PCNA, the Maestro of the Replication Fork

DNA methylation patterns and epigenetic memory

Bird, A. (2002) · Genes & Development · doi:10.1101/gad.947102 · Cited by 7,124

Molecular Mechanisms of Mammalian DNA Repair and the DNA Damage Checkpoints

Sancar, A., Lindsey-Boltz, L. A., Ünsal-Kaçmaz, K., & Linn, S. (2004) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.073723 · Cited by 3,317

RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO

Hoege, C., Pfander, B., Moldovan, G., Pyrowolakis, G., & Jentsch, S. (2002) · Nature · doi:10.1038/nature00991 · Cited by 2,202

DNA Replication in Eukaryotic Cells

Bell, S. P., & Dutta, A. (2002) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.71.110601.135425 · Cited by 2,065

The p21 inhibitor of cyclin-dependent kinases controls DNA replication by interaction with PCNA

Waga, S., Hannon, G. J., Beach, D., & Stillman, B. (1994) · Nature · doi:10.1038/369574a0 · Cited by 1,655

The multifaceted mismatch-repair system

Jiricny, J. (2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1907 · Cited by 1,375

Human DNA-(Cytosine-5) Methyltransferase-PCNA Complex as a Target for p21 WAF1

Chuang, L. S.-H., Ian, H.-I., Koh, T., Ng, H., Xu, G., & Li, B. F. L. (1997) · Science · doi:10.1126/science.277.5334.1996 · Cited by 902

Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation

Stelter, P., & Ulrich, H. D. (2003) · Nature · doi:10.1038/nature01965 · Cited by 850

Interaction of Human DNA Polymerase η with Monoubiquitinated PCNA

Kannouche, P. L., Wing, J., & Lehmann, A. R. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00259-x · Cited by 845

NMR Structure of the Human Rad18 Zinc Finger in Complex with Ubiquitin Defines a Class of UBZ Domains in Proteins Linked to the DNA Damage Response

Rizzo, A. A., Salerno, P., Bezsonova, I., & Korzhnev, D. M. (2014) · Biochemistry · doi:10.1021/bi500823h · Cited by 35

An intranucleolar body associated with rDNA

Hutten, S., Prescott, A. R., James, J. L., Riesenberg, S., Boulon, S., Lam, Y. W., & Lamond, A. I. (2011) · Chromosoma · doi:10.1007/s00412-011-0327-8 · Cited by 34

DNA Damage-induced Ubiquitylation of RFC2 Subunit of Replication Factor C Complex

Tomida, J., Masuda, Y., Hiroaki, H., Ishikawa, T., Song, I. Y., Tsurimoto, T., Tateishi, S., Shiomi, T., Kamei, Y., Kim, J., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m709835200 · Cited by 37

Antitumor Effects of a Novel Small Molecule Targeting PCNA Chromatin Association in Prostate Cancer

McKillip, K. D., Lu, S., & Dong, Z. (2014) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-14-0522 · Cited by 35

PARI Overexpression Promotes Genomic Instability and Pancreatic Tumorigenesis

O’Connor, K. W., Dejsuphong, D., Park, E., Nicolae, C. M., Kimmelman, A. C., D’Andrea, A. D., & Moldovan, G. (2013) · Cancer Research · doi:10.1158/0008-5472.can-12-3313 · Cited by 35

p21 Exploits Residue Tyr151 as a Tether for High-Affinity PCNA Binding

Kroker, A. J., & Bruning, J. B. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00241 · Cited by 35

Structure of the human RAD17–RFC clamp loader and 9–1–1 checkpoint clamp bound to a dsDNA–ssDNA junction

Day, M., Oliver, A. W., & Pearl, L. H. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac588 · Cited by 32

Connexin‐mediated communication controls cell proliferation and is essential in retinal histogenesis

Kihara, A. H., Santos, T. O., Melo, E. J. O., Paschon, V., Vidal, K. S. M., Akamine, P. S., de Castro, L. M., Resende, R. R., Hamassaki‐Britto, D. E., & Britto, L. R. (2009) · International Journal of Developmental Neuroscience · doi:10.1016/j.ijdevneu.2009.09.006 · Cited by 34

Sequential assembly of translesion DNA polymerases at UV-induced DNA damage sites

Andersen, P. L., Xu, F., Ziola, B. R., McGregor, W. G., & Xiao, W. (2011) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-12-0938 · Cited by 35

