A Cancer-Specific Ubiquitin Ligase Drives mRNA Alternative Polyadenylation by Ubiquitinating the mRNA 3′ End Processing Complex

STAR: ultrafast universal RNA-seq aligner

Dobin, A., Davis, C. A., Schlesinger, F., Drenkow, J., Zaleski, C., Jha, S., Batut, P., Chaisson, M., & Gingeras, T. R. (2013) · Bioinformatics · doi:10.1093/bioinformatics/bts635 · Cited by 51,709 · see citing works

BEDTools: a flexible suite of utilities for comparing genomic features

Quinlan, A. R., & Hall, I. M. (2010) · Bioinformatics · doi:10.1093/bioinformatics/btq033 · Cited by 27,437 · see citing works

HTSeq—a Python framework to work with high-throughput sequencing data

Anders, S., Pyl, P. T., & Huber, W. (2015) · Bioinformatics · doi:10.1093/bioinformatics/btu638 · Cited by 21,464 · see citing works

Differential expression analysis for sequence count data

Anders, S., & Huber, W. (2010) · Genome Biology · doi:10.1186/gb-2010-11-10-r106 · Cited by 15,581 · see citing works

Predicting effective microRNA target sites in mammalian mRNAs

Agarwal, V., Bell, G. W., Nam, J.-W., & Bartel, D. P. (2015) · eLife · doi:10.7554/elife.05005 · Cited by 7,318 · see citing works

A ceRNA Hypothesis: The Rosetta Stone of a Hidden RNA Language?

Salmena, L., Poliseno, L., Tay, Y., Kats, L., & Pandolfi, P. P. (2011) · Cell · doi:10.1016/j.cell.2011.07.014 · Cited by 7,262 · see citing works

Widespread Shortening of 3′UTRs by Alternative Cleavage and Polyadenylation Activates Oncogenes in Cancer Cells

Mayr, C., & Bartel, D. P. (2009) · Cell · doi:10.1016/j.cell.2009.06.016 · Cited by 1,613 · see citing works

Cancer/testis antigens, gametogenesis and cancer

Simpson, A. J. G., Caballero, O. L., Jungbluth, A. A., Chen, Y., & Old, L. J. (2005) · Nature reviews. Cancer · doi:10.1038/nrc1669 · Cited by 1,587 · see citing works

Proliferating Cells Express mRNAs with Shortened 3' Untranslated Regions and Fewer MicroRNA Target Sites

Sandberg, R., Neilson, J. R., Sarma, A., Sharp, P. A., & Burge, C. B. (2008) · Science · doi:10.1126/science.1155390 · Cited by 1,349 · see citing works

Alternative polyadenylation of mRNA precursors

Tian, B., & Manley, J. L. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.116 · Cited by 1,179 · see citing works

D-type cyclins

Sherr, C. J. (1995) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)89005-2 · Cited by 980 · see citing works

The proliferation gene expression signature is a quantitative integrator of oncogenic events that predicts survival in mantle cell lymphoma

Rosenwald, A., Wright, G. W., Wiestner, A. U., Chan, W. C., Connors, J. M., Campo, E., Gascoyne, R. D., Grogan, T. M., Müller-Hermelink, H. K., Smeland, E. B., et al. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00028-x · Cited by 905 · see citing works

Cumulative haploinsufficiency and triplosensitivity drive aneuploidy patterns and shape the cancer genome

Davoli, T., Xu, A. W., Mengwasser, K. E., Sack, L. M., Yoon, J. C., Park, P. J., & Elledge, S. J. (2013) · Cell · doi:10.1016/j.cell.2013.10.011 · Cited by 815 · see citing works

Alternative cleavage and polyadenylation: extent, regulation and function

Elkon, R., Ugalde, A. P., & Agami, R. (2013) · Nature Reviews Genetics · doi:10.1038/nrg3482 · Cited by 805 · see citing works

Cyclin D2 is an FSH-responsive gene involved in gonadal cell proliferation and oncogenesis

Siciński, P., Donaher, J. L., Geng, Y., Parker, S. B., Gardner, H., Park, M. Y., Robker, R. L., Richards, J. S., McGinnis, L. K., Biggers, J. D., et al. (1996) · Nature · doi:10.1038/384470a0 · Cited by 697 · see citing works

