Potent inhibitors of LXXLL-based protein-protein interactions. - Wikidata - wikimedia - TriplyDB

Potent inhibitors of LXXLL-based protein-protein interactions.

Potent inhibitors of LXXLL-based protein-protein interactions.

http://www.wikidata.org/entity/Q46750747

about

Development of a novel molecular sensor for imaging estrogen receptor-coactivator protein-protein interactions The molecular basis of the interaction between the proline-rich SH3-binding motif of PNRC and estrogen receptor alpha.Constraining cyclic peptides to mimic protein structure motifs.Dual-purpose linker for alpha helix stabilization and imaging agent conjugation to glucagon-like peptide-1 receptor ligands.Tetrahydro-iso-alpha Acids Antagonize Estrogen Receptor Alpha Activity in MCF-7 Breast Cancer Cells Blocking estrogen signaling after the hormone: pyrimidine-core inhibitors of estrogen receptor-coactivator binding.Minireview: Not picking pockets: nuclear receptor alternate-site modulators (NRAMs)Discovering small-molecule estrogen receptor α/coactivator binding inhibitors: high-throughput screening, ligand development, and models for enhanced potency.Positional screening and NMR structure determination of side-chain-to-side-chain cyclized β3-peptides.Noncanonical mechanisms to regulate nuclear receptor signaling.MED25 is a mediator component of HNF4α-driven transcription leading to insulin secretion in pancreatic beta-cells.Steroid receptor coactivators 1, 2, and 3: critical regulators of nuclear receptor activity and steroid receptor modulator (SRM)-based cancer therapy Inhibitors for the Vitamin D Receptor-Coregulator Interaction.Regulatory function of the P295-T311 motif of the estrogen receptor alpha - does proteasomal degradation of the receptor induce emergence of peptides implicated in estrogenic responses?A Helix-Stabilizing Linker Improves Subcutaneous Bioavailability of a Helical Peptide Independent of Linker Lipophilicity.Beyond the ligand-binding pocket: targeting alternate sites in nuclear receptors.Structure-Based Design of Inhibitors of Protein-Protein Interactions: Mimicking Peptide Binding Epitopes.Bicyclo[2.2.2]octanes: close structural mimics of the nuclear receptor-binding motif of steroid receptor coactivators.Investigating hydrophobic ligand-receptor interactions in parathyroid hormone receptor using peptide probes.Perfluoro-tert-butyl Homoserine Is a Helix-Promoting, Highly Fluorinated, NMR-Sensitive Aliphatic Amino Acid: Detection of the Estrogen Receptor·Coactivator Protein-Protein Interaction by 19F NMR.A Cell-Permeable Stapled Peptide Inhibitor of the Estrogen Receptor/Coactivator Interaction.Crosslinked Aspartic Acids as Helix-Nucleating Templates.Probing the effect of MODY mutations near the co-activator-binding pocket of HNF4α.Foldamers as Anticancer Therapeutics: Targeting Protein-Protein Interactions and the Cell Membrane.Stimuli-responsive α-helical peptide gatekeepers for mesoporous silica nanocarriers Structure–activity relationship studies of miniproteins targeting the androgen receptor–coactivator interaction

P2860

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P2860

Potent inhibitors of LXXLL-based protein-protein interactions.

http://www.wikidata.org/entity/Q46750747

description

2005 nî lūn-bûn

@nan

2005年の論文

@ja

2005年学术文章

@wuu

2005年学术文章

@zh-cn

2005年学术文章

@zh-hans

2005年学术文章

@zh-my

2005年学术文章

@zh-sg

2005年學術文章

@yue

2005年學術文章

@zh

2005年學術文章

@zh-hant

name

Potent inhibitors of LXXLL-based protein-protein interactions.

@en

Potent inhibitors of LXXLL-based protein-protein interactions.

@nl

type

label

Potent inhibitors of LXXLL-based protein-protein interactions.

@en

Potent inhibitors of LXXLL-based protein-protein interactions.

@nl

prefLabel

Potent inhibitors of LXXLL-based protein-protein interactions.

@en

Potent inhibitors of LXXLL-based protein-protein interactions.

@nl

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Potent inhibitors of LXXLL-based protein-protein interactions

@en

P2093

Amit K Galande

http://www.w3.org/2001/XMLSchema#string

Arno F Spatola

http://www.w3.org/2001/XMLSchema#string

James L Wittliff

http://www.w3.org/2001/XMLSchema#string

John O Trent

http://www.w3.org/2001/XMLSchema#string

Kelli S Bramlett

http://www.w3.org/2001/XMLSchema#string

P2860

Helix-stabilized cyclic peptides as selective inhibitors of steroid receptor-coactivator interactions

Molecular basis of agonism and antagonism in the oestrogen receptor

Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-gamma

Structure and specificity of nuclear receptor-coactivator interactions

The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen

A signature motif in transcriptional co-activators mediates binding to nuclear receptors

Molecular determinants for the tissue specificity of SERMs

Determinants of coactivator LXXLL motif specificity in nuclear receptor transcriptional activation

Dissection of the LXXLL nuclear receptor-coactivator interaction motif using combinatorial peptide libraries: discovery of peptide antagonists of estrogen receptors alpha and beta.

Novel selective inhibitors of the interaction of individual nuclear hormone receptors with a mutually shared steroid receptor coactivator 2.

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1991-1998

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scholarly article

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10.1002/CBIC.200500083

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11

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6

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2005-11-01T00:00:00Z

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16222726

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