Post-Translational Modification of Cellular Proteins by Ubiquitin and Ubiquitin-Like Molecules: Role in Cellular Senescence and Aging

Grillari, J., Grillari‐Voglauer, R., & Jansen‐Dürr, P. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-7002-2_13 · Cited by 36

Drug-Free Approach To Study the Unusual Cell Cycle of Giardia intestinalis

Horlock-Roberts, K., Reaume, C., Dayer, G., Ouellet, C., Cook, N., & Yee, J. (2017) · mSphere · doi:10.1128/msphere.00384-16 · Cited by 33

Inhibition of DNA replication by an anti-PCNA aptamer/PCNA complex

Kowalska, E., Bartnicki, F., Fujisawa, R., Bonarek, P., Hermanowicz, P., Tsurimoto, T., Muszyńska, K., & Strzałka, W. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx1184 · Cited by 34

Post-hepatectomy liver regeneration in the context of bile acid homeostasis and the gut-liver signaling axis

de Haan, L. R., van der Lely, S. J., Warps, A. K., Hofsink, Q., Olthof, P. B., de Keijzer, M. J., Lionarons, D. A., Dias, L. M., Bruinsma, B. G., Uygun, K., et al. (2018) · Journal of Clinical and Translational Research · doi:10.18053/jctres.04.201801.001 · Cited by 33

Functions of Multiple Clamp and Clamp-Loader Complexes in Eukaryotic DNA Replication

Ohashi, E., & Tsurimoto, T. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-981-10-6955-0_7 · Cited by 34

Hub genes and key pathways of non‑small lung cancer identified using bioinformatics

Tang, Q., Zhang, H., Kong, M., Mao, X., & Cao, X. (2018) · Oncology Letters · doi:10.3892/ol.2018.8882 · Cited by 34

Activity-based ubiquitin-protein probes reveal target protein specificity of deubiquitinating enzymes

Gong, P., Davidson, G. A., Gui, W., Yang, K., Bozza, W. P., & Zhuang, Z. (2018) · Chemical Science · doi:10.1039/c8sc01573b · Cited by 34

Unanchored Ubiquitin Chains, Revisited

Blount, J. R., Johnson, S. L., & Todi, S. V. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.582361 · Cited by 36

c-Myc-induced Aberrant DNA Synthesis and Activation of DNA Damage Response in p300 Knockdown Cells

Natesan, S., Kadeppagari, R., & Thimmapaya, B. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900776200 · Cited by 32

Dextran sulfate sodium-induced ulcerative colitis leads to increased hematopoiesis and induces both local as well as systemic genotoxicity in mice

Trivedi, P. P., & Jena, G. (2012) · Mutation Research/Genetic Toxicology and Environmental Mutagenesis · doi:10.1016/j.mrgentox.2012.03.001 · Cited by 34

Extracorporeal shock wave therapy with low-energy flux density inhibits hypertrophic scar formation in an animal model

Zhao, J., Zhang, B.-R., Hong, L., Shi, K., Wu, W., & Yu, J. (2018) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2018.3434 · Cited by 34

From bacteria to plants: A compendium of mismatch repair assays

Spampinato, C. P., Gómez, R., Galles, C., & Lario, L. D. (2009) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2009.07.001 · Cited by 34

Regulatory Role of Ubiquitin in Eukaryotic DNA Translesion Synthesis

Yang, K., Weinacht, C. P., & Zhuang, Z. (2013) · Biochemistry · doi:10.1021/bi400194r · Cited by 35

Dynamics of enzymatic interactions during short flap human Okazaki fragment processing by two forms of human DNA polymerase δ

Lin, S. H. S., Wang, X., Zhang, S., Zhang, Z., Lee, E. Y. C., & Lee, M. (2013) · DNA repair · doi:10.1016/j.dnarep.2013.08.008 · Cited by 33

Agnoprotein of polyomavirus BK interacts with proliferating cell nuclear antigen and inhibits DNA replication

Gerits, N., Johannessen, M., Tümmler, C., Walquist, M. J., Kostenko, S., Snapkov, I., van Loon, B., Ferrari, E. S., Hübscher, U., & Moens, U. L. (2015) · Virology Journal · doi:10.1186/s12985-014-0220-1 · Cited by 33

Comparative quantitative proteomics unveils putative mechanisms involved into mercury toxicity and tolerance in Tigriopus japonicus under multigenerational exposure scenario

