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0026559568
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Regulating Transcription Factor Activity by Phosphorylation
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(1992)
Trends Cell Biol
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Jackson1
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0026636883
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The Regulation of transcription by Phosphorylation
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(1992)
Cell
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Hunter1
Karin2
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3
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0024445798
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Cycle AMP Stimulates Somatostatin Gene Transcription by Phosphorylation of CREB at Serine 133
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(1989)
Cell
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Gonzalez1
Montminy2
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4
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0027433708
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Phosphorylated CREB Binds Specifically to the Nuclear Protein CBP
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of special interest, Identifies a protein, CBP, that binds to the CREB activation domain only after its phosphorylation on Ser133. CBP may be a mediator linking phospho-CREB to the transcriptional machinery.
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(1993)
Nature
, vol.365
, pp. 855-859
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Chrivia1
Kwok2
Lamb3
Hagiwara4
Montminy5
Goodman6
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9
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0025764217
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Mutation of Serum Response Factor Phosphorylation Sites and the Mechanism by Which its DNA-Binding Activity Is Increased by Casein Kinase II
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(1991)
Mol Cell Biol
, vol.11
, pp. 3652-3659
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Manak1
Prywes2
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11
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0026695645
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Phosphorylation of p62TCF by MAP Kinase Stimulates Ternary Complex Formation at cFos Promoter
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(1992)
Nature
, vol.358
, pp. 414-417
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Gille1
Sharrocks2
Shaw3
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12
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0027297647
-
The SRF Accessory Protein ELK-1 Contains a Growth Factor Regulated Transcription Domain
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of outstanding interest, More extensive analysis of the regulation of TCF activity by protein phosphorylation.
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(1993)
Cell
, vol.73
, pp. 381-393
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Marais1
Wynne2
Treisman3
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15
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0026480716
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Elk-1 Domains Responsible for Autonomous DNA Binding SRE: SRF Interaction and Negative Regulation of DNA Binding
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(1992)
Oncogene
, vol.7
, pp. 2335-2440
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Rao1
Reddy2
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17
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0027322153
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c-fos Transcriptional Activation and Repression Correlate Temporally with the Phosphorylation Status of TCE
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EMBO J
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, pp. 2377-2387
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Zinck1
Hipskind2
Pingoud3
Nordheim4
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19
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0027165150
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The Mitogen-Activated Protein Kinase Signal Transduction Pathway
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(1993)
J Biol Chem
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Davis1
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24
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0027250250
-
Mammalian ras Interacts Directly with the Serine/Threonine Kinase raf
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of special interest, The authors show that Raf-1 directly interacts with activated Ras. This may provide a mechanism for regulating Raf-1 activity
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(1993)
Cell
, vol.74
, pp. 205-214
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Vojtek1
Hollenberg2
Cooper3
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26
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0027225936
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Serum-Induced Translocation of Mitogen-Activated Protein Kinase to the Cell Surface Ruffling Membrane and the Nucleus
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of special interest, The nuclear translocation of ERK following growth factor stimulation is described.
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(1993)
J Cell Biol
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, pp. 1089-1101
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Gonzalez1
Seth2
Raden3
Bowman4
Fay5
Davis6
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27
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0027358722
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MKP-1 (3CH134), an Immediate Early Gene Product, Is a Dual Specificity Phosphatase that Dephosphorylates MAP Kinase in Vivo
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(1993)
Cell
, vol.75
, pp. 487-494
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Sun1
Charles2
Lau3
Tonks4
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28
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0025720735
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The Role of Jun, Fos and the AP-1 Complex in Cell Proliferation and Transformation
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Biochim Biophys Acta
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Angel1
Karin2
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29
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0026661584
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Control of Transcription Factor Activity by Phosphorylation: the Beginning of the End
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(1992)
Trends Biochem Sci
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Karin1
Smeal2
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40
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0027423418
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Identification of an Oncoprotein- and UV-Responsive Protein Kinase that Binds and Potentiates the c-Jun Activation Domain
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of outstanding interest, A protein kinase that binds to the activation domain of c-Jun and stimulates its activity through phosphorylation at Ser63 and Ser73 is described. This protein kinase, JNK, is activated following UV irradiation and transformation with Ha-Ras.
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(1993)
Genes Dev
, vol.7
, pp. 2135-2148
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Hibi1
Lin2
Smeal3
Minden4
Karin5
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41
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0028329953
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JNK1: A Protein Kinase Stimulated by UV Light and Ha-Ras that Binds and Phosphorylates the c-Jun Activation Domain
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of outstanding interest, A JNK cDNA clone is characterized, activated by dual phosphorylation, indicating it is a new member of the MAP kinase family.