A quantitative atlas of polyadenylation in five mammalsPreprint

Derti, A., Garrett-Engele, P. W., MacIsaac, K. D., Stevens, R. C., Sriram, S., Chen, R., Rohl, C. A., Johnson, J. M., & Babak, T. (2012) · Genome Research · doi:10.1101/gr.132563.111 · Cited by 642 · see citing works

Progressive lengthening of 3′ untranslated regions of mRNAs by alternative polyadenylation during mouse embryonic development

Ji, Z., Lee, J. Y., Pan, Z., Jiang, B., & Tian, B. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900028106 · Cited by 595 · see citing works

Molecular Architecture of the Human Pre-mRNA 3′ Processing Complex

Shi, Y., Giammartino, D. C. D., Taylor, D. J., Sarkeshik, A., Rice, W. J., Yates, J. R., Frank, J., & Manley, J. L. (2009) · Molecular Cell · doi:10.1016/j.molcel.2008.12.028 · Cited by 560 · see citing works

Dynamic Analyses of Alternative Polyadenylation from RNA-Seq Reveal 3′-UTR Landscape Across 7 Tumor Types

Xia, Z., Donehower, L., Cooper, T., Neilson, J., Wheeler, D., Wagner, E., & Li, W. (2014) · Nature Communications · doi:10.1038/ncomms6274 · Cited by 509 · see citing works

Alternative poly(A) site selection in complex transcription units: means to an end?

Edwalds-Gilbert, G. (1997) · Nucleic Acids Research · doi:10.1093/nar/25.13.2547 · Cited by 509 · see citing works

MAGE-RING Protein Complexes Comprise a Family of E3 Ubiquitin Ligases

Doyle, J., Gao, J., Wang, J., Yang, M., & Potts, P. R. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.08.029 · Cited by 468 · see citing works

Cyclin D activates the Rb tumor suppressor by mono-phosphorylation

Narasimha, A. M., Kaulich, M., Shapiro, G. S., Choi, Y. J., Siciński, P., & Dowdy, S. F. (2014) · eLife · doi:10.7554/elife.02872 · Cited by 462 · see citing works

CFIm25 links alternative polyadenylation to glioblastoma tumour suppression

Masamha, C. P., Xia, Z., Yang, J., Albrecht, T. R., Li, M., Shyu, A., Li, W., & Wagner, E. J. (2014) · Nature · doi:10.1038/nature13261 · Cited by 449 · see citing works

Analysis of alternative cleavage and polyadenylation by 3′ region extraction and deep sequencing

Hoque, M., Ji, Z., Zheng, D., Luo, W., Li, W., You, B., Park, J. Y., Yehia, G., & Tian, B. (2012) · Nature Methods · doi:10.1038/nmeth.2288 · Cited by 442 · see citing works

Genome-Wide Analysis of MEF2 Transcriptional Program Reveals Synaptic Target Genes and Neuronal Activity-Dependent Polyadenylation Site Selection

Flavell, S. W., Kim, T.-K., Gray, J. M., Harmin, D. A., Hemberg, M., Hong, E. J., Markenscoff-Papadimitriou, E., Bear, D. M., & Greenberg, M. E. (2008) · Neuron · doi:10.1016/j.neuron.2008.11.029 · Cited by 440 · see citing works

Degradation of AMPK by a Cancer-Specific Ubiquitin Ligase

Pineda, C. T., Ramanathan, S., Fon Tacer, K., Weon, J. L., Potts, M. B., Ou, Y.-H., White, M. A., & Potts, P. R. (2015) · Cell · doi:10.1016/j.cell.2015.01.034 · Cited by 389 · see citing works

The UCSC Cancer Genomics Browser: update 2015

Goldman, M. J., Craft, B., Swatloski, T., Cline, M., Morozova, O., Diekhans, M., Haussler, D. H., & Zhu, J. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku1073 · Cited by 371 · see citing works

Genome-wide Analysis of Pre-mRNA 3′ End Processing Reveals a Decisive Role of Human Cleavage Factor I in the Regulation of 3′ UTR Length

Martin, G., Gruber, A. R., Keller, W., & Zavolan, M. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.05.003 · Cited by 361 · see citing works

The role of the 3' untranslated region in post-transcriptional regulation of protein expression in mammalian cells.

