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Cellular Signalling, ISSN 0898-6568, 2006, Volume 18, Issue 9, pp. 1351 - 1359
Follicle-stimulating hormone (FSH) is necessary and sufficient to induce maturation of ovarian follicles to a mature, preovulatory phenotype in the intact... 
Protein kinase A | Mitogen-activated protein kinase | Follicle-stimulating hormone | Female reproduction | Hypoxia-induced factor 1 | Histone H3 | histone H3 | SIDE-CHAIN CLEAVAGE | follicle-stimulating hormone | OVARIAN-FOLLICLE | ELEMENT-BINDING PROTEIN | HISTONE H3 PHOSPHORYLATION | hypoxia-induced factor 1 | STEROIDOGENIC FACTOR-I | TRANSCRIPTION FACTOR FKHR | female reproduction | P38 MAP KINASE | LUTEINIZING-HORMONE | CELL BIOLOGY | mitogen-activated protein kinase | FOLLICLE-STIMULATING-HORMONE | protein kinase A | GROWTH-FACTOR-I | Cyclic AMP-Dependent Protein Kinases - metabolism | Follicle Stimulating Hormone - metabolism | Tumor Suppressor Proteins - metabolism | Granulosa Cells - physiology | Gene Expression Regulation | Protein Tyrosine Phosphatases - metabolism | Phosphatidylinositol 3-Kinases - metabolism | Animals | Forkhead Transcription Factors - metabolism | Cyclic AMP Response Element-Binding Protein - metabolism | Female | Signal Transduction - physiology | p38 Mitogen-Activated Protein Kinases - metabolism | Enzyme Activation | Histones - metabolism | Tyrosine | Chromatin | Phosphatases | Corticosteroids | Peptides | Tuberous sclerosis | Glycoproteins | DNA binding proteins | Hormones | Gene expression | Phosphatidylinositol | Luteinizing hormone | Mitogens | Vascular endothelial growth factor | Protein kinases | Growth factors | Protein binding | GIOT-1, gonadotropin-inducible ovarian transcription factor-1 | p70S6K, p70 ribosomal S6 kinase | TGFβ, transforming growth factor β | EGF, epidermal growth factor | CREB, cAMP response element binding protein | PDE, phosphodiesterase | R, PKA regulatory subunits | GPCR, G-protein-coupled receptor | MAP2D, microtubule-associated protein 2D | Sp1 | Epac, exchange proteins activated by cAMP | PI3K, phosphatidylinositol 3-kinase | IGF, insulin-like growth factor | mTOR, mammalian target of rapamycin | AKAP, A kinase anchoring protein | Sp3, specific protein 1 | PKI, PKA inhibitor peptide | PKC, protein kinase C | SCC, P450 cholesterol side chain cleavage | VEGF, vascular endothelial growth factor | CBP, CREB binding protein | ERK, extracellular regulated kinase | MNK, MAPK-interacting kinase | Aromatase, P450 aromatase | ChIP, chromatin immunoprecipitation assay | HIF-1, hypoxia-induced factor-1 | Egr-1, early growth response protein-1 | LH, luteinizing hormone | MEK, mitogen- and extracellular-regulated kinase kinase | TSC, tuberous sclerosis complex tumor suppressor gene | SF-1, steroidogenic factor-1 | SGK, serum glucocorticoid kinase | RSK, p90 ribosomal S6 protein kinase | LRH-1, liver receptor homolog-1 | MAPK, mitogen-activated protein kinase | PKA, protein kinase A | PTP, protein tyrosine phosphatase | FSH, follicle-stimulating hormone | MK, MAPK-activated protein kinases
Journal Article
Nature, ISSN 0028-0836, 03/2011, Volume 471, Issue 7337, pp. 189 - 196
B-cell non-Hodgkin's lymphoma comprises biologically and clinically distinct diseases the pathogenesis of which is associated with genetic lesions affecting... 
CBP | RUBINSTEIN-TAYBI SYNDROME | HISTONE ACETYLTRANSFERASES | ACETYLATION | P300 | MULTIDISCIPLINARY SCIENCES | CREB-BINDING-PROTEIN | CYCLE ARREST | ACUTE MYELOID-LEUKEMIA | TRANSCRIPTIONAL COACTIVATOR | P53 | Histone Acetyltransferases - deficiency | Recurrence | Acetyltransferases - metabolism | Histone Acetyltransferases - chemistry | Humans | E1A-Associated p300 Protein - genetics | Gene Expression Regulation, Neoplastic | Histone Acetyltransferases - genetics | CREB-Binding Protein - chemistry | E1A-Associated p300 Protein - metabolism | Lymphoma, B-Cell - genetics | Acetyltransferases - genetics | Mutation, Missense - genetics | CREB-Binding Protein - genetics | DNA-Binding Proteins - metabolism | CREB-Binding Protein - metabolism | Lymphoma, Follicular - genetics | Acetyltransferases - deficiency | Base Sequence | Histone Acetyltransferases - metabolism | Lymphoma, B-Cell - enzymology | HEK293 Cells | Acetylation | CREB-Binding Protein - deficiency | Lymphoma, Large B-Cell, Diffuse - pathology | Lymphoma, Follicular - pathology | Cells, Cultured | E1A-Associated p300 Protein - chemistry | Lymphoma, Large B-Cell, Diffuse - enzymology | Tumor Suppressor Protein p53 - metabolism | Protein Structure, Tertiary - genetics | Mutation - genetics | Acetyl Coenzyme A - metabolism | Acetyltransferases - chemistry | Animals | Lymphoma, B-Cell - pathology | Polymorphism, Single Nucleotide - genetics | Protein Binding | Lymphoma, Follicular - enzymology | Mice | E1A-Associated p300 Protein - deficiency | Lymphoma, Large B-Cell, Diffuse - genetics | Proto-Oncogene Proteins c-bcl-6 | Sequence Deletion - genetics | Lymphomas | Genetic aspects | B cells | Gene mutations | Health aspects | Abnormalities | Proteins | Congenital diseases | Pathogenesis | Genes | Cell cycle | Genomes | Genetic engineering | Mutation | Binding sites
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) superfamily play critical roles in fundamental biological processes.... 
