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Nature (London), ISSN 1476-4687, 2015, Volume 526, Issue 7572, pp. 263 - 267
.... In late-stage colorectal cancer, the most commonly used targeted therapies are the monoclonal antibodies cetuximab and panitumumab, which prevent epidermal growth factor receptor (EGFR) activation(1... 
PANITUMUMAB | THERAPY | MULTIDISCIPLINARY SCIENCES | SEQUENCE | ACQUIRED-RESISTANCE | SOMATIC MUTATION | IDENTIFICATION | GENE COPY NUMBER | ACTIVATING MUTATIONS | BREAST | INSIGHTS | Receptor, Epidermal Growth Factor - genetics | Receptor, ErbB-2 - genetics | Proto-Oncogene Proteins p21(ras) - genetics | Colorectal Neoplasms - genetics | Genomics | Humans | Antibodies, Monoclonal - therapeutic use | Antineoplastic Agents - therapeutic use | Cetuximab - therapeutic use | Molecular Targeted Therapy | Receptor, Fibroblast Growth Factor, Type 1 - genetics | MAP Kinase Kinase 1 - genetics | Colorectal Neoplasms - drug therapy | Female | Antineoplastic Agents - pharmacology | Insulin Receptor Substrate Proteins - genetics | Colorectal Neoplasms - metabolism | Antibodies, Monoclonal - pharmacology | Cetuximab - pharmacology | DNA Copy Number Variations - genetics | Mutation - genetics | Genome, Human - genetics | Receptor, Epidermal Growth Factor - chemistry | Xenograft Model Antitumor Assays | Drug Resistance, Neoplasm - genetics | Exome - genetics | Animals | Receptor, Platelet-Derived Growth Factor alpha - genetics | Receptor, Epidermal Growth Factor - antagonists & inhibitors | Mice | Drug Resistance, Neoplasm - drug effects | Care and treatment | Gene mutations | Colorectal cancer | Drug metabolism | Genetic aspects | Identification and classification | Health aspects | Proteins | Epidermal growth factor | Genes | Clinical trials | Mutation | Kinases | Cancer therapies | Tumors
Journal Article
by Kilpeläinen, Tuomas and Zillikens, Carola and Stancáková, Alena and Finucane, Francis and Ried, Janina and Langenberg, Claudia and Zhang, Weihua and Beckmann, Jacques and Luan, J and Vandenput, Liesbeth and Styrkarsdottir, Unnur and Zhou, Yanhua and Smith, Albert Vernon and Zhao, Jing Hua and Amin, Najaf and Vedantam, Sailaja and Shin, S.-Y and Haritunians, Talin and Fu, Mao and Feitosa, Mary Furlan and Kumari, Meena and Halldorsson, Bjarni and Tikkanen, Emmi and Mangino, Massimo and Hayward, Caroline and Song, Ci and Arnold, Alice and Oostra, Ben and Campbell, Harry and Cupples, Aienne and Davis, Kathryn and Döring, Angela and Eiriksdottir, Gudny and Estrada Gil, Karol and Fernández-Real, J.M and Garcia, Melissa and Gieger, Christian and Glazer, Nicole and Guiducci, Candace and Hofman, Albert and Humphries, Steve and Isomaa, Bo and Jacobs, Leonie and Jula, Antti and Karasik, David and Karlsson, Magnus and Khaw, Kay-Tee and Kim, Lauren and Kivimaki, Mika and Klopp, Norman and Kuhnel, Brigitte and Kuusisto, Johanna and Liu, YongMei and Ljunggren, Ö and Lorentzon, Mattias and Luben, Robert and McKnight, Barbara and Mellström, Dan and Mitchell, Braxton and Mooser, Vincent and Moreno, J.M and Männistö, Satu and O'Connell, Jeffery and Pascoe, Laura and Peltonen, Leena Johanna and Peral, Belén and Perola, Markus and Psaty, Bruce and Salomaa, Veikko and Savage, David and Semple, Robert and Skaric-Juric, Tatjana and Sigurdsson, Gunnar and Spector, Timothy and Syvänen, A.-C and Talmud, Philippa and Thorleifsson, Gudmar and Thorsteinsdottir, Unnur and Uitterlinden, Ané and Tikka-Kleemola, Päivi and Vidal-Puig, Antonio and Wild, Sarah and Wright, Alan and Clegg, Deborah and Schadt, Eric and Wilson, James and Rudan, Igor and Ripatti, Samuli and Borecki, Ingrid and Shuldiner, Alan and Ingelsson, Erik and Jansson, J.O and Kaplan, Robert and Gudnason, Vilmundur and Harris, Tamara and Groop, Leif and Kiel, Douglas and Rivadeneira Ramirez, Fernando and Walker, Mark and Barroso, Inês and ... and Göteborgs universitet and Institutionen för medicin, avdelningen för invärtesmedicin and Gothenburg University and Institute of Neuroscience and Physiology, Department of Physiology and Sahlgrenska Academy and Centre for Bone and Arthritis Research and Sahlgrenska akademin and Institutionen för neurovetenskap och fysiologi, sektionen för fysiologi and Institute of Medicine, Department of Internal Medicine
Nature genetics, ISSN 1061-4036, 08/2011, Volume 43, Issue 8, pp. 753 - 760
Journal Article
Molecular cell, ISSN 1097-2765, 2008, Volume 30, Issue 4, pp. 403 - 414
Journal Article
The Journal of biological chemistry, ISSN 1083-351X, 2014, Volume 289, Issue 16, pp. 11230 - 11241
Journal Article
The Journal of biological chemistry, ISSN 1083-351X, 2010, Volume 285, Issue 8, pp. 5204 - 5211
Journal Article
Nature cell biology, ISSN 1476-4679, 2004, Volume 6, Issue 4, pp. 351 - 357
Journal Article
Nature Cell Biology, ISSN 1465-7392, 06/2005, Volume 7, Issue 6, pp. 601 - 611
.... Insulin receptor substrate proteins regulate a necdin-E2F4 interaction... 