Matoulkova, E., Michalova, E., Vojtesek, B., & Hrstka, R. (2012) · RNA Biology · doi:10.4161/rna.20231 · Cited by 357 · see citing works

Widespread and extensive lengthening of 3′ UTRs in the mammalian brainPreprint

Miura, P., Shenker, S., Andreu-Agulló, C., Westholm, J. O., & Lai, E. C. (2013) · Genome Research · doi:10.1101/gr.146886.112 · Cited by 339 · see citing works

Functional Interaction of Yeast Pre-mRNA 3′ End Processing Factors with RNA Polymerase II

Licatalosi, D. D., Geiger, G., Minet, M., Schroeder, S. C., Cilli, K., McNeil, J. B., & Bentley, D. L. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00518-x · Cited by 316 · see citing works

Recognition of RNA polymerase II carboxy-terminal domain by 3′-RNA-processing factors

Meinhart, A., & Cramer, P. (2004) · Nature · doi:10.1038/nature02679 · Cited by 315 · see citing works

Differential genome-wide profiling of tandem 3′ UTRs among human breast cancer and normal cells by high-throughput sequencingPreprint

Fu, Y., Sun, Y., Li, Y., Li, J., Rao, X., Chen, C., & Xu, A. (2011) · Genome Research · doi:10.1101/gr.115295.110 · Cited by 270 · see citing works

Reprogramming of 3′ Untranslated Regions of mRNAs by Alternative Polyadenylation in Generation of Pluripotent Stem Cells from Different Cell Types

Ji, Z., & Tian, B. (2009) · PLoS ONE · doi:10.1371/journal.pone.0008419 · Cited by 264 · see citing works

Systematic Profiling of Poly(A)+ Transcripts Modulated by Core 3’ End Processing and Splicing Factors Reveals Regulatory Rules of Alternative Cleavage and Polyadenylation

Li, W., You, B., Hoque, M., Zheng, D., Luo, W., Ji, Z., Park, J. Y., Gunderson, S., Kalsotra, A., Manley, J. L., et al. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005166 · Cited by 263 · see citing works

The MAGE protein family and cancer

Weon, J. L., & Potts, P. R. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2015.08.002 · Cited by 257 · see citing works

PolyA_DB 3 catalogs cleavage and polyadenylation sites identified by deep sequencing in multiple genomes

Wang, R., Nambiar, R., Zheng, D., & Tian, B. (2018) · Nucleic Acids Research · doi:10.1093/nar/gkx1000 · Cited by 239 · see citing works

Regulation of WASH-Dependent Actin Polymerization and Protein Trafficking by Ubiquitination

Hao, Y.-H., Doyle, J., Ramanathan, S., Gomez, T. S., Jia, D., Xu, M., Chen, Z. J., Billadeau, D. D., Rosen, M. K., & Potts, P. R. (2013) · Cell · doi:10.1016/j.cell.2013.01.051 · Cited by 238 · see citing works

Levels of Polyadenylation Factor CstF-64 Control IgM Heavy Chain mRNA Accumulation and Other Events Associated with B Cell Differentiation

Takagaki, Y., & Manley, J. L. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80291-9 · Cited by 223 · see citing works

Molecular Mechanisms for CFIm-Mediated Regulation of mRNA Alternative Polyadenylation

Zhu, Y., Wang, X., Forouzmand, E., Jeong, J., Qiao, F., Sowd, G. A., Engelman, A., Xie, X. S., Hertel, K. J., & Shi, Y. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.11.031 · Cited by 221 · see citing works

Loss of cyclin D2 expression in the majority of breast cancers is associated with promoter hypermethylation.

Evron, E., Umbricht, C. B., Korz, D., Raman, V., Loeb, D. M., Niranjan, B., Buluwela, L., Weitzman, S. A., Marks, J. R., & Sukumar, S. V. (2001) · PubMed · Cited by 212 · see citing works

Transcriptome-wide analyses of CstF64–RNA interactions in global regulation of mRNA alternative polyadenylation

Yao, C., Biesinger, J., Wan, J., Weng, L., Xing, Y., Xie, X. S., & Shi, Y. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1211101109 · Cited by 209 · see citing works

USP7 acts as a molecular rheostat to promote WASH-dependent endosomal protein recycling and is mutated in a human neurodevelopmental disorder.