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
Journal of Biological Chemistry, ISSN 0021-9258, 03/2012, Volume 287, Issue 10, pp. 7026 - 7038
Journal Article
Protein Science, ISSN 0961-8368, 12/2016, Volume 25, Issue 12, pp. 2256 - 2267
Many viruses deregulate the cell and force transcription of viral genes by competing with cellular proteins for binding to the transcriptional co‐activators... 
NMR | intrinsically disordered protein | oncogenic viral protein | adenovirus | TRANSCRIPTIONAL ACTIVATION | COMPLEX | BIOCHEMISTRY & MOLECULAR BIOLOGY | CBP/P300 | CELL-CYCLE CONTROL | P53 TRANSACTIVATION DOMAIN | RETINOBLASTOMA PROTEIN | VIRAL ONCOPROTEIN | KIX DOMAIN | GENE-EXPRESSION | TUMOR-SUPPRESSOR | Adenovirus E1A Proteins - chemistry | E1A-Associated p300 Protein - chemistry | E1A-Associated p300 Protein - genetics | Tumor Suppressor Protein p53 - metabolism | CREB-Binding Protein - chemistry | E1A-Associated p300 Protein - metabolism | Tumor Suppressor Protein p53 - genetics | Amino Acid Motifs | CREB-Binding Protein - genetics | CREB-Binding Protein - metabolism | Adenovirus E1A Proteins - metabolism | Adenovirus E1A Proteins - genetics | Adenoviridae - genetics | Protein Domains | Tumor Suppressor Protein p53 - chemistry | Adenoviridae - metabolism | Adenoviridae - chemistry | Proteins | Genetic transcription | Adenoviruses | Protein binding | Binding sites | Cell cycle | Competition | Deregulation | Transcription factors | Complex formation | Nuclear magnetic resonance--NMR | Transcription | Peptides | p53 Protein | Retinoblastoma protein | Viruses | Homology | Event-related potentials | Early region | Cyclic AMP response element-binding protein | Peptide mapping | CREB-binding protein | Rodents | Serotypes | Retinoblastoma
Journal Article
FEBS Letters, ISSN 0014-5793, 2005, Volume 579, Issue 15, pp. 3346 - 3354
Intrinsically unstructured proteins (IUPs) are common in various proteomes and occupy a unique structural and functional niche in which function is directly... 
Protein disorder in vivo | Functional classification | Intrinsically disordered protein | Natively unfolded protein | Residual structure | PCS | intrinsically unstructured protein | NACP | calpastatin | Fourier-transformed infrared spectroscopy | circular dichroism | Cdk | non-A beta component of Alzheimer's disease amyloid plaque (also termed α-synuclein) | PP II | PEVK | CBP | CREB-binding protein | MoRE | CREB | molecular recognition element | MAP2 | FTIR | sodium dodecyl sulfate–polyacrylamide gel electrophoresis | Raman optical activity | primary contact site | cAMP response element binding protein | RNAP II | CST | IUP | ROA | DHPR | KID | kinase-inducible domain | polyproline II helix | SDS–PAGE | nuclear magnetic resonance | region rich in Pro, Glu, Val and Lys | NMR | DNA-dependent RNA polymerase II | dihydropyridine receptor | cyclin-dependent kinase | microtubule-associated protein 2 | RAMAN OPTICAL-ACTIVITY | TAU-PROTEIN | TRANSCRIPTIONAL ACTIVATION | intrinsically disordered protein | residual structure | TERMINAL DOMAIN | CYTOPLASMIC P21(CIP1/WAF1) | BIOCHEMISTRY & MOLECULAR BIOLOGY | DISORDERED PROTEINS | protein disorder in vivo | CELL BIOLOGY | NATIVELY UNFOLDED PROTEINS | CALPASTATIN SUBDOMAIN-A | BIOPHYSICS | natively unfolded protein | SIGMA-FACTOR | functional classification | SEQUENCE EVOLUTION | Animals | Proteins - metabolism | Protein Conformation | Proteins - classification | Structure-Activity Relationship | Proteins - chemistry | Protein Folding | Nuclear magnetic resonance | RNA | Binding proteins | Alzheimer's disease | RNA polymerases | Protein binding
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 9/2013, Volume 110, Issue 37, pp. 14942 - 14947
Journal Article