Xu, X., Shi, L., & Wang, M. (2016) · Environmental Pollution · doi:10.1016/j.envpol.2016.08.087 · Cited by 33

Risks at the DNA Replication Fork: Effects upon Carcinogenesis and Tumor Heterogeneity

Mertz, T. M., Harcy, V., & Roberts, S. A. (2017) · Genes · doi:10.3390/genes8010046 · Cited by 34

Regulation of Replication Fork Advance and Stability by Nucleosome Assembly

Prado, F., & Maya‐Miles, D. (2017) · Genes · doi:10.3390/genes8020049 · Cited by 37

Avian Ganglioneuritis in Clinical Practice

Rossi, G., Dahlhausen, R. D., Galosi, L., & Orosz, S. E. (2017) · Veterinary Clinics of North America Exotic Animal Practice · doi:10.1016/j.cvex.2017.08.009 · Cited by 33

Transcriptional profiling of skeletal muscle reveals starvation response and compensatory growth in Spinibarbus hollandi

Yang, Y., Zhou, H., Hou, L., Xing, K., & Shu, H. (2019) · BMC Genomics · doi:10.1186/s12864-019-6345-2 · Cited by 32

PCNA Unloading Is Negatively Regulated by BET Proteins

Kang, M.-S., Kim, J., Ryu, E., Ha, N. Y., Hwang, S., Kim, B., Ra, J. S., Kim, Y. J., Hwang, J. M., Myung, K., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.11.114 · Cited by 30

Developmental titanium dioxide nanoparticle exposure induces oxidative stress and neurobehavioral changes in zebrafish

Chen, J., Lei, L., Mo, W., Dong, H., Li, J., Bai, C., Huang, K., Truong, L., Tanguay, R. L., Dong, Q., et al. (2021) · Aquatic Toxicology · doi:10.1016/j.aquatox.2021.105990 · Cited by 33

Endogenous protein tagging in medaka using a simplified CRISPR/Cas9 knock-in approach

Seleit, A., Aulehla, A., & Paix, A. (2021) · eLife · doi:10.7554/elife.75050 · Cited by 33

Functions and evolution of FAM111 serine proteases

Welter, A. L., & Machida, Y. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.1081166 · Cited by 35

Proliferating Cell Nuclear Antigen (PCNA) Interactions in Solution Studied by NMR

Biasio, A. D., Campos‐Olivas, R., Sánchez, R., López-Alonso, J. P., Pantoja‐Uceda, D., Merino, N., Villate, M., Martin-Garcia, J. M., Castillo, F., Luque, I., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0048390 · Cited by 33

The tail that wags the dog: p12, the smallest subunit of DNA polymerase δ, is degraded by ubiquitin ligases in response to DNA damage and during cell cycle progression

Lee, M., Zhang, S., Lin, S. H. S., Wang, X., Darżynkiewicz, Z., Zhang, Z., & Lee, E. (2013) · Cell Cycle · doi:10.4161/cc.27407 · Cited by 35

Dynamic and Nucleolin-Dependent Localization of Human Cytomegalovirus UL84 to the Periphery of Viral Replication Compartments and Nucleoli

Bender, B. J., Coen, D. M., & Strang, B. L. (2014) · Journal of Virology · doi:10.1128/jvi.01889-14 · Cited by 33

Structure of human DNA polymerase iota and the mechanism of DNA synthesis

Makarova, А. V., & Kulbachinskiy, A. V. (2012) · Biochemistry (Moscow) · doi:10.1134/s0006297912060016 · Cited by 33

PDIP38 is translocated to the spliceosomes/nuclear speckles in response to UV-induced DNA damage and is required for UV-induced alternative splicing of MDM2

Wong, A., Zhang, S., Mordue, D. G., WU, J. M., Zhang, Z., Darżynkiewicz, Z., Lee, E. Y. C., & Lee, M. (2013) · Cell Cycle · doi:10.4161/cc.26221 · Cited by 33

Differential expression of decorin, EGFR and cyclin D1 during mammary gland carcinogenesis in TA2 mice with spontaneous breast cancer

Gu, Y., Zhang, S., Wu, Q., Xu, S., Cui, Y., Yang, Z., Zhao, X., & Sun, B. (2010) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/1756-9966-29-6 · Cited by 33

Immunohistochemistry

Ramos, J. A., & Borst, L. B. (2016) · doi:10.1002/9781119181200.ch3 · Cited by 33

