Transient structure and dynamics in the disordered c-Myc transactivation domain affect Bin1 binding. - Wikidata - awgldk - TriplyDB

Transient structure and dynamics in the disordered c-Myc transactivation domain affect Bin1 binding.

Transient structure and dynamics in the disordered c-Myc transactivation domain affect Bin1 binding.

http://www.wikidata.org/entity/Q42053910

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Computational approaches for inferring the functions of intrinsically disordered proteins Fuzzy complexes: Specific binding without complete folding Protein Folding and Mechanisms of Proteostasis Relating sequence encoded information to form and function of intrinsically disordered proteins Pre-Anchoring of Pin1 to Unphosphorylated c-Myc in a Fuzzy Complex Regulates c-Myc Activity.High-resolution structure of TBP with TAF1 reveals anchoring patterns in transcriptional regulation Characterization of ERM transactivation domain binding to the ACID/PTOV domain of the Mediator subunit MED25 Silencing c-Myc translation as a therapeutic strategy through targeting PI3Kδ and CK1ε in hematological malignancies Hepatitis C virus NS5A is able to competitively displace c-Myc from the Bin1 SH3 domain in vitro.Resilience of death: intrinsic disorder in proteins involved in the programmed cell death.Transcriptional repressor domain of MBD1 is intrinsically disordered and interacts with its binding partners in a selective manner MYC interacts with the human STAGA coactivator complex via multivalent contacts with the GCN5 and TRRAP subunits.The Stress-response protein prostate-associated gene 4, interacts with c-Jun and potentiates its transactivation.Therapeutic strategies to inhibit MYC Protein/protein interactions in the mammalian heme degradation pathway: heme oxygenase-2, cytochrome P450 reductase, and biliverdin reductase MTMDAT-HADDOCK: high-throughput, protein complex structure modeling based on limited proteolysis and mass spectrometry Origins of Myc proteins--using intrinsic protein disorder to trace distant relatives.Spectroscopic studies reveal that the heme regulatory motifs of heme oxygenase-2 are dynamically disordered and exhibit redox-dependent interaction with heme.Dynamic Protein Interaction Networks and New Structural Paradigms in Signaling.Phosphorylation-induced Conformational Ensemble Switching in an Intrinsically Disordered Cancer/Testis Antigen.From sequence and forces to structure, function, and evolution of intrinsically disordered proteins Pluralistic and stochastic gene regulation: examples, models and consistent theory.MYC interaction with the tumor suppressive SWI/SNF complex member INI1 regulates transcription and cellular transformation.Identification of a novel transcript isoform of the TTLL12 gene in human cancers Therapeutic Interventions of Cancers Using Intrinsically Disordered Proteins as Drug Targets: c-Myc as Model System.Phosphorylation-induced conformational dynamics in an intrinsically disordered protein and potential role in phenotypic heterogeneity.FuzDB: database of fuzzy complexes, a tool to develop stochastic structure-function relationships for protein complexes and higher-order assemblies.Phenotypic Plasticity and Cell Fate Decisions in Cancer: Insights from Dynamical Systems Theory Complex domain interactions regulate stability and activity of closely related proneural transcription factors.MB0 and MBI Are Independent and Distinct Transactivation Domains in MYC that Are Essential for Transformation.Long disordered regions of the C-terminal domain of Abelson tyrosine kinase have specific and additive functions in regulation and axon localization.An NMR study on the intrinsically disordered core transactivation domain of human glucocorticoid receptor.Fuzziness enables context dependence of protein interactions.Structural Characterization of the Intrinsically Disordered Protein p53 Using Raman Spectroscopy.Phenotypic Plasticity, Bet-Hedging, and Androgen Independence in Prostate Cancer: Role of Non-Genetic Heterogeneity.Regulation and Function of the MYC Oncogene Mammalian MYC Proteins and Cancer

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Transient structure and dynamics in the disordered c-Myc transactivation domain affect Bin1 binding.

http://www.wikidata.org/entity/Q42053910

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2012年論文

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name

Transient structure and dynami ...... on domain affect Bin1 binding.

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Transient structure and dynami ...... on domain affect Bin1 binding.

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Transient structure and dynami ...... on domain affect Bin1 binding.

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Transient structure and dynami ...... on domain affect Bin1 binding.

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Transient structure and dynami ...... on domain affect Bin1 binding.

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Transient structure and dynami ...... on domain affect Bin1 binding.

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Nucleic Acids Research

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Transient structure and dynami ...... on domain affect Bin1 binding.

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Christophe Farès

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Jonas Carlsson

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Maria Sunnerhagen

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Patrik Lundström

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Sara Helander

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Veronika Csizmok

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P2860

BRICHOS - a superfamily of multidomain proteins with diverse functions

Intrinsically unstructured proteins and their functions

Efficient p53 activation and apoptosis by simultaneous disruption of binding to MDM2 and MDMX

A structure-based model of the c-Myc/Bin1 protein interaction shows alternative splicing of Bin1 and c-Myc phosphorylation are key binding determinants

Identification of a novel c-Myc protein interactor, JPO2, with transforming activity in medulloblastoma cells

The Axin1 scaffold protein promotes formation of a degradation complex for c-Myc

Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain

Proteomic profiling of Myc-associated proteins

BIN1 is a novel MYC-interacting protein with features of a tumour suppressor

The novel ATM-related protein TRRAP is an essential cofactor for the c-Myc and E2F oncoproteins

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10.1093/NAR/GKS263

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13

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40

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Alexander Lemak

Julie D Forman-Kay

Cecilia Andresen

Cheryl Arrowsmith

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2012-03-28T00:00:00Z

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223136810

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22457068

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3401448

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