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by McRae, Jeremy F and Clayton, Stephen and Fitzgerald, Tomas W and Kaplanis, Joanna and Prigmore, Elena and Rajan, Diana and Sifrim, Alejandro and Aitken, Stuart and Akawi, Nadia and Alvi, Mohsan and Ambridge, Kirsty and Barrett, Daniel M and Bayzetinova, Tanya and Jones, Philip and Jones, Wendy D and King, Daniel and Krishnappa, Netravathi and Mason, Laura E and Singh, Tarjinder and Tivey, Adrian R and Ahmed, Munaza and Anjum, Uruj and Archer, Hayley and Armstrong, Ruth and Awada, Jana and Balasubramanian, Meena and Banka, Siddharth and Baralle, Diana and Barnicoat, Angela and Batstone, Paul and Baty, David and Bennett, Chris and Berg, Jonathan and Bernhard, Birgitta and Bevan, A. Paul and Bitner-Glindzicz, Maria and Blair, Edward and Blyth, Moira and Bohanna, David and Bourdon, Louise and Bourn, David and Bradley, Lisa and Brady, Angela and Brent, Simon and Brewer, Carole and Brunstrom, Kate and Bunyan, David J and Burn, John and Canham, Natalie and Castle, Bruce and Chandler, Kate and Chatzimichali, Elena and Cilliers, Deirdre and Clarke, Angus and Clasper, Susan and Clayton-Smith, Jill and Clowes, Virginia and Coates, Andrea and Cole, Trevor and Colgiu, Irina and Collins, Amanda and Collinson, Morag N and Connell, Fiona and Cooper, Nicola and Cox, Helen and Cresswell, Lara and Cross, Gareth and Crow, Yanick and D'Alessandro, Mariella and Dabir, Tabib and Davidson, Rosemarie and Davies, Sally and De Vries, Dylan and Dean, John and Deshpande, Charu and Devlin, Gemma and Dixit, Abhijit and Dobbie, Angus and Donaldson, Alan and Donnai, Dian and Donnelly, Deirdre and Donnelly, Carina and Douglas, Angela and Douzgou, Sofia and Duncan, Alexis and Eason, Jacqueline and Ellard, Sian and Ellis, Ian and Elmslie, Frances and Evans, Karenza and Everest, Sarah and Fendick, Tina and Fisher, Richard and Flinter, Frances and Foulds, Nicola and Fry, Andrew and Fryer, Alan and Gardiner, Carol and Gaunt, Lorraine and Ghali, Neeti and ... and Deciphering Developmental Disorders Study
Nature (London), ISSN 1476-4687, 01/2017, Volume 542, Issue 7642, pp. 433 - 438
The genomes of individuals with severe, undiagnosed developmental disorders are enriched in damaging de novo mutations (DNMs) in developmentally important... 
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Prevalence | Humans | Middle Aged | Parents | Male | Mi-2 Nucleosome Remodeling and Deacetylase Complex - genetics | Developmental Disabilities - genetics | Casein Kinase II - genetics | Autoantigens - genetics | Young Adult | ras GTPase-Activating Proteins - genetics | Adult | Female | Child | CDC2 Protein Kinase - genetics | Histone-Lysine N-Methyltransferase - genetics | Repressor Proteins - genetics | Sex Characteristics | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Mutation - genetics | Nerve Tissue Proteins - genetics | Sequence Analysis, DNA | Homeodomain Proteins - genetics | DEAD-box RNA Helicases - genetics | Exome - genetics | Phenotype | Myeloid-Lymphoid Leukemia Protein - genetics | Adolescent | Heredity - genetics | Protein Phosphatase 2C - genetics | Cohort Studies | Child development deviations | Genetic aspects | Genetic disorders | Developmental disabilities | Distribution | Genes | Families & family life | Births | Genomes | Mutation | Causality | Estimates | Age | Index Medicus | TRIO | MYT1L | EHMT1 | HNRNPU | SUV420H1 | COL4A3BP | SYNGAP1 | PPP2R1A | POGZ | EP300 | KCNH1 | SCN1A | MEF2C | CDKL5 | CSNK2A1 | DYRK1A | CASK | ALG13 | FOXP1 | KAT6B | TBL1XR1 | KAT6A | SCN8A | KCNQ2 | EEF1A2 | KCNQ3 | ADNP | PhenIcons | SET | KMT2A | ANKRD11 | STXBP1 | FOXG1 | ZC4H2 | ITPR1 | De novo mutation | Seizures | ZBTB18 | CREBBP | SMAD4 | PDHA1 | IQSEC2 | AUTS2 | BCL11A | BRAF | SMARCA2 | GRIN2B | MED13L | GNAO1 | CNOT3 | TCF4 | SCN2A | CDK13 | GABRB3 | SETD5 | KDM5B | Developmental Disease | DDX3X | CHD8 | PTEN | CHD4 | TCF20 | CTCF | CHD2 | WDR45 | SLC6A1 | MECP2 | CHAMP1 | KIF1A | Average Faces | MSL3 | PPP2R5D | SMC1A | ARID1B | DNM1 | CNKSR2 | PACS1 | WAC | ZMYND11 | AHDC1 | NFIX | SATB2 | HDAC8 | PPM1D | GNAI1 | PURA | PUF60 | NSD1 | Intellectual Disability | SLC35A2 | DYNC1H1 | NAA10 | USP9X | PTPN11 | GATAD2B | ASXL1 | KANSL1 | ASXL3 | CTNNB1 | QRICH1
Journal Article
Journal Article
PloS one, ISSN 1932-6203, 09/2011, Volume 6, Issue 9, pp. e25021 - e25021
Background: Hub proteins are connected through binding interactions to many other proteins... 