Epidermal Growth Factor Receptor Protects Proliferating Cell Nuclear Antigen from Cullin 4A Protein-mediated Proteolysis

Lo, Y., Ho, P.-C., & Wang, S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.388843 · Cited by 31

Crystal Structure of SUMO-Modified Proliferating Cell Nuclear Antigen

Freudenthal, B., Brogie, J. E., Gakhar, L., Kondratick, C. M., & Washington, M. T. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.12.015 · Cited by 34

Keeping chromatin quiet

Mermoud, J. E., Rowbotham, S. P., & Varga‐Weisz, P. (2011) · Cell Cycle · doi:10.4161/cc.10.23.18558 · Cited by 35

Chemical form of selenium differentially influences DNA repair pathways following exposure to lead nitrate

McKelvey, S. M., Horgan, K. A., & Murphy, R. A. (2014) · Journal of Trace Elements in Medicine and Biology · doi:10.1016/j.jtemb.2014.06.005 · Cited by 32

PCNA stimulates catalysis by structure-specific nucleases using two distinct mechanisms: substrate targeting and catalytic step

Hutton, R. D., Roberts, J. A., Penedo, J. C., & White, M. F. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn745 · Cited by 32

The helicase Pif1 functions in the template switching pathway of DNA damage bypass

García‐Rodríguez, N., Wong, R. P. C., & Ulrich, H. D. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky648 · Cited by 33

An Overview of Candidate Therapeutic Target Genes in Ovarian Cancer

Alexandrova, E., Pecoraro, G., Sellitto, A., Melone, V., Ferravante, C., Rocco, T., Guacci, A., Giurato, G., Nassa, G., Rizzo, F. M., et al. (2020) · Cancers · doi:10.3390/cancers12061470 · Cited by 32

Mechanisms of DNA−protein cross-link formation and repair

Wei, X., Peng, Y., Bryan, C., & Yang, K. (2021) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2021.140669 · Cited by 35

Targeting protein–protein interactions in the DNA damage response pathways for cancer chemotherapy

McPherson, K. S., & Korzhnev, D. M. (2021) · RSC Chemical Biology · doi:10.1039/d1cb00101a · Cited by 35

PCNA trimer instability inhibits translesion synthesis by DNA polymerase η and by DNA polymerase δ

Dieckman, L. M., & Washington, M. T. (2013) · DNA repair · doi:10.1016/j.dnarep.2013.02.007 · Cited by 32

Contributions of the individual hydrophobic clefts of the Escherichia coli sliding clamp to clamp loading, DNA replication and clamp recycling

Ponticelli, S. K. S., Duzen, J. M., & Sutton, M. D. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp128 · Cited by 32

Ca2+ signals coordinate zygotic polarization and cell cycle progression in the brown algaFucus serratus

Bothwell, J. H. F., Kisielewska, J., Genner, M. J., McAinsh, M. R., & Brownlee, C. (2008) · Development · doi:10.1242/dev.017558 · Cited by 32

Regulation by Polycomb and Trithorax Group Proteins in Arabidopsis

Álvarez-Venegas, R. (2010) · The Arabidopsis Book · doi:10.1199/tab.0128 · Cited by 36

Sumoylation and the DNA Damage Response

Cremona, C. A., Sarangi, P., & Zhao, X. (2012) · Biomolecules · doi:10.3390/biom2030376 · Cited by 32

PI3K Stimulates DNA Synthesis and Cell-Cycle Progression via Its p55PIK Regulatory Subunit Interaction with PCNA

Wang, G., Cao, X., Lai, S., Luo, X., Feng, Y., Xia, X., Yen, P. M., Gong, J., & Hu, J. (2013) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-12-0920 · Cited by 32

Structural basis for processive daughter-strand synthesis and proofreading by the human leading-strand DNA polymerase Pol ε

Roske, J. J., & Yeeles, J. T. P. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01370-y · Cited by 31

KG-135, enriched with selected ginsenosides, inhibits the proliferation of human prostate cancer cells in culture and inhibits xenograft growth in athymic mice

Yoo, J., Kwon, H. C., Kim, Y., Park, J. H., & Yang, H. O. (2009) · Cancer Letters · doi:10.1016/j.canlet.2009.08.008 · Cited by 31