Hao, Y.-H., Fountain, M. D., Fon Tacer, K., Xia, F., Bi, W., Kang, S.-H. L., Patel, A., Rosenfeld, J. A., Le Caignec, C., Isidor, B., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.07.033 · Cited by 206 · see citing works

miRmine: a database of human miRNA expression profiles

Panwar, B., Omenn, G. S., & Guan, Y. (2017) · Bioinformatics · doi:10.1093/bioinformatics/btx019 · Cited by 198 · see citing works

JUMP: a tag-based database search tool for peptide identification with high sensitivity and accuracy

Wang, X., Li, Y., Wu, Z., Wang, H., Tan, H., & Peng, J. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o114.039586 · Cited by 194 · see citing works

3′ UTR shortening represses tumor-suppressor genes in trans by disrupting ceRNA crosstalk

Park, H. J., Ji, P., Kim, S., Xia, Z., Rodriguez, B. A. T., Li, L., Su, J., Chen, K., Masamha, C. P., Baillat, D., et al. (2018) · Nature Genetics · doi:10.1038/s41588-018-0118-8 · Cited by 180 · see citing works

CRIS.py: A Versatile and High-throughput Analysis Program for CRISPR-based Genome Editing

Connelly, J. P., & Pruett‐Miller, S. M. (2019) · Scientific Reports · doi:10.1038/s41598-019-40896-w · Cited by 174 · see citing works

Cyclin D2 Overexpression and Lack of p27 Correlate Positively and Cyclin E Inversely with a Poor Prognosis in Gastric Cancer Cases

Takano, Y., Kato, Y., van Diest, P. J., Masuda, M., Mitomi, H., & Okayasu, I. (2000) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64763-3 · Cited by 159 · see citing works

Estrogen Mediated-Activation of miR-191/425 Cluster Modulates Tumorigenicity of Breast Cancer Cells Depending on Estrogen Receptor Status

Leva, G. D., Piovan, C., Gasparini, P., Ngankeu, A., Taccioli, C., Briskin, D., Cheung, D. G., Bolon, B. N., Anderlucci, L., Alder, H., et al. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003311 · Cited by 156 · see citing works

Cotranscriptional Recruitment of the mRNA Export Factor Yra1 by Direct Interaction with the 3′ End Processing Factor Pcf11

Johnson, S. A., Cubberley, G., & Bentley, D. L. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.12.007 · Cited by 153 · see citing works

Selective Roles of Vertebrate PCF11 in Premature and Full-Length Transcript Termination

Kamieniarz-Gdula, K., Gdula, M. R., Panser, K., Nojima, T., Monks, J., Wiśniewski, J. R., Riepsaame, J., Brockdorff, N., Pauli, A., & Proudfoot, N. J. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.01.027 · Cited by 141 · see citing works

A Comprehensive Guide to the MAGE Family of Ubiquitin Ligases

Lee, A. K., & Potts, P. R. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.03.005 · Cited by 136 · see citing works

Melanoma Antigen Gene Protein MAGE-11 Regulates Androgen Receptor Function by Modulating the Interdomain Interaction

Bai, S., He, B., & Wilson, E. M. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.4.1238-1257.2005 · Cited by 133 · see citing works

Alternative 3′ UTRs direct localization of functionally diverse protein isoforms in neuronal compartments

Mattioli, C. C., Rom, A., Franke, V., Imami, K., Arrey, G., Terne, M., Woehler, A., Akalin, A., Ulitsky, I., & Chekulaeva, M. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky1270 · Cited by 125 · see citing works

TC3A: The Cancer 3′ UTR Atlas

Feng, X., Li, L., Wagner, E. J., & Li, W. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx892 · Cited by 123 · see citing works

Genome-wide Analysis of RNA Polymerase II Termination at Protein-Coding Genes

Baejen, C., Andréani, J., Torkler, P., Battaglia, S., Schwalb, B., Lidschreiber, M., Maier, K. C., Boltendahl, A., Rus, P., Esslinger, S., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.02.009 · Cited by 122 · see citing works

Deep Profiling of Proteome and Phosphoproteome by Isobaric Labeling, Extensive Liquid Chromatography, and Mass Spectrometry

Bai, B., Tan, H., Pagala, V., High, A. A., Ichhaporia, V. P., Hendershot, L. M., & Peng, J. (2016) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2016.10.007 · Cited by 119 · see citing works

Extensive Peptide Fractionation and <i>y</i>₁ Ion-Based Interference Detection Method for Enabling Accurate Quantification by Isobaric Labeling and Mass Spectrometry

