NMR chemical shift and relaxation measurements provide evidence for the coupled folding and binding of the p53 transactivation domain - sprookjes - yvandenbroek - TriplyDB

NMR chemical shift and relaxation measurements provide evidence for the coupled folding and binding of the p53 transactivation domain

NMR chemical shift and relaxation measurements provide evidence for the coupled folding and binding of the p53 transactivation domain

http://www.wikidata.org/entity/Q24792064

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Fuzziness: linking regulation to protein dynamics Classification of intrinsically disordered regions and proteins Structural basis for p300 Taz2-p53 TAD1 binding and modulation by phosphorylation Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53 Fuzzy complexes: Specific binding without complete folding A dynamic model for replication protein A (RPA) function in DNA processing pathways Comparing models of evolution for ordered and disordered proteins.Single-stranded DNA mimicry in the p53 transactivation domain interaction with replication protein A Nontarget DNA binding shapes the dynamic landscape for enzymatic recognition of DNA damage.Regulatory functions of the N-terminal domain of the 70-kDa subunit of replication protein A (RPA)Two distinct motifs within the p53 transactivation domain bind to the Taz2 domain of p300 and are differentially affected by phosphorylation Pathological unfoldomics of uncontrolled chaos: intrinsically disordered proteins and human diseases Disorder predictors also predict backbone dynamics for a family of disordered proteins Impact of the K24N mutation on the transactivation domain of p53 and its binding to murine double-minute clone 2 DNA-PK, ATM and ATR collaboratively regulate p53-RPA interaction to facilitate homologous recombination DNA repair Secondary structure and dynamics of an intrinsically unstructured linker domain.A small molecule directly inhibits the p53 transactivation domain from binding to replication protein A.Alanine and proline content modulate global sensitivity to discrete perturbations in disordered proteins.Structural divergence is more extensive than sequence divergence for a family of intrinsically disordered proteins.Dual-site interactions of p53 protein transactivation domain with anti-apoptotic Bcl-2 family proteins reveal a highly convergent mechanism of divergent p53 pathways.Understanding the structural ensembles of a highly extended disordered protein.Regulation of cell division by intrinsically unstructured proteins: intrinsic flexibility, modularity, and signaling conduits.Physical and functional interactions between human mitochondrial single-stranded DNA-binding protein and tumour suppressor p53 A transient α-helical molecular recognition element in the disordered N-terminus of the Sgs1 helicase is critical for chromosome stability and binding of Top3/Rmi1.Using chemical shifts to generate structural ensembles for intrinsically disordered proteins with converged distributions of secondary structure.The relevance of protein-protein interactions for p53 function: the CPE contribution.Intrinsically disordered regions as affinity tuners in protein-DNA interactions.Backbone dynamics of the 18.5 kDa isoform of myelin basic protein reveals transient alpha-helices and a calmodulin-binding site.Proteins Recognizing DNA: Structural Uniqueness and Versatility of DNA-Binding Domains in Stem Cell Transcription Factors.Disorder and residual helicity alter p53-Mdm2 binding affinity and signaling in cells.FuzDB: database of fuzzy complexes, a tool to develop stochastic structure-function relationships for protein complexes and higher-order assemblies.Structural details on mdm2-p53 interaction.Long-range modulation of chain motions within the intrinsically disordered transactivation domain of tumor suppressor p53.Interaction between the transactivation domain of p53 and PC4 exemplifies acidic activation domains as single-stranded DNA mimics.Susceptibility of p53 unstructured N terminus to 20 S proteasomal degradation programs the stress response.Triple resonance ¹⁵Ν NMR relaxation experiments for studies of intrinsically disordered proteins.p53 binds the mdmx mRNA and controls its translation.

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NMR chemical shift and relaxation measurements provide evidence for the coupled folding and binding of the p53 transactivation domain

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2005 nî lūn-bûn

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NMR chemical shift and relaxat ...... the p53 transactivation domain

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NMR chemical shift and relaxat ...... the p53 transactivation domain

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NMR chemical shift and relaxat ...... the p53 transactivation domain

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NMR chemical shift and relaxat ...... the p53 transactivation domain

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NMR chemical shift and relaxat ...... the p53 transactivation domain

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NMR chemical shift and relaxat ...... the p53 transactivation domain

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NMR chemical shift and relaxat ...... the p53 transactivation domain

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NMR chemical shift and relaxat ...... the p53 transactivation domain

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NMR chemical shift and relaxat ...... the p53 transactivation domain

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Nucleic Acids Research

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NMR chemical shift and relaxat ...... the p53 transactivation domain

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Andrew J Latos

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Bharat Baral

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Gary W Daughdrill

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Pamela D Vise

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P2860

Replication Protein A (RPA): The Eukaryotic SSB

Identification of a novel p53 functional domain that is necessary for efficient growth suppression

Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA

RPA involvement in the damage-recognition and incision steps of nucleotide excision repair

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

Human replication protein A: global fold of the N-terminal RPA-70 domain reveals a basic cleft and flexible C-terminal linker

Crystal structure of the mouse p53 core DNA-binding domain at 2.7 A resolution

Solution structure of the tetrameric minimum transforming domain of p53

Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations

The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data

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2061-77

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10.1093/NAR/GKI336

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7

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33

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15824059

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1075921

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