Die Chemie und Biologie des Ubiquitin‐Signals

Spasser, L., & Brik, A. (2012) · Angewandte Chemie · doi:10.1002/ange.201200020 · Cited by 31

Proteomic Analyses of the Eukaryotic Replication Machinery

Cortez, D. (2017) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2017.03.002 · Cited by 32

DNA Replication Is Required for Circadian Clock Function by Regulating Rhythmic Nucleosome Composition

Liu, X., Dang, Y., Matsuura, T., He, Y., He, Q., Hong, C. I., & Liu, Y. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.05.029 · Cited by 31

Leflunomide-induced liver injury in mice: Involvement of TLR4 mediated activation of PI3K/mTOR/NFκB pathway

Elshaer, R. E., Tawfik, M. K., Nosseir, N., El-Ghaiesh, S. H., Toraih, E. A., Elsherbiny, N. M., & Zaitone, S. A. (2019) · Life Sciences · doi:10.1016/j.lfs.2019.116824 · Cited by 31

Calunduloside E inhibits HepG2 cell proliferation and migration via p38/JNK-HMGB1 signalling axis

Wang, S., Chen, X., Cheng, J. Q., Cai, T., Wu, X., Cheng, Z., Qi, S., & Qi, Z. (2021) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2021.05.005 · Cited by 31

RAD5a and REV3 function in two alternative pathways of DNA-damage tolerance in Arabidopsis

Wang, S., Wen, R., Shi, X., Lambrecht, A. D., Wang, H., & Xiao, W. (2011) · DNA repair · doi:10.1016/j.dnarep.2011.04.009 · Cited by 31

Reduced Stability and Increased Dynamics in the Human Proliferating Cell Nuclear Antigen (PCNA) Relative to the Yeast Homolog

Biasio, A. D., Sánchez, R., Prìeto, J., Villate, M., Campos‐Olivas, R., & Blanco, F. J. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016600 · Cited by 31

Drosophila SUUR protein associates with PCNA and binds chromatin in a cell cycle-dependent manner

Kolesnikova, T. D., Posukh, O. V., Andreyeva, E. N., Bebyakina, D. S., Ivankin, A. V., & Zhimulev, I. F. (2012) · Chromosoma · doi:10.1007/s00412-012-0390-9 · Cited by 31

Analysis of the Association of the Human Cytomegalovirus DNA Polymerase Subunit UL44 with the Viral DNA Replication Factor UL84

Strang, B. L., Sinigalia, E., Silva, L. A., Coen, D. M., & Loregian, A. (2009) · Journal of Virology · doi:10.1128/jvi.00663-09 · Cited by 31

Association of human cytomegalovirus proteins IRS1 and TRS1 with the viral DNA polymerase accessory subunit UL44

Strang, B. L., Geballe, A. P., & Coen, D. M. (2010) · Journal of General Virology · doi:10.1099/vir.0.022640-0 · Cited by 31

Assessing the link between BACH1/FANCJ and MLH1 in DNA crosslink repair

Cantor, S. B., & Xie, J. (2010) · Environmental and Molecular Mutagenesis · doi:10.1002/em.20568 · Cited by 29

p21 limits S phase DNA damage caused by the Wee1 inhibitor MK1775

Hauge, S., Macurek, L., & Syljuåsen, R. G. (2019) · Cell Cycle · doi:10.1080/15384101.2019.1593649 · Cited by 30

AKT inhibition impairs PCNA ubiquitylation and triggers synthetic lethality in homologous recombination-deficient cells submitted to replication stress

Villafañez, F., García, I. A., Carbajosa, S., Pansa, M. F., Mansilla, S., Llorens, M. C., Angiolini, V., Guantay, L., Jacobs, H., Madauss, K. P., et al. (2019) · Oncogene · doi:10.1038/s41388-019-0724-7 · Cited by 30

EZH2 promotes DNA replication by stabilizing interaction of POLδ and PCNA via methylation-mediated PCNA trimerization

A, P., Xu, X., Wang, C., Yang, J., Wang, S., Dai, J., & Ye, L. (2018) · Epigenetics & Chromatin · doi:10.1186/s13072-018-0213-1 · Cited by 30

The abundance of Rad51 protein in mouse embryonic stem cells is regulated at multiple levels

Tichy, E. D., Pillai, R., Deng, L., Tischfield, J. A., Hexley, P., Babcock, G. F., & Stambrook, P. J. (2012) · Stem Cell Research · doi:10.1016/j.scr.2012.05.004 · Cited by 30

Replication stress, a source of epigenetic aberrations in cancer?

