Structural Basis of Bcl-xL Recognition by a BH3-Mimetic α/β-Peptide Generated by Sequence-Based Design - Test2 - elhamkhani - TriplyDB

Structural Basis of Bcl-xL Recognition by a BH3-Mimetic α/β-Peptide Generated by Sequence-Based Design

Structural Basis of Bcl-xL Recognition by a BH3-Mimetic α/β-Peptide Generated by Sequence-Based Design

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Stapled BH3 peptides against MCL-1: mechanism and design using atomistic simulations Evaluation of Diverse α/β-Backbone Patterns for Functional α-Helix Mimicry: Analogues of the Bim BH3 Domain 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 Structural similarity between β(3)-peptides synthesized from β(3)-homo-amino acids and aspartic acid monomers.A β-peptide agonist of the GLP-1 receptor, a class B GPCR.Crystal structure of an amphiphilic foldamer reveals a 48-mer assembly comprising a hollow truncated octahedron Folding and binding of an intrinsically disordered protein: fast, but not 'diffusion-limited'.Folding and function in α/β-peptides: targets and therapeutic applications.Behavior of solvent-exposed hydrophobic groove in the anti-apoptotic Bcl-XL protein: clues for its ability to bind diverse BH3 ligands from MD simulations.Probing Protein Surfaces: QSAR Analysis with Helix Mimetics.Structural biology of the intrinsic cell death pathway: what do we know and what is missing?Molecular determinants of the binding specificity of BH3 ligands to BclXL apoptotic repressor.Peptide and peptoid foldamers in medicinal chemistry.Cell death and the mitochondria: therapeutic targeting of the BCL-2 family-driven pathway.Residue-Based Preorganization of BH3-Derived α/β-Peptides: Modulating Affinity, Selectivity and Proteolytic Susceptibility in α-Helix Mimics.New Modalities for Challenging Targets in Drug Discovery.α/β-Peptide Foldamers Targeting Intracellular Protein-Protein Interactions with Activity in Living Cells.Extending foldamer design beyond α-helix mimicry: α/β-peptide inhibitors of vascular endothelial growth factor signaling.α-Helix mimicry with α/β-peptides.Hydrocarbon constrained peptides - understanding preorganisation and binding affinity.Stereocontrolled protein surface recognition using chiral oligoamide proteomimetic foldamers† †Electronic supplementary information (ESI) available. See DOI: 10.1039/c4sc03559c Click here for additional data file.Stereocontrolled protein surface recognition using chiral oligoamide proteomimetic foldamers.Helix Propensities of Amino Acid Residues via Thioester Exchange.Aromatic Oligoamide Foldamers with a “Wet Edge” as Inhibitors of the α-Helix-Mediated p53-hDM2 Protein-Protein Interaction

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Structural Basis of Bcl-xL Recognition by a BH3-Mimetic α/β-Peptide Generated by Sequence-Based Design

http://www.wikidata.org/entity/Q27670755

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2011 nî lūn-bûn

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2011 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

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2011 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2011年の論文

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Structural Basis of Bcl-xL Rec ...... rated by Sequence-Based Design

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Structural Basis of Bcl-xL Rec ...... rated by Sequence-Based Design

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Structural Basis of Bcl-xL Rec ...... rated by Sequence-Based Design

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Structural Basis of Bcl-xL Rec ...... rated by Sequence-Based Design

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Structural Basis of Bcl-xL Rec ...... rated by Sequence-Based Design

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Structural Basis of Bcl-xL Rec ...... rated by Sequence-Based Design

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Kelsey N Mayer

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

Marco Evangelista

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

Peter M Colman

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Samuel H Gellman

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W Douglas Fairlie

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W Seth Horne

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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.

Mutation to Bax beyond the BH3 domain disrupts interactions with pro-survival proteins and promotes apoptosis

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

Systematic analysis of helical protein interfaces reveals targets for synthetic inhibitors

Rationale for Bcl-xL/Bad peptide complex formation from structure, mutagenesis, and biophysical studies

Processing of X-ray diffraction data collected in oscillation mode

The structure of a Bcl-xL/Bim fragment complex: implications for Bim function

Crystal structure of the Bcl-XL-Beclin 1 peptide complex: Beclin 1 is a novel BH3-only protein

Helix bundle quaternary structure from alpha/beta-peptide foldamers

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2025-32

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scholarly article

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10.1002/CBIC.201100314

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13

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12

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2011-09-05T00:00:00Z

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51481978

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21744457

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3263372

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