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Selective Affimers Recognize BCL-2 Family Proteins Through Non-Canonical Structural Motifs

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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Design and Evolution of a Miniature Bcl-2 Binding Protein

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Using a β‐Hairpin To Mimic an α‐Helix: Cyclic Peptidomimetic Inhibitors of the p53–HDM2 Protein–Protein Interaction

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Dissecting the Hydrophobic Effect on the Molecular Level: The Role of Water, Enthalpy, and Entropy in Ligand Binding to Thermolysin

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Selective and Potent Proteomimetic Inhibitors of Intracellular Protein–Protein Interactions

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Structure‐Based Design of Inhibitors of Protein–Protein Interactions: Mimicking Peptide Binding Epitopes

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Deactivation of Mcl‐1 by Dual‐Function Small‐Molecule Inhibitors Targeting the Bcl‐2 Homology 3 Domain and Facilitating Mcl‐1 Ubiquitination

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Structure–Activity Studies in a Family of β‐Hairpin Protein Epitope Mimetic Inhibitors of the p53–HDM2 Protein–Protein Interaction

inferredcites →https://doi.org/10.1002/cbic.201300351openalex-snapshot

Structure‐Guided Rational Design of α/β‐Peptide Foldamers with High Affinity for BCL‐2 Family Prosurvival Proteins

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Monobodies and other synthetic binding proteins for expanding protein science

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The fibronectin type III domain as a scaffold for novel binding proteins

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The Bcl-2 family: structures, interactions and targets for drug discovery

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Engineered protein scaffolds as leads for synthetic inhibitors of protein–protein interactions

inferredcites →https://doi.org/10.1016/j.ccr.2006.03.027openalex-snapshot

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

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Small-Molecule Inhibitors of Protein-Protein Interactions: Progressing toward the Reality

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Bcl-2 family of proteins as drug targets for cancer chemotherapy: the long way of BH3 mimetics from bench to bedside

inferredcites →https://doi.org/10.1016/j.jmb.2005.08.001openalex-snapshot

Design and Validation of a Neutral Protein Scaffold for the Presentation of Peptide Aptamers

inferredcites →https://doi.org/10.1016/j.jmb.2011.12.019openalex-snapshot

Teaching an Old Scaffold New Tricks: Monobodies Constructed Using Alternative Surfaces of the FN3 Scaffold

inferredcites →https://doi.org/10.1016/j.jmb.2012.05.022openalex-snapshot

Predictive Bcl-2 Family Binding Models Rooted in Experiment or Structure

inferredcites →https://doi.org/10.1016/j.jmb.2012.11.009openalex-snapshot

Structure-Based Redesign of the Binding Specificity of Anti-Apoptotic Bcl-xL

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Differential Targeting of Prosurvival Bcl-2 Proteins by Their BH3-Only Ligands Allows Complementary Apoptotic Function

inferredcites →https://doi.org/10.1016/j.molcel.2006.08.020openalex-snapshot

A Stapled BID BH3 Helix Directly Binds and Activates BAX

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Nanobody stabilization of G protein-coupled receptor conformational states

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Protein structure-based drug design: from docking to molecular dynamics

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Tertiary Structural Motif Sequence Statistics Enable Facile Prediction and Design of Peptides that Bind Anti-apoptotic Bfl-1 and Mcl-1

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Non-immunoglobulin scaffolds: a focus on their targets

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Designing Repeat Proteins: Well-expressed, Soluble and Stable Proteins from Combinatorial Libraries of Consensus Ankyrin Repeat Proteins

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[19] Free R value: Cross-validation in crystallography

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Navitoclax, a targeted high-affinity inhibitor of BCL-2, in lymphoid malignancies: a phase 1 dose-escalation study of safety, pharmacokinetics, pharmacodynamics, and antitumour activity

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Enthalpic and Entropic Contributions to Hydrophobicity

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In Silico and in Vitro Elucidation of BH3 Binding Specificity toward Bcl-2

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Peptide Ligands for Pro-survival Protein Bfl-1 from Computationally Guided Library Screening

inferredcites →https://doi.org/10.1021/cb500340wopenalex-snapshot

Designed BH3 Peptides with High Affinity and Specificity for Targeting Mcl-1 in Cells

inferredcites →https://doi.org/10.1021/cb501020ropenalex-snapshot

Hydrocarbon Stapled Peptides as Modulators of Biological Function

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Modulators of Protein–Protein Interactions

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How Can Hydrophobic Association Be Enthalpy Driven?