Jasencakova, Z., & Groth, A. (2010) · BioEssays · doi:10.1002/bies.201000055 · Cited by 29

REV1 promotes PCNA monoubiquitylation through interacting with ubiquitylated RAD18

Wang, Z., Huang, M., Ma, X., Li, H., Tang, T.-S., & Guo, C. (2016) · Journal of Cell Science · doi:10.1242/jcs.179408 · Cited by 31

Interferon-Stimulated Gene 15 in the Control of Cellular Responses to Genotoxic Stress

Jeon, Y. J., Park, J. H., & Chung, C. H. (2017) · Molecules and Cells · doi:10.14348/molcells.2017.0027 · Cited by 30

The Inherent Asymmetry of DNA Replication

Snedeker, J. C., Wooten, M., & Chen, X. (2017) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100616-060447 · Cited by 34

Phosphorylation of proliferating cell nuclear antigen promotes cancer progression by activating the ATM/Akt/GSK3β/Snail signaling pathway

Peng, B., Ortega, J., Gu, L., Chang, Z., & Li, G. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.007897 · Cited by 30

Mitochondrial chaperone, TRAP1 modulates mitochondrial dynamics and promotes tumor metastasis

Dharaskar, S. P., Paithankar, K., Kanugovi, A., Kara, H. S., & Subbarao, S. A. (2020) · Mitochondrion · doi:10.1016/j.mito.2020.08.001 · Cited by 32

USP39 mediates p21‐dependent proliferation and neoplasia of colon cancer cells by regulating the p53/p21/CDC2/cyclin B1 axis

Yuan, J., Li, X., Zhang, G., Cheng, W., Wang, W., Lei, Y., Ma, Q., & Song, G. (2021) · Molecular Carcinogenesis · doi:10.1002/mc.23290 · Cited by 29

Targeting Non-Oncogene Addiction for Cancer Therapy

Chang, H. R., Jung, E., Cho, S., Jeon, Y.-J., & Kim, Y. (2021) · Biomolecules · doi:10.3390/biom11020129 · Cited by 30

Structure of PCNA in complex with DNMT1 PIP box reveals the basis for the molecular mechanism of the interaction

Jimenji, T., Matsumura, R., Kori, S., & Arita, K. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.06.060 · Cited by 30

The Functions of PCNA in Tumor Stemness and Invasion

Wang, Y., Wu, W., Lin, P., Shen, Y.-C., Lin, Y.-Z., Li, H., Hsu, K., & Wang, S. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23105679 · Cited by 30

Curcumin, Polydatin and Quercetin Synergistic Activity Protects from High-Glucose-Induced Inflammation and Oxidative Stress

Matacchione, G., Valli, D., Silvestrini, A., Giuliani, A., Sabbatinelli, J., Giordani, C., Coppari, S., Rippo, M. R., Albertini, M. C., & Olivieri, F. (2022) · Antioxidants · doi:10.3390/antiox11061037 · Cited by 32

pcaGoPromoter - An R Package for Biological and Regulatory Interpretation of Principal Components in Genome-Wide Gene Expression Data

Hansen, M., Gerds, T. A., Nielsen, O. H., Seidelin, J. B., Troelsen, J. T., & Olsen, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0032394 · Cited by 29

Biochemical properties and base excision repair complex formation of apurinic/apyrimidinic endonuclease from Pyrococcus furiosus

Kiyonari, S., Tahara, S., Shirai, T., Iwai, S., Ishino, S., & Ishino, Y. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp720 · Cited by 30

Targeting the Ubiquitin Proteasome System: Beyond Proteasome Inhibition

Xolalpa, W., Pérez‐Galán, P., Rodríguez, M. S., & Roué, G. (2013) · Current Pharmaceutical Design · doi:10.2174/1381612811319220014 · Cited by 30

The distribution pattern of proliferating cell nuclear antigen in the nuclei of Leishmania donovani

Kumar, D., Minocha, N., Rajanala, K., & Saha, S. (2009) · Microbiology · doi:10.1099/mic.0.033217-0 · Cited by 30

Error-Prone Splicing Controlled by the Ubiquitin Relative Hub1

Karaduman, R., Chanarat, S., Pfander, B., & Jentsch, S. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.06.021 · Cited by 30

A comparison of apoptosis levels in keloid tissue, physiological scars and normal skin.