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Cell Proliferation | Luciferases - metabolism | Oligonucleotide Array Sequence Analysis | Humans | Gene Expression Profiling | Smad3 Protein - metabolism | Immunoenzyme Techniques | DNA-Binding Proteins - metabolism | Smad3 Protein - genetics | Kidney - metabolism | Myoblasts - metabolism | Smad4 Protein - genetics | Smad2 Protein - genetics | Myoblasts - cytology | Protein Interaction Domains and Motifs | Real-Time Polymerase Chain Reaction | Biomarkers - metabolism | Proto-Oncogene Proteins - metabolism | Signal Transduction | RNA, Messenger - genetics | Trans-Activators | Cells, Cultured | Gene Expression Regulation | Smad2 Protein - metabolism | Ubiquitin-Protein Ligases - metabolism | Models, Molecular | Proto-Oncogene Proteins - genetics | Kidney - cytology | DNA-Binding Proteins - genetics | Mutation - genetics | Reverse Transcriptase Polymerase Chain Reaction | Nerve Tissue Proteins - genetics | Smad4 Protein - metabolism | Blotting, Western | Nerve Tissue Proteins - metabolism | Carrier Proteins - genetics | Animals | Carrier Proteins - metabolism | Transforming Growth Factor beta - genetics | Protein Conformation | Smad3 Protein - chemistry | Mice | Ubiquitin-Protein Ligases - genetics | Transforming Growth Factor beta - metabolism | Amino acids | Bone morphogenetic proteins | Cellular signal transduction | Genetic aspects | Binding proteins | Transforming growth factors | Gene expression | Protein-protein interactions | Protein binding | Transcription factors | Laboratories | Genes | Transforming growth factor-b | Oncology | Smad3 protein | Kinases | Smad4 protein | Proteins | Signal transduction | Cell growth | Reporter gene | Cooperation | Spots | Interleukin 1 | Stress response | Growth factors | Public health | Binding | Medical research | Interleukin 11 | Lymphoma | Gelatinase B | Mutants | Medicine | Signaling | Mutagenesis | Mutation | Protein interaction | Binding sites | Cancer | Apoptosis | Index Medicus | Lymphomas | Transduction
Journal Article
PloS one, ISSN 1932-6203, 03/2015, Volume 10, Issue 3, pp. e0120045 - e0120045
Cervical cancer is the major cause of cancer related deaths in women, especially in developing countries and Human Papilloma Virus infection in conjunction... 