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(1994)
Cell
, vol.76
, pp. 1025-1037
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Dérijard1
Hibi2
Wu3
Barrett4
Su5
Deng6
Karin7
Davis8
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42
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0024276523
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The Jun Protooncogene Is Positively Autoregulated by its Product, Jun.AP-1
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Angel1
Hattori2
Smeal3
Karin4
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Interferon-Induced Nuclear Factors that Bind a Shared Promoter Element Correlate with Positive and Negative Transcriptional Control
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Genes Dev
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Levy1
Kessler2
Pine3
Reich4
Darnell5
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44
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0024721567
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Cytoplasmic Activation of ISGF3, the Positive Regulator of Interferon-α-Stimulated Transcription, Reconstituted in Vitro
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Genes Dev
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Levy1
Kessler2
Pine3
Darnell4
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49
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0026723419
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A Transcription Factor with SH2 and SH3 Domains Is Directly Activated by an Interferon α-Induced Cytoplasmic Protein Tyrosine Kinase(s)
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(1992)
Cell
, vol.70
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Fu1
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50
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0026484261
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SH2 and SH3 Domains: From Structure to Function
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(1992)
Cell
, vol.71
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Pawson1
Gish2
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52
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0027493650
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A Single Phosphotyrosine Residue of Stat91 Required for Gene Activation by Interferon-Gamma
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of special interest, A genetic proof that phosphorylation of a specific tyrosine residue is a critical step in STAT1α activation.
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Science
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, pp. 1744-1746
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Shuai1
Stark2
Kerr3
Darnell4
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53
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0027498311
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Two Domains of ISGF3 γ that Mediate Protein DNA and Protein-Protein Interactions during Transcription Factor Assembly Contribute to DNA-Binding Specificity
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Mol Cell Biol
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, pp. 196-206
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Veals1
Santa Maria2
Levy3
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54
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0025084603
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Interferon-α Regulates Nuclear Translocation and DNA-Binding Affinity of ISGF3, a Multimeric Transcriptional Activator
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Genes Dev
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, pp. 1753-1765
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Kessler1
Veals2
Fu3
Levy4
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55
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0026069531
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Overlapping Elements in the Guanylate Binding Protein Gene Promoter Mediate Transcriptional Induction by α and γ Interferons
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(1992)
Mol Cell Biol
, vol.11
, pp. 182-191
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Lew1
Decker2
Streblow3
Darnell4
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56
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0026347205
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Characterization of the Promoter of the Human Gene Encoding the High Affinity IgG Receptor: Transcriptional Induction by γ-Interferon Is Mediated through Common DNA Response Elements
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(1991)
Proc Natl Acad Sci USA
, vol.88
, pp. 11305-11309
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Pearse1
Feinman2
Ravetch3
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59
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0027138211
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A Novel cis Element Mediating Ligand-Independent Activation by c-ErbA: Implications for Hormonal Regulation
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(1993)
Cell
, vol.75
, pp. 1095-1105
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Saatcioglu1
Deng2
Karin3
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64
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0027914830
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Cytokine Connections
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(1993)
Nature
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, pp. 114-116
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Hunter1
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66
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0027408634
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Cell-Free Activation of a DNA-Binding Protein by Epidermal Growth Factor
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of special interest, The first indication that activation of SIF may involve tyrosine phosphorylation and interaction with SH2 domains
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(1993)
Nature
, vol.362
, pp. 79-83
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Sadowski1
Gilman2
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67
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0027385186
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Induction of EGF and Interferon-γ of Tyrosine Phosphorylated DNA Binding Proteins in Mouse Liver Nuclei
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of special interest, EGF is shown to activate STAT proteins.
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(1993)
Science
, vol.261
, pp. 1733-1736
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Ruff-Jamison1
Chen2
Cohen3
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68
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0027371337
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Ras-Independent Growth Factor Signalling by Transcription Factor Tyrosine Phosphorylation
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of special interest, Growth factor activation of STAT proteins occurs through a Ras independent pathway.
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(1993)
Science
, vol.261
, pp. 1736-1739
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Silvennoinen1
Schindler2
Schlessinger3
Levy4
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69
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0027372119
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Transcription Factor p91 Interacts with the Epidermal Growth Factor Receptor and Mediates Activation of the c-fos Gene Promoter
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of special interest, Activation of STAT1α occur through direct binding and phosphorylation by the epidermal growth factor receptor.
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(1993)
Cell
, vol.74
, pp. 1135-1145
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Fu1
Zhang2
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71
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0027327484
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JAK2 associates with the erythro-poietin receptor and is tyrosine phosphorylated and activated following stimulation with erythropoietin
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of outstanding interest, The first indication that JAK2 activation occurs following cell-surface receptor stimulation.
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(1993)
Cell
, vol.74
, pp. 227-236
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Witthuhn1
Quelle2
Silvennoinen3
Yi4
Tang5
Miura6
Ihle7
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76
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0027253814
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FUS3 Phosphorylates Multiple Components of the Mating Signal Transduction Cascade: Evidence for STE12 and FAR1
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of outstanding interest, The authors demonstrate that FUS3 is physically associated with a set of proteins that are likely to represent its physiological substrates.
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(1993)
Mol Biol Cell
, vol.4
, pp. 495-510
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-
Elion1
Satterberg2
Krantz3
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