inferredcites →https://doi.org/10.1021/ja0441211openalex-snapshot

Paralog-Selective Ligands for Bcl-2 Proteins

inferredcites →https://doi.org/10.1021/jacs.5b05896openalex-snapshot

α/β-Peptide Foldamers Targeting Intracellular Protein–Protein Interactions with Activity in Living Cells

inferredcites →https://doi.org/10.1021/jm4001105openalex-snapshot

A Potent and Highly Efficacious Bcl-2/Bcl-xL Inhibitor

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Hydrocarbon-Stapled Peptides: Principles, Practice, and Progress

inferredcites →https://doi.org/10.1038/cdd.2013.153openalex-snapshot

The rheostat in the membrane: BCL-2 family proteins and apoptosis

inferredcites →https://doi.org/10.1038/cdd.2013.79openalex-snapshot

Evaluation and critical assessment of putative MCL-1 inhibitors

inferredcites →https://doi.org/10.1038/cddis.2014.561openalex-snapshot

Potent and selective small-molecule MCL-1 inhibitors demonstrate on-target cancer cell killing activity as single agents and in combination with ABT-263 (navitoclax)

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Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch

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Allosteric nanobodies reveal the dynamic range and diverse mechanisms of G-protein-coupled receptor activation

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Hypersensitive termination of the hypoxic response by a disordered protein switch

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An interconnected hierarchical model of cell death regulation by the BCL-2 family

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Inhibition of α-helix-mediated protein–protein interactions using designed molecules

inferredcites →https://doi.org/10.1038/nchembio.391openalex-snapshot

The MCL-1 BH3 Helix is an Exclusive MCL-1 Inhibitor and Apoptosis Sensitizer

inferredcites →https://doi.org/10.1038/nm.3048openalex-snapshot

ABT-199, a potent and selective BCL-2 inhibitor, achieves antitumor activity while sparing platelets

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BCL-2 family antagonists for cancer therapy

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Development of an Affimer-antibody combined immunological diagnosis kit for glypican-3

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Small molecules targeting Mcl-1: the search for a silver bullet in cancer therapy

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Hydrocarbon constrained peptides – understanding preorganisation and binding affinity

inferredcites →https://doi.org/10.1039/c6cc09395gopenalex-snapshot

Interfacing native and non-native peptides: using Affimers to recognise α-helix mimicking foldamers

inferredcites →https://doi.org/10.1073/pnas.1114107108openalex-snapshot

Mechanism of the hydrophobic effect in the biomolecular recognition of arylsulfonamides by carbonic anhydrase

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Interplay between partner and ligand facilitates the folding and binding of an intrinsically disordered protein

inferredcites →https://doi.org/10.1073/pnas.1707856115openalex-snapshot

Affimer proteins inhibit immune complex binding to FcγRIIIa with high specificity through competitive and allosteric modes of action

inferredcites →https://doi.org/10.1073/pnas.1812939115openalex-snapshot

Peptide design by optimization on a data-parameterized protein interaction landscape

inferredcites →https://doi.org/10.1074/jbc.m306021200openalex-snapshot

Bcl-XL Mutations Suppress Cellular Sensitivity to Antimycin A

inferredcites →https://doi.org/10.1093/protein/8.6.601openalex-snapshot

A combinatorial library of an α-helical bacterial receptor domain

inferredcites →https://doi.org/10.1093/protein/gzu007openalex-snapshot

Adhiron: a stable and versatile peptide display scaffold for molecular recognition applications

inferredcites →https://doi.org/10.1107/s0021889807021206openalex-snapshot

Phaser crystallographic software

inferredcites →https://doi.org/10.1107/s0021889809045701openalex-snapshot

xia2 : an expert system for macromolecular crystallography data reduction

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REFMAC 5 dictionary: organization of prior chemical knowledge and guidelines for its use

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MolProbity : all-atom structure validation for macromolecular crystallography

inferredcites →https://doi.org/10.1107/s0907444910007493openalex-snapshot

Features and development of Coot

inferredcites →https://doi.org/10.1107/s0907444996012255openalex-snapshot

Refinement of Macromolecular Structures by the Maximum-Likelihood Method

inferredcites →https://doi.org/10.1126/science.1099191openalex-snapshot

Activation of Apoptosis in Vivo by a Hydrocarbon-Stapled BH3 Helix

inferredcites →https://doi.org/10.1126/scisignal.aaj2005openalex-snapshot

Generation of specific inhibitors of SUMO-1– and SUMO-2/3–mediated protein-protein interactions using Affimer (Adhiron) technology

inferredcites →https://doi.org/10.1172/jci46231openalex-snapshot

A stapled BIM peptide overcomes apoptotic resistance in hematologic cancers

inferredcites →https://doi.org/10.7554/elife.20352openalex-snapshot

Computationally designed high specificity inhibitors delineate the roles of BCL2 family proteins in cancer

inferredcites →https://doi.org/10.7554/elife.24903openalex-snapshot

Affimer proteins are versatile and renewable affinity reagents

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1016/j.pep.2020.105677openalex-snapshot

Affimers as an alternative to antibodies for protein biomarker enrichment

inferred← citeshttps://doi.org/10.1038/s41467-021-24316-0openalex-snapshot

RAS-inhibiting biologics identify and probe druggable pockets including an SII-α3 allosteric site

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