Sequence-based design of alpha/beta-peptide foldamers that mimic BH3 domains. - Wikidata - awgldk - TriplyDB

Sequence-based design of alpha/beta-peptide foldamers that mimic BH3 domains.

Sequence-based design of alpha/beta-peptide foldamers that mimic BH3 domains.

http://www.wikidata.org/entity/Q42146826

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Protein backbone engineering as a strategy to advance foldamers toward the frontier of protein-like tertiary structure Adding diverse noncanonical backbones to rosetta: enabling peptidomimetic design Interplay among side chain sequence, backbone composition, and residue rigidification in polypeptide folding and assembly High-Resolution Structural Characterization of a Helical α/β-Peptide Foldamer Bound to the Anti-Apoptotic Protein Bcl-xL Structural and biological mimicry of protein surface recognition by / -peptide foldamers Structural Consequences of β-Amino Acid Preorganization in a Self-Assembling α/β-Peptide: Fundamental Studies of Foldameric Helix Bundles Intrinsic Order and Disorder in the Bcl-2 Member Harakiri: Insights into Its Proapoptotic Activity Structural Basis of Bcl-xL Recognition by a BH3-Mimetic α/β-Peptide Generated by Sequence-Based Design Rational Design of Proteolytically Stable, Cell-Permeable Peptide-Based Selective Mcl-1 Inhibitors Evaluation of Diverse α/β-Backbone Patterns for Functional α-Helix Mimicry: Analogues of the Bim BH3 Domain Quasiracemic Crystallization as a Tool To Assess the Accommodation of Noncanonical Residues in Nativelike Protein Conformations Differential Impact of β and γ Residue Preorganization on α/β/γ-Peptide Helix Stability in Water Enhancement of α-Helix Mimicry by an α/β-Peptide Foldamer via Incorporation of a Dense Ionic Side-Chain Array Structure-Guided Rational Design of α/β-Peptide Foldamers with High Affinity for BCL-2 Family Prosurvival Proteins Structure of a complex formed by a protein and a helical aromatic oligoamide foldamer at 2.1 Å resolution A foldamer-dendrimer conjugate neutralizes synaptotoxic β-amyloid oligomers Characterization of a novel interaction between Bcl-2 members Diva and Harakiri.Comparison of backbone modification in protein β-sheets by α→γ residue replacement and α-residue methylation.A potent α/β-peptide analogue of GLP-1 with prolonged action in vivo.Folding and function in α/β-peptides: targets and therapeutic applications.Consequences of periodic α-to-β(3) residue replacement for immunological recognition of peptide epitopes.Discovering functional, non-proteinogenic amino acid containing, peptides using genetic code reprogramming.Foldamers with heterogeneous backbones.Molecular determinants of the binding specificity of BH3 ligands to BclXL apoptotic repressor.Helix-mediated protein--protein interactions as targets for intervention using foldamers.α/β-Peptide foldamers: state of the art.Stabilized helical peptides: overview of the technologies and therapeutic promises.Peptide and peptoid foldamers in medicinal chemistry.Residue-Based Preorganization of BH3-Derived α/β-Peptides: Modulating Affinity, Selectivity and Proteolytic Susceptibility in α-Helix Mimics.Modulating protein-protein interactions: the potential of peptides.Structure-Based Design of Inhibitors of Protein-Protein Interactions: Mimicking Peptide Binding Epitopes.An overview of peptide and peptoid foldamers in medicinal chemistry.Characterization of signal bias at the GLP-1 receptor induced by backbone modification of GLP-1.Targeting recognition surfaces on natural proteins with peptidic foldamers Iterative Nonproteinogenic Residue Incorporation Yields α/β-Peptides with a Helix-Loop-Helix Tertiary Structure and High Affinity for VEGF.Facile synthesis of stapled, structurally reinforced peptide helices via a photoinduced intramolecular 1,3-dipolar cycloaddition reaction.α/β-Peptide Foldamers Targeting Intracellular Protein-Protein Interactions with Activity in Living Cells.An α-Helix-Mimicking 12,13-Helix: Designed α/β/γ-Foldamers as Selective Inhibitors of Protein-Protein Interactions.Computational design of a self-assembling β-peptide oligomer.Extending foldamer design beyond α-helix mimicry: α/β-peptide inhibitors of vascular endothelial growth factor signaling.

P2860

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P2860

Sequence-based design of alpha/beta-peptide foldamers that mimic BH3 domains.

http://www.wikidata.org/entity/Q42146826

description

2008 nî lūn-bûn

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2008年の論文

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2008年論文

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2008年論文

@zh-hant

2008年論文

@zh-hk

2008年論文

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2008年論文

@zh-tw

2008年论文

@wuu

2008年论文

@zh

2008年论文

@zh-cn

name

Sequence-based design of alpha/beta-peptide foldamers that mimic BH3 domains.

@en

Sequence-based design of alpha/beta-peptide foldamers that mimic BH3 domains.

@nl

type

label

Sequence-based design of alpha/beta-peptide foldamers that mimic BH3 domains.

@en

Sequence-based design of alpha/beta-peptide foldamers that mimic BH3 domains.

@nl

prefLabel

Sequence-based design of alpha/beta-peptide foldamers that mimic BH3 domains.

@en

Sequence-based design of alpha/beta-peptide foldamers that mimic BH3 domains.

@nl

P1433

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Angewandte Chemie International Edition

P1476

Sequence-based design of alpha/beta-peptide foldamers that mimic BH3 domains

@en

P2093

Melissa D Boersma

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

Samuel H Gellman

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

W Seth Horne

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

P2860

Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function

Proapoptotic Bak is sequestered by Mcl-1 and Bcl-xL, but not Bcl-2, until displaced by BH3-only proteins.

Mitochondria primed by death signals determine cellular addiction to antiapoptotic BCL-2 family members

Activation of apoptosis in vivo by a hydrocarbon-stapled BH3 helix.

The Bcl-2 apoptotic switch in cancer development and therapy

Helix bundle quaternary structure from alpha/beta-peptide foldamers

Structural insights into the degradation of Mcl-1 induced by BH3 domains

Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis

Proteinase K from Tritirachium album Limber

Foldamers as versatile frameworks for the design and evolution of function

P304

2853-2856

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scholarly article

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10.1002/ANIE.200705315

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P433

15

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47

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P50

Matthew A Windsor

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2008-01-01T00:00:00Z

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5521118

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18330876

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3429126

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