Science & Technology - Other Topics | Multidisciplinary Sciences | Science & Technology | Receptors, Transforming Growth Factor beta - genetics | Humans | Collagen - chemistry | Epithelial-Mesenchymal Transition - drug effects | Wnt Proteins - metabolism | Smad4 Protein - genetics | Cyclin-Dependent Kinase Inhibitor p21 - metabolism | Peptidylprolyl Isomerase - metabolism | Peptidylprolyl Isomerase - genetics | Protein-Serine-Threonine Kinases - metabolism | Emodin - pharmacology | Curcumin - pharmacology | Cyclin-Dependent Kinase Inhibitor p21 - antagonists & inhibitors | Smad3 Protein - antagonists & inhibitors | beta Catenin - metabolism | Drug Synergism | Cell Movement - drug effects | Receptors, Transforming Growth Factor beta - antagonists & inhibitors | Cyclin D1 - genetics | Signal Transduction - drug effects | Cell Line, Tumor | Laminin - chemistry | HeLa Cells | Cyclin D1 - metabolism | Smad4 Protein - antagonists & inhibitors | Gene Expression Regulation, Neoplastic | Smad3 Protein - metabolism | Proteoglycans - chemistry | Smad3 Protein - genetics | Cyclin D1 - antagonists & inhibitors | Cyclin-Dependent Kinase Inhibitor p21 - genetics | Wnt Proteins - genetics | Protein-Serine-Threonine Kinases - antagonists & inhibitors | Transforming Growth Factor beta - antagonists & inhibitors | Female | Snail Family Transcription Factors | Protein-Serine-Threonine Kinases - genetics | Transcription Factors - antagonists & inhibitors | NIMA-Interacting Peptidylprolyl Isomerase | Transcription Factors - genetics | Smad4 Protein - metabolism | beta Catenin - genetics | Transcription Factors - metabolism | Transforming Growth Factor beta - genetics | Receptors, Transforming Growth Factor beta - metabolism | beta Catenin - antagonists & inhibitors | Cell Proliferation - drug effects | Antineoplastic Agents, Phytogenic - pharmacology | Transforming Growth Factor beta - metabolism | Drug Combinations | Biotechnology | Deregulation | Wnt protein | Mesenchyme | Downstream effects | Crosstalk | Viruses | Smad3 protein | Biochemistry | Metastasis | Kinases | Pin1 protein | Cancer therapies | Carcinogenesis | Smad4 protein | Developing countries--LDCs | Cell adhesion & migration | Proteins | β-catenin | Signal transduction | Carcinogens | Pathways | Cell cycle | Curcumin | Tumorigenesis | Inhibition | Downstream | Medical research | Breast cancer | Tumor cell lines | Gene expression | Cervix | Emodin | Signaling | Chemotherapy | Phytochemicals | Ligands | Cell migration | Cervical cancer | Cancer | Apoptosis | Index Medicus | Developing countries | LDCs
Journal Article
EMBO reports, ISSN 1469-3178, 12/2017, Volume 19, Issue 1, pp. 135 - 155
During epithelial–mesenchymal transition (EMT), reprogramming of gene expression is accompanied by histone modifications. Whether EMT‐promoting signaling... 
histone methylation | cancer drug resistance | epithelial stem cells | cancer cell dissemination | TGF‐β signaling | TGF-β signaling | Biochemistry & Molecular Biology | Life Sciences & Biomedicine | Science & Technology | Cell Biology | Epithelial Cells - metabolism | Carcinoma, Ductal - genetics | Carcinoma, Ductal - pathology | Epithelial Cells - drug effects | Humans | Protein Methyltransferases - genetics | Gene Expression Regulation, Neoplastic | Spheroids, Cellular - pathology | Smad3 Protein - metabolism | Epithelial-Mesenchymal Transition - genetics | Mammary Glands, Human - metabolism | Protein Methyltransferases - metabolism | Breast Neoplasms - metabolism | Smad3 Protein - genetics | Matrix Metalloproteinase 9 - metabolism | Snail Family Transcription Factors - genetics | Smad4 Protein - genetics | Matrix Metalloproteinase 9 - genetics | Female | Carcinoma, Ductal - metabolism | Spheroids, Cellular - drug effects | Acetylation | Snail Family Transcription Factors - metabolism | Signal Transduction | Mammary Glands, Animal - pathology | Matrix Metalloproteinase 2 - metabolism | Spheroids, Cellular - metabolism | Epithelial Cells - pathology | Mammary Glands, Human - pathology | Smad4 Protein - metabolism | Matrix Metalloproteinase 2 - genetics | Transforming Growth Factor beta - pharmacology | Animals | Breast Neoplasms - genetics | Histones - genetics | Mammary Glands, Animal - metabolism | Breast Neoplasms - pathology | Cell Line, Tumor | Mice | Protein Processing, Post-Translational | Histones - metabolism | Methylation | Drugs | Smad protein | Chromatin | Mesenchyme | Methyltransferase | Event-related potentials | Breast cancer | Smad3 protein | Gene expression | Metastases | Recruitment | Gene silencing | Signaling | Lysine | Stem cells | DNA methylation | Inhibition | Snail protein | Cancer | Index Medicus | Chromatin, Epigenetics, Genomics & Functional Genomics
Journal Article