Niu, M., Cho, J.-H., Kodali, K., Pagala, V., High, A. A., Wang, H., Wu, Z., Li, Y., Bi, W., Zhang, H., et al. (2017) · Analytical Chemistry · doi:10.1021/acs.analchem.6b04415 · Cited by 118 · see citing works

APAtrap: identification and quantification of alternative polyadenylation sites from RNA-seq data

Ye, C., Long, Y., Ji, G., Li, Q. Q., & Wu, X. (2018) · Bioinformatics · doi:10.1093/bioinformatics/bty029 · Cited by 115 · see citing works

Expression of D-type cyclins in colon cancer and in cell lines from colon carcinomas

Mermelshtein, A., Gerson, A., Walfisch, S., et al. (2005) · British Journal of Cancer · doi:10.1038/sj.bjc.6602709 · Cited by 103 · see citing works

The Non-coding 3′UTR of CD44 Induces Metastasis by Regulating Extracellular Matrix Functions

Jeyapalan, Z., & Yang, B. B. (2012) · Journal of Cell Science · doi:10.1242/jcs.100818 · Cited by 103 · see citing works

Transcriptome 3′end organization by PCF11 links alternative polyadenylation to formation and neuronal differentiation of neuroblastoma

Ogorodnikov, A., Levin, M., Tattikota, S., Tokalov, S., Hoque, M., Scherzinger, D., Marini, F., Poetsch, A., Binder, H., Macher-Göppinger, S., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-07580-5 · Cited by 95 · see citing works

3’UTR Shortening Potentiates MicroRNA-Based Repression of Pro-differentiation Genes in Proliferating Human Cells

Hoffman, Y., Bublik, D. R., P. Ugalde, A., Elkon, R., Biniashvili, T., Agami, R., Oren, M., & Pilpel, Y. (2016) · PLOS Genetics · doi:10.1371/journal.pgen.1005879 · Cited by 90 · see citing works

Ubiquitin‐Activated Interaction Traps (UBAITs) identify E3 ligase binding partners

O’Connor, H. F., Lyon, N., Leung, J. W. C., Agarwal, P., Swaim, C. D., Miller, K. M., & Huibregtse, J. M. (2015) · EMBO Reports · doi:10.15252/embr.201540620 · Cited by 85 · see citing works

Alternative cleavage and polyadenylation in spermatogenesis connects chromatin regulation with post-transcriptional control

Li, W., Park, J. Y., Zheng, D., Hoque, M., Yehia, G., & Tian, B. (2016) · BMC Biology · doi:10.1186/s12915-016-0229-6 · Cited by 84 · see citing works

Reexamining the polyadenylation signal: were we wrong about AAUAAA?

MacDonald, C. C., & Redondo, J.-L. (2002) · Molecular and Cellular Endocrinology · doi:10.1016/s0303-7207(02)00044-8 · Cited by 83 · see citing works

Quantitative Protein Analysis by Mass Spectrometry

Pagala, V., High, A. A., Wang, X., Tan, H., Kodali, K., Mishra, A., Kavdia, K., Xu, Y., Wu, Z., & Peng, J. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2425-7_17 · Cited by 66 · see citing works

Pre-Messenger RNA Cleavage Factor I (CFIm): Potential Role in Alternative Polyadenylation During Spermatogenesis1

Sartini, B. L., Wang, H., Wang, W., et al. (2007) · Biology of Reproduction · doi:10.1095/biolreprod.107.064774 · Cited by 61 · see citing works

HUWE1 interacts with PCNA to alleviate replication stress

Choe, K. N., Nicolae, C. M., Constantin, D., Kawasawa, Y. I., Delgado‐Diaz, M. R., De, S., Freire, R., Smits, V. A. J., & Moldovan, G. (2016) · EMBO Reports · doi:10.15252/embr.201541685 · Cited by 59 · see citing works

Tissue‐specific mechanisms of alternative polyadenylation: Testis, brain, and beyond (2018 update)

MacDonald, C. C. (2019) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1526 · Cited by 57 · see citing works

Cross-Linking Immunoprecipitation and qPCR (CLIP-qPCR) Analysis to Map Interactions Between Long Noncoding RNAs and RNA-Binding Proteins

Yoon, J., & Gorospe, M. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-3378-5_2 · Cited by 48 · see citing works

Expressions of MAGE-A10 and MAGE-A11 in breast cancers and their prognostic significance: a retrospective clinical study

