An atlas of posttranslational modifications on RNA binding proteins
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[1] Christopher J. Oldfield,et al. Intrinsic Disorder in Human RNA-binding Proteins. , 2021, Journal of molecular biology.
[2] A. Lundby,et al. Proteome-wide profiling and mapping of post translational modifications in human hearts , 2021, Scientific Reports.
[3] Kara Dolinski,et al. The BioGRID database: A comprehensive biomedical resource of curated protein, genetic, and chemical interactions , 2020, Protein science : a publication of the Protein Society.
[4] Peifeng Li,et al. The biological function and clinical significance of SF3B1 mutations in cancer , 2020, Biomarker Research.
[5] Antja-Voy Hartley,et al. Modulating the modulators: regulation of protein arginine methyltransferases by post-translational modifications. , 2020, Drug discovery today.
[6] V. Kim,et al. Chemical RNA digestion enables robust RNA-binding site mapping at single amino acid resolution , 2020, Nature Structural & Molecular Biology.
[7] Gene W. Yeo,et al. How RNA-Binding Proteins Interact with RNA: Molecules and Mechanisms. , 2020, Molecular cell.
[8] Norman E. Davey,et al. ELM—the eukaryotic linear motif resource in 2020 , 2019, Nucleic Acids Res..
[9] Gene W. Yeo,et al. Principles of RNA processing from analysis of enhanced CLIP maps for 150 RNA binding proteins , 2019, Genome Biology.
[10] M. Esteller,et al. Disruption of Long Noncoding RNAs Targets Cancer Hallmark Pathways in Lung Tumorigenesis. , 2019, Cancer research.
[11] Tom Liu,et al. KRAS G12V Mutation in Acquired Resistance to Combined BRAF and MEK Inhibition in Papillary Thyroid Cancer. , 2019, Journal of the National Comprehensive Cancer Network : JNCCN.
[12] A. Millar,et al. The Scope, Functions, and Dynamics of Posttranslational Protein Modifications. , 2019, Annual review of plant biology.
[13] Jeroen Krijgsveld,et al. The Human RNA-Binding Proteome and Its Dynamics during Translational Arrest , 2019, Cell.
[14] B. Baradaran,et al. The role of DEAD‐box RNA helicase p68 (DDX5) in the development and treatment of breast cancer , 2018, Journal of cellular physiology.
[15] S. Aoki,et al. The intellectual disability gene PQBP1 rescues Alzheimer’s disease pathology , 2018, Molecular Psychiatry.
[16] John S. Mattick,et al. The State of Long Non-Coding RNA Biology , 2018, Non-coding RNA.
[17] A. Bairoch,et al. Kinases and Cancer , 2018, Cancers.
[18] Karl W Barber,et al. The ABCs of PTMs. , 2018, Nature chemical biology.
[19] Jernej Ule,et al. Advances in CLIP Technologies for Studies of Protein-RNA Interactions. , 2018, Molecular cell.
[20] Matthias W. Hentze,et al. A brave new world of RNA-binding proteins , 2018, Nature Reviews Molecular Cell Biology.
[21] M. Perkins,et al. Chemical methods for mapping cysteine oxidation. , 2018, Chemical Society reviews.
[22] P. S. Ray,et al. The GAIT translational control system , 2017, Wiley interdisciplinary reviews. RNA.
[23] E. Dassi. Handshakes and Fights: The Regulatory Interplay of RNA-Binding Proteins , 2017, Front. Mol. Biosci..
[24] B. Garcia,et al. Phosphoproteomics reveals that glycogen synthase kinase-3 phosphorylates multiple splicing factors and is associated with alternative splicing , 2017, The Journal of Biological Chemistry.
[25] Gene W. Yeo,et al. A Large-Scale Binding and Functional Map of Human RNA Binding Proteins , 2017, bioRxiv.
[26] Claire D. McWhite,et al. Integration of over 9,000 mass spectrometry experiments builds a global map of human protein complexes , 2017, Molecular systems biology.
[27] Damian Szklarczyk,et al. The STRING database in 2017: quality-controlled protein–protein association networks, made broadly accessible , 2016, Nucleic Acids Res..
[28] Michelle C. Chen,et al. Physiologic Expression of Sf3b1(K700E) Causes Impaired Erythropoiesis, Aberrant Splicing, and Sensitivity to Therapeutic Spliceosome Modulation. , 2016, Cancer cell.
[29] Jeroen Krijgsveld,et al. Comprehensive Identification of RNA-Binding Domains in Human Cells , 2016, Molecular cell.
[30] Ralf Schmidt,et al. A comprehensive analysis of 3′ end sequencing data sets reveals novel polyadenylation signals and the repressive role of heterogeneous ribonucleoprotein C on cleavage and polyadenylation , 2015, bioRxiv.
[31] V. Timmerman,et al. The hnRNP family: insights into their role in health and disease , 2016, Human Genetics.
[32] Howard Y. Chang,et al. Long Noncoding RNAs in Cancer Pathways. , 2016, Cancer cell.
[33] Jeroen Krijgsveld,et al. Comprehensive Identification of RNA-Binding Proteins by RNA Interactome Capture. , 2016, Methods in molecular biology.
[34] A. Albakr,et al. The role of RNA metabolism in neurological diseases , 2015, Balkan journal of medical genetics : BJMG.
[35] L. Abrami,et al. SwissPalm: Protein Palmitoylation database , 2015, F1000Research.
[36] R. Thapar. Structural Basis for Regulation of RNA-Binding Proteins by Phosphorylation , 2014, ACS chemical biology.