MATRIX METALLOPROTEINASES | ACTIVATION | INHIBITION | PROTEIN | INTERACTS | RESISTANCE | ADIPOCYTE DIFFERENTIATION | ADIPOGENESIS | PRADER-WILLI-SYNDROME | ADIPOSE-TISSUE | CELL BIOLOGY | Oligonucleotide Array Sequence Analysis | Gene Expression Regulation, Developmental - genetics | Adipocytes - cytology | Gene Expression Profiling | Stem Cells - cytology | Wnt Proteins | PPAR gamma - metabolism | Stem Cells - metabolism | DNA-Binding Proteins - metabolism | Cell Differentiation - genetics | Intercellular Signaling Peptides and Proteins - metabolism | E2F4 Transcription Factor | Membrane Proteins - metabolism | Nuclear Proteins - genetics | Repressor Proteins - metabolism | PPAR gamma - genetics | Membrane Proteins - genetics | Cells, Cultured | Intercellular Signaling Peptides and Proteins - genetics | Repressor Proteins - genetics | Nuclear Proteins - metabolism | Signal Transduction - genetics | Transcription Factors - genetics | DNA-Binding Proteins - genetics | Nerve Tissue Proteins - genetics | Mice, Knockout | Nerve Tissue Proteins - metabolism | Transcription Factors - metabolism | Cyclic AMP Response Element-Binding Protein - genetics | Adipose Tissue, Brown - cytology | Animals | Adipocytes - metabolism | Cyclic AMP Response Element-Binding Protein - metabolism | Adipose Tissue, Brown - growth & development | Receptor, Insulin - metabolism | Adipose Tissue, Brown - metabolism | Mice | Physiological aspects | Receptors | Research | Cell differentiation | Gene expression | Insulin
Journal Article
Journal Article
Biochemical Journal, ISSN 0264-6021, 02/2007, Volume 402, Issue 1, pp. 1 - 15
It is now well established that the members of the PTP (protein tyrosine phosphatase... 
Substrate identification | Tyrosine phosphorylation | Protein tyrosine phosphatase (PTP) | Substrate-trapping | KINASE-ACTIVITY | BIOCHEMISTRY & MOLECULAR BIOLOGY | FACTOR RECEPTOR | NEGATIVE REGULATOR | SIGNAL-TRANSDUCTION | INSULIN-RECEPTOR | protein tyrosine phosphatase (PTP) | EPIDERMAL-GROWTH-FACTOR | IN-VIVO | HELICOBACTER-PYLORI CAGA | substrate-trapping | tyrosine phosphorylation | PTP-PEST | substrate identification | T-CELLS | Protein Structure, Tertiary | Phosphorylation | Protein Tyrosine Phosphatase, Non-Receptor Type 11 | Humans | Substrate Specificity | Protein Tyrosine Phosphatases - metabolism | Intracellular Signaling Peptides and Proteins - metabolism | Protein Tyrosine Phosphatases - genetics | Tyrosine - metabolism | Animals | Models, Biological | Protein Tyrosine Phosphatase, Non-Receptor Type 1 | Binding Sites | serine | SH, Src homology | CSK, C-terminal Src kinase | RNAi, RNA interference | PTK, protein tyrosine kinase | MKP, MAPK phosphatase | IRS, IR substrate | CSF-1, colony-stimulating factor 1 | SHP, SH2-domain-containing protein tyrosine phosphatase | ERK, extracellular-signal-regulated kinase | PIR-B, paired immunoglobulin-like receptor B | ZAP-70, ζ-chain-associated protein kinase of 70 kDa | KIM, kinase-interacting motif | FAK, focal adhesion kinase | EGFR, epidermal growth factor receptor | STEP, striatal-enriched PTP | LYP, lymphoid phosphatase | MAPK, mitogen-activated protein kinase | PTP, protein tyrosine phosphatase | SNARE, NSF-attachment protein receptor | TCR, T-cell receptor | PI3K, phosphoinositide 3-kinase | Gab1, Grb2-associated binder-1 | PAG, phosphoprotein associated with glycosphingolipid-enriched membrane microdomains | Cbp, C-terminal Src kinase-binding protein | SNP, single-nucleotide polymorphism | Review | WASP, Wiskott–Aldrich syndrome protein | NSF, N-ethylmaleimide-sensitive factor | PDGFR, platelet-derived growth factor receptor | AP-1, activator protein 1 | PEP, PEST (Pro-Glu-Ser-Thr) domain phosphatase | SFK, Src family kinase | DSP, dual-specificity phosphatase | PSTPIP, proline | NS, Noonan syndrome | IR, insulin receptor | IFN, interferon | STAT, signal transducer and activator of transcription | NFAT, nuclear factor of activated T-cells | IGF-1, insulin-like growth factor 1 | BIT, brain immunoglobulin-like molecule with tyrosine-based activation motifs | threonine-phosphatase-interacting protein | TCPTP, T-cell PTP | JAK, Janus kinase | MEF, mouse embryonic fibroblast | BCR, B-cell receptor | GAP, GTPase-activating protein | HGF, hepatocyte growth factor
Journal Article