C-terminal binding: an expanded repertoire and function of 14-3-3 proteins. - Wikidata - awgldk - TriplyDB

C-terminal binding: an expanded repertoire and function of 14-3-3 proteins.

C-terminal binding: an expanded repertoire and function of 14-3-3 proteins.

http://www.wikidata.org/entity/Q36403805

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Structural Analysis of the 14-3-3ζ/Chibby Interaction Involved in Wnt/β-Catenin Signaling The chaperone-like protein 14-3-3η interacts with human α-synuclein aggregation intermediates rerouting the amyloidogenic pathway and reducing α-synuclein cellular toxicity The central proline rich region of POB1/REPS2 plays a regulatory role in epidermal growth factor receptor endocytosis by binding to 14-3-3 and SH3 domain-containing proteins Regulation of IRSp53-dependent filopodial dynamics by antagonism between 14-3-3 binding and SH3-mediated localization.Modulation of 14-3-3 interaction with phosphorylated histone H3 by combinatorial modification patterns Protein kinase A-mediated 14-3-3 association impedes human Dapper1 to promote dishevelled degradation Phosphorylation-independent interaction between 14-3-3 and exoenzyme S: from structure to pathogenesis Discovery and structural characterization of a small molecule 14-3-3 protein-protein interaction inhibitor The crystal structure of Giardia duodenalis 14-3-3 in the apo form: when protein post-translational modifications make the difference Quantitative proteomics analysis reveals BAG3 as a potential target to suppress severe acute respiratory syndrome coronavirus replication Insight into conformational change for 14-3-3σ protein by molecular dynamics simulation.Emerging evidence for the importance of phosphorylation in the regulation of NADPH oxidases.The Arabidopsis ABA-activated kinase OST1 phosphorylates the bZIP transcription factor ABF3 and creates a 14-3-3 binding site involved in its turnover Phosphorylation-dependent protein interaction with Trypanosoma brucei 14-3-3 proteins that display atypical target recognition 14-3-3ε boosts bleomycin-induced DNA damage response by inhibiting the drug-resistant activity of MVP Electrostatic interactions play a minor role in the binding of ExoS to 14-3-3 proteins 14-3-3ε mediates the cell fate decision-making pathways in response of hepatocellular carcinoma to Bleomycin-induced DNA damage.PI3K/Akt signalling-mediated protein surface expression sensed by 14-3-3 interacting motif.Specificity of ε and non-ε isoforms of arabidopsis 14-3-3 proteins towards the H+-ATPase and other targets Transcriptional regulation of YWHAZ, the gene encoding 14-3-3ζ.Protein-protein interactions as drug targets.The Functional Human C-Terminome In vivo functional specificity and homeostasis of Drosophila 14-3-3 proteins.The Hsp70 homolog Ssb and the 14-3-3 protein Bmh1 jointly regulate transcription of glucose repressed genes in Saccharomyces cerevisiae Kinase-dependent regulation of inositol 1,4,5-trisphosphate-dependent Ca2+ release during oocyte maturation.Oligomeric structure of 14-3-3 protein: what do we know about monomers?PRMT5 C-terminal Phosphorylation Modulates a 14-3-3/PDZ Interaction Switch.Moonlighting chaperone-like activity of the universal regulatory 14-3-3 proteins.Quantitative proteomic dissection of a native 14-3-3ε interacting protein complex associated with hepatocellular carcinoma.Cyclic nucleotide dependent dephosphorylation of regulator of G-protein signaling 18 in human platelets.The phytotoxin fusicoccin promotes platelet aggregation via 14-3-3-glycoprotein Ib-IX-V interaction.Biotin tagging coupled with amino acid-coded mass tagging for efficient and precise screening of interaction proteome in mammalian cells Interrogation of phosphor-specific interaction on a high-throughput label-free optical biosensor system-Epic system.Bioinformatic and experimental survey of 14-3-3-binding sites.The carboxyl-terminal PDZ ligand motif of chemokine receptor CXCR2 modulates post-endocytic sorting and cellular chemotaxis.Structure of the 14-3-3ζ-LKB1 fusion protein provides insight into a novel ligand-binding mode of 14-3-3.14-3-3-Pred: improved methods to predict 14-3-3-binding phosphopeptides Chimeric 14-3-3 proteins for unraveling interactions with intrinsically disordered partners.Monomeric 14-3-3ζ has a chaperone-like activity and is stabilized by phosphorylated HspB6.14-3-3 (Bmh) proteins inhibit transcription activation by Adr1 through direct binding to its regulatory domain.

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C-terminal binding: an expanded repertoire and function of 14-3-3 proteins.

http://www.wikidata.org/entity/Q36403805

description

2006 nî lūn-bûn

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2006年の論文

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2006年学术文章

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2006年学术文章

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2006年学术文章

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2006年学术文章

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2006年学术文章

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2006年學術文章

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2006年學術文章

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2006年學術文章

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name

C-terminal binding: an expanded repertoire and function of 14-3-3 proteins.

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C-terminal binding: an expanded repertoire and function of 14-3-3 proteins.

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type

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C-terminal binding: an expanded repertoire and function of 14-3-3 proteins.

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C-terminal binding: an expanded repertoire and function of 14-3-3 proteins.

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C-terminal binding: an expanded repertoire and function of 14-3-3 proteins.

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C-terminal binding: an expanded repertoire and function of 14-3-3 proteins.

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Brian Coblitz

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Meng Wu

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Min Li

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Sojin Shikano

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P2860

Crystal structure of the 14-3-3zeta:serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation

Molecular basis for the recognition of phosphorylated and phosphoacetylated histone h3 by 14-3-3

14-3-3 Protein interacts with nuclear localization sequence of forkhead transcription factor FoxO4

Interaction of 14-3-3 with signaling proteins is mediated by the recognition of phosphoserine

14-3-3zeta interacts with the alpha-chain of human interleukin 9 receptor

On the attribution and additivity of binding energies

Interaction with 14-3-3 proteins promotes functional expression of the potassium channels TASK-1 and TASK-3

Structural analysis of 14-3-3 phosphopeptide complexes identifies a dual role for the nuclear export signal of 14-3-3 in ligand binding

Structural view of a fungal toxin acting on a 14-3-3 regulatory complex

Forward transport. 14-3-3 binding overcomes retention in endoplasmic reticulum by dibasic signals

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