Lian, Y., Sang, M., Ding, C., et al. (2011) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-011-1122-x · Cited by 47 · see citing works

Cytosolic Iron-Sulfur Assembly Is Evolutionarily Tuned by a Cancer-Amplified Ubiquitin Ligase

Weon, J. L., Yang, S. W., & Potts, P. R. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.11.010 · Cited by 46 · see citing works

Proto-oncogene Activity of Melanoma Antigen-A11 (MAGE-A11) Regulates Retinoblastoma-related p107 and E2F1 Proteins

Su, S., Minges, J. T., Grossman, G., Blackwelder, A. J., Mohler, J. L., & Wilson, E. M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.468579 · Cited by 38 · see citing works

Structures of Two Melanoma-Associated Antigens Suggest Allosteric Regulation of Effector Binding

Newman, J. A., Cooper, C. D. O., Roos, A. K., Aitkenhead, H., Oppermann, U. C. T., Cho, H. J., Osman, R., & Gileadi, O. (2016) · PLoS ONE · doi:10.1371/journal.pone.0148762 · Cited by 37 · see citing works

Merkel cells in the human oesophagus

Harmse, J. L., Carey, F. A., Baird, A., Craig, S., Christie, K. N., Hopwood, D., & Lucocq, J. M. (1999) · Journal of Pathology · doi:10.1002/(sici)1096-9896(199910)189:2 · Cited by 33 · see citing works

Ubiquitin Ligase Huwe1 Modulates Spermatogenesis by Regulating Spermatogonial Differentiation and Entry into Meiosis

Bose, R., Sheng, K., Moawad, A. R. R., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-17902-0 · Cited by 25 · see citing works

Overexpression of the 3′-Untranslated Region of Myelin Proteolipid Protein mRNA Leads to Reduced Expression of Endogenous Proteolipid mRNA

Mallon, B. S., & Macklin, W. B. (2002) · Neurochemical Research · doi:10.1023/a:1021623700009 · Cited by 22 · see citing works

Differences in polyadenylation site choice between somatic and male germ cells

McMahon, K. W., Hirsch, B. A., & MacDonald, C. C. (2006) · BMC Molecular Biology · doi:10.1186/1471-2199-7-35 · Cited by 21 · see citing works

WNK1 kinase and the termination factor PCF11 connect nuclear mRNA export with transcriptionPreprint

Volanakis, A., Kamieniarz-Gdula, K., Schlackow, M., et al. (2017) · Genes & Development · doi:10.1101/gad.303677.117 · Cited by 19 · see citing works

Expression of MAGE-A11 in breast cancer tissues and its effects on the proliferation of breast cancer cells

Xia, L., Xu, M., Chen, Y., et al. (2012) · Molecular Medicine Reports · doi:10.3892/mmr.2012.1126 · Cited by 17 · see citing works

PROTAC targeted protein degraders: the past is prologue

Békés, M., Langley, D. R., & Crews, C. M. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-021-00371-6 · Cited by 3,395 · see citing works

The poxvirus encoded ubiquitin ligase, p28, is regulated by proteasomal degradation and autoubiquitination

Mottet, K., Bareiss, B., Milne, C. D., et al. (2014) · Virology · doi:10.1016/j.virol.2014.08.028 · Cited by 10 · see citing works

Ubiquitination and Degradation of Mutant p53

Lukashchuk, N., & Vousden, K. H. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00050-07 · Cited by 223 · see citing works

Promiscuous Interactions of gp78 E3 Ligase CUE Domain with Polyubiquitin Chains

Liu, S., Chen, Y., Li, J., Huang, T., Tarasov, S. G., King, A., Weissman, A. M., Byrd, R. A., & Das, R. (2012) · Structure · doi:10.1016/j.str.2012.09.020 · Cited by 31 · see citing works

Multiple E3 ligases act as antiviral factors against SARS-CoV-2 via inducing the ubiquitination and degradation of ORF9b

Yu, M., Li, J., Gao, W., et al. (2024) · Journal of Virology · doi:10.1128/jvi.01624-23 · Cited by 21 · see citing works

The Antibiotic Treatment Index: A Novel Tool to Improve Antibiotic Resistance Monitoring

Manomayitthikan, T., Kessomboon, N., & Borlace, G. N. (2014) · Research in Social and Administrative Pharmacy · doi:10.1016/j.sapharm.2014.07.138