Zhang, M., Dong, X., Guan, E., Si, L., Zhuge, R., Zhao, P., Zhang, X., Liu, M., Adzavon, Y. M., Long, X., et al. (2017) · PubMed Central · Cited by 30

CDK-independent role of D-type cyclins in regulating DNA mismatch repair

Róna, G., Miwatani-Minter, B., Zhang, Q., Goldberg, H. V., Kerzhnerman, M. A., Howard, J., Simoneschi, D., Lane, E., Hobbs, J. W., Sassani, E., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.02.010 · Cited by 34

A fluorescent bimolecular complementation screen reveals MAF1, RNF7 and SETD3 as PCNA-associated proteins in human cells

Cooper, S. E., Hodimont, E., & Green, C. (2015) · Cell Cycle · doi:10.1080/15384101.2015.1053667 · Cited by 30

Non-enzymatic synthesis of ubiquitin chains: Where chemistry makes a difference

Hemantha, H. P., & Brik, A. (2013) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2013.02.004 · Cited by 29

H3K56me1 Marks a Spot for PCNA

Lee, S., Jasencakova, Z., & Groth, A. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.03.022 · Cited by 29

miR-200a-3p promotes the proliferation of human esophageal cancer cells by post-transcriptionally regulating cytoplasmic collapsin response mediator protein-1

Zang, Y., Tai, Y., Wan, B., & Jia, X. (2016) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2016.2758 · Cited by 29

NEDDylation antagonizes ubiquitination of proliferating cell nuclear antigen and regulates the recruitment of polymerase η in response to oxidative DNA damage

Guan, J., Yu, S., & Zheng, X. (2017) · Protein & Cell · doi:10.1007/s13238-017-0455-x · Cited by 29

miR-29 promotes osteosarcoma cell proliferation and migration by targeting PTEN

Liu, Q., Geng, P., Shi, L., Wang, Q., & Wang, P. (2018) · Oncology Letters · doi:10.3892/ol.2018.9646 · Cited by 29

Cytotoxicity and genotoxicity of MWCNT-7 and crocidolite: assessment in alveolar epithelial cells versus their coculture with monocyte-derived macrophages

Ventura, C., Pereira, J., Matos, P., Marques, B., Jordan, P., Uva, A. D. S., & Silva, M. J. (2020) · Nanotoxicology · doi:10.1080/17435390.2019.1695975 · Cited by 30

Timely termination of repair DNA synthesis by ATAD5 is important in oxidative DNA damage-induced single-strand break repair

Park, S. H., Kim, Y., Ra, J. S., Wie, M., Kang, M.-S., Kang, S., Myung, K., & Lee, K. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab999 · Cited by 27

Long Non-Coding RNAs in Pancreatic Cancer: Biologic Functions, Mechanisms, and Clinical Significance

Li, J., Hou, S., Ye, Z., Wang, W., Hu, X., & Hang, Q. (2022) · Cancers · doi:10.3390/cancers14092115 · Cited by 30

African swine fever virus pE301R negatively regulates cGAS-STING signaling pathway by inhibiting the nuclear translocation of IRF3

Liu, X., Liu, H., Ye, G., Xue, M., Yu, H., Feng, C., Zhou, Q., Liu, X., Zhang, L., Jiao, S., et al. (2022) · Veterinary Microbiology · doi:10.1016/j.vetmic.2022.109556 · Cited by 29

Forging Ahead through Darkness: PCNA, Still the Principal Conductor at the Replication Fork

Choe, K. N., & Moldovan, G.-L. (2017) · Molecular Cell · doi:10.1016/j.molcel.2016.12.020 · Cited by 325

Ub‐family modifications at the replication fork: Regulating PCNA‐interacting components

Kirchmaier, A. L. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.08.008 · Cited by 26

The Many Roles of PCNA in Eukaryotic DNA Replication

Boehm, E. M., Gildenberg, M. S., & Washington, M. T. (2016) · The Enzymes · doi:10.1016/bs.enz.2016.03.003 · Cited by 306

3 PCNA and DNA replication (I)

Görisch, S. M., & Cardoso, M. C. (2015)

The fellowship of the rings: distinct pools of proliferating cell nuclear antigen trimer at work

Prosperi, E. (2006) · The FASEB Journal · doi:10.1096/fj.05-5469hyp · Cited by 42