARylation and histone modification." In Bioinformatics of Genome Regulation and Structure/Systems Biology (BGRS/SB-2022) :. Institute of Cytology and Genetics, the Siberian Branch of the Russian Academy of Sciences, 2022. http://dx.doi.org/10.18699/sbb-2022-588.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

"Regulation of PARP1 activity by its protein partners." In Bioinformatics of Genome Regulation and Structure/Systems Biology (BGRS/SB-2022) :. Institute of Cytology and Genetics, the Siberian Branch of the Russian Academy of Sciences, 2022. http://dx.doi.org/10.18699/sbb-2022-593.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

"TOP1, TDP1 and PARP1 inhibition: coupling and association." In Bioinformatics of Genome Regulation and Structure/Systems Biology (BGRS/SB-2022) :. Institute of Cytology and Genetics, the Siberian Branch of the Russian Academy of Sciences, 2022. http://dx.doi.org/10.18699/sbb-2022-577.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Gill, Sonja J., Ruth Macdonald, Carmen Pin, Rob Collins, Emilyanne Leonard, Gareth Maglennon, Andy Pike, et al. "Abstract 1374: The novel PARP1-selective inhibitor AZD5305 has reduced hematological toxicity when compared to PARP1/2 inhibitors in pre-clinical models." In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-1374.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Reports on the topic "PARP1":

1

Ting, Aili. Secondary Radiation in LIGA Exposure Part1. The Influence of X-Rays Scattering. Office of Scientific and Technical Information (OSTI), May 2001. http://dx.doi.org/10.2172/787889.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Yazinski, Stephanie. Novel Mechanisms of PARP Inhibitor Resistance in BRCA1-Deficient Breast Cancers. Fort Belvoir, VA: Defense Technical Information Center, December 2013. http://dx.doi.org/10.21236/ada612869.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Yazinski, Stephanie. Novel Mechanisms of PARP Inhibitor Resistance in BRCA1-Deficient Breast Cancers. Fort Belvoir, VA: Defense Technical Information Center, December 2014. http://dx.doi.org/10.21236/ada614186.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Cai, Zhaolun, Chunyu Liu, Chen Chang, Chaoyong Shen, Yuan Yin, Xiaonan Yin, Zhiyuan Jiang, et al. Comparative safety of PARP inhibitors in cancer: A network meta-analysis. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, March 2021. http://dx.doi.org/10.37766/inplasy2021.3.0018.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Dent, Paul, and Yong Tang. PARP Inhibitors Synergize With Loss of Checkpoint Control to Kill Mammary Carcinoma Cells. Fort Belvoir, VA: Defense Technical Information Center, June 2011. http://dx.doi.org/10.21236/ada555901.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Langton, C. EVALUATION OF SULFATE ATTACK ON SALTSTONE VAULT CONCRETE AND SALTSTONESIMCO TECHNOLOGIES, INC. PART1 FINAL REPORT. Office of Scientific and Technical Information (OSTI), August 2008. http://dx.doi.org/10.2172/944877.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Konstantinopoulos, Panagiotis. A Gene Expression Profile of BRCAness that Predicts for Responsiveness to Platinum and PARP Inhibitors. Fort Belvoir, VA: Defense Technical Information Center, August 2014. http://dx.doi.org/10.21236/ada613331.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Zhang, Meilin, Jian Song, Hongguang Yang, Feng Jin, and Ang Zheng. Efficacy and safety of PARP inhibitors in breast cancer: a systematic review and meta-analysis. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, October 2022. http://dx.doi.org/10.37766/inplasy2022.10.0105.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Shao, Fengping, Shanyang He, Yanyun Duan, Yunhe Zhao, Yinguang LI, and Lan Jing. A meta-analysis of efficacy of PARP inhibitors versus conventional therapy or placebo in various cancers patients. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, June 2020. http://dx.doi.org/10.37766/inplasy2020.6.0013.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Shea, Lonnie D. Identification of a PARP Inhibitor Sensitivity Signature in Breast Cancer Using a Novel Transcription Factor Activity Array. Fort Belvoir, VA: Defense Technical Information Center, March 2012. http://dx.doi.org/10.21236/ada559941.

Full text
APA, Harvard, Vancouver, ISO, and other styles

To the bibliography