[37] Yu-Ju Chen,et al. dbSNO 2.0: a resource for exploring structural environment, functional and disease association and regulatory network of protein S-nitrosylation , 2014, Nucleic Acids Res..
[38] S. Gerstberger,et al. A census of human RNA-binding proteins , 2014, Nature Reviews Genetics.
[39] A. Quinlan. BEDTools: The Swiss‐Army Tool for Genome Feature Analysis , 2014, Current protocols in bioinformatics.
[40] Oliver Kohlbacher,et al. Photo-cross-linking and high-resolution mass spectrometry for assignment of RNA-binding sites in RNA-binding proteins , 2014, Nature Methods.
[41] Liu Cao,et al. P68 RNA helicase as a molecular target for cancer therapy , 2014, Journal of experimental & clinical cancer research : CR.
[42] Predrag Radivojac,et al. The structural and functional signatures of proteins that undergo multiple events of post‐translational modification , 2014, Protein science : a publication of the Protein Society.
[43] K. Morris,et al. The rise of regulatory RNA , 2014, Nature Reviews Genetics.
[44] Pierrick Craveur,et al. PTM-SD: a database of structurally resolved and annotated posttranslational modifications in proteins , 2014, Database J. Biol. Databases Curation.
[45] Man Kit Cheung,et al. Human proteins with target sites of multiple post-translational modification types are more prone to be involved in disease. , 2014, Journal of proteome research.
[46] Yu-Chieh Wang,et al. Protein post-translational modifications and regulation of pluripotency in human stem cells , 2013, Cell Research.
[47] Shane T. Jensen,et al. Quantitative phosphoproteomics reveals extensive cellular reprogramming during HIV-1 entry. , 2013, Cell host & microbe.
[48] Wei Ge,et al. RedoxDB - a curated database for experimentally verified protein oxidative modification , 2012, Bioinform..
[49] W. Lim,et al. Systematic Functional Prioritization of Protein Posttranslational Modifications , 2012, Cell.
[50] Norman E. Davey,et al. Insights into RNA Biology from an Atlas of Mammalian mRNA-Binding Proteins , 2012, Cell.
[51] Bin Zhang,et al. PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse , 2011, Nucleic Acids Res..
[52] Livia Perfetto,et al. MINT, the molecular interaction database: 2012 update , 2011, Nucleic Acids Res..
[53] Howard Y. Chang,et al. Molecular mechanisms of long noncoding RNAs. , 2011, Molecular cell.
[54] S. Elledge,et al. The Prp19 complex and the Usp4Sart3 deubiquitinating enzyme control reversible ubiquitination at the spliceosome. , 2010, Genes & development.
[55] Hans-Werner Mewes,et al. CORUM: the comprehensive resource of mammalian protein complexes , 2007, Nucleic Acids Res..
[56] D.G. Knorre,et al. Chemical and Functional Aspects of Posttranslational Modification of Proteins , 2009, Acta naturae.
[57] R. Mukhopadhyay,et al. The GAIT system: a gatekeeper of inflammatory gene expression. , 2009, Trends in biochemical sciences.
[58] Yixue Li,et al. SysPTM: A Systematic Resource for Proteomic Research on Post-translational Modifications* , 2009, Molecular & Cellular Proteomics.
[59] Sandhya Rani,et al. Human Protein Reference Database—2009 update , 2008, Nucleic Acids Res..
[60] R. Wenham,et al. The molecular biology of endometrial cancers and the implications for pathogenesis, classification, and targeted therapies. , 2009, Cancer control : journal of the Moffitt Cancer Center.
[61] E. Sontheimer,et al. A role for ubiquitin in the spliceosome assembly pathway , 2008, Nature Structural &Molecular Biology.
[62] M. Mann,et al. PHOSIDA (phosphorylation site database): management, structural and evolutionary investigation, and prediction of phosphosites , 2007, Genome Biology.
[63] Michel Schneider,et al. UniProtKB/Swiss-Prot. , 2007, Methods in molecular biology.
[64] Alejandro Garcia,et al. UbiProt: a database of ubiquitylated proteins , 2007, BMC Bioinformatics.
[65] Yu Xue,et al. MeMo: a web tool for prediction of protein methylation modifications , 2006, Nucleic Acids Res..
[66] Jernej Ule,et al. CLIP: a method for identifying protein-RNA interaction sites in living cells. , 2005, Methods.
[67] G. Gill,et al. SUMO and ubiquitin in the nucleus: different functions, similar mechanisms? , 2004, Genes & development.
[68] Nikolaj Blom,et al. Phospho.ELM: A database of experimentally verified phosphorylation sites in eukaryotic proteins , 2004, BMC Bioinformatics.
[69] S. Dehm,et al. SRC gene expression in human cancer: the role of transcriptional activation. , 2004, Biochemistry and cell biology = Biochimie et biologie cellulaire.
[70] Adam J. Smith,et al. The Database of Interacting Proteins: 2004 update , 2004, Nucleic Acids Res..
[71] Martin Vingron,et al. IntAct: an open source molecular interaction database , 2004, Nucleic Acids Res..
[72] T. Yeatman,et al. Role of Src expression and activation in human cancer , 2000, Oncogene.
[73] P. Silver,et al. Arginine methylation facilitates the nuclear export of hnRNP proteins. , 1998, Genes & development.
[74] Ole Lund,et al. O-GLYCBASE: a revised database of O-glycosylated proteins , 1996, Nucleic Acids Res..
[75] G. Dreyfuss,et al. In vivo and in vitro arginine methylation of RNA-binding proteins , 1995, Molecular and cellular biology.