Thermodynamic and Structural Effects of Macrocyclization as a Constraining Method in Protein-Ligand Interactions. - Wikidata - awgldk - TriplyDB

Thermodynamic and Structural Effects of Macrocyclization as a Constraining Method in Protein-Ligand Interactions.

Thermodynamic and Structural Effects of Macrocyclization as a Constraining Method in Protein-Ligand Interactions.

http://www.wikidata.org/entity/Q27666108

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Protein–Ligand Interactions: Thermodynamic Effects Associated with Increasing Nonpolar Surface Area High Resolution Crystal Structure of the Grb2 SH2 Domain with a Phosphopeptide Derived from CD28 Protein–ligand interactions: Probing the energetics of a putative cation–π interaction Structural and biophysical investigation of the interaction of a mutant Grb2 SH2 domain (W121G) with its cognate phosphopeptide.Entropy-enthalpy compensation: role and ramifications in biomolecular ligand recognition and design.Applications of isothermal titration calorimetry in pure and applied research--survey of the literature from 2010.Probing the effect of conformational constraint on phosphorylated ligand binding to an SH2 domain using polarizable force field simulations.Hitting a Moving Target: How Does an N-Methyl Group Impact Biological Activity?Protein-Ligand Interactions: Thermodynamic Effects Associated with Increasing the Length of an Alkyl Chain.Peptides and proteins as a continuing exciting source of inspiration for peptidomimetics.Limiting assumptions in structure-based design: binding entropy.Macrocycles in new drug discovery.Polyketide synthase and non-ribosomal peptide synthetase thioesterase selectivity: logic gate or a victim of fate?Natural Products and Their Mimics as Targets of Opportunity for Discovery.Flexibility is important for inhibition of the MDM2/p53 protein-protein interaction by cyclic β-hairpins.Design and optimisation of bioactive cyclic peptides: generation of a down-regulator of TNF secretion.Synthesis and Cytotoxicity of Semisynthetic Withalongolide A Analogues.Peptide bicycles that inhibit the Grb2 SH2 domain.Comparison of diffusion coefficients for matched pairs of macrocyclic and linear molecules over a drug-like molecular weight range.Increased Conformational Flexibility of a Macrocycle-Receptor Complex Contributes to Reduced Dissociation Rates.Flexibility vs rigidity of amphipathic peptide conjugates when interacting with lipid bilayers.Elucidating the energetic contributions to the binding free energy.Synthesis, structure and reactivity of [15]-macrodilactones.

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P2860

Thermodynamic and Structural Effects of Macrocyclization as a Constraining Method in Protein-Ligand Interactions.

http://www.wikidata.org/entity/Q27666108

description

2010 nî lūn-bûn

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2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

Thermodynamic and Structural E ...... in Protein−Ligand Interactions

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Thermodynamic and Structural E ...... n Protein-Ligand Interactions.

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Thermodynamic and Structural E ...... n Protein-Ligand Interactions.

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Thermodynamic and Structural E ...... in Protein−Ligand Interactions

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Thermodynamic and Structural E ...... in Protein−Ligand Interactions

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Thermodynamic and Structural E ...... n Protein-Ligand Interactions.

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Thermodynamic and Structural E ...... n Protein-Ligand Interactions.

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P1433

ACS Medicinal Chemistry Letters

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Thermodynamic and Structural E ...... n Protein-Ligand Interactions.

@en

P2093

Benjamin B Whiddon

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John E Delorbe

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John H Clements

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Stephen F Martin

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P2860

Crystal structures of the SH2 domain of Grb2: highlight on the binding of a new high-affinity inhibitor

Structural and conformational requirements for high-affinity binding to the SH2 domain of Grb2(1)

Calorimetric and structural studies of 1,2,3-trisubstituted cyclopropanes as conformationally constrained peptide inhibitors of Src SH2 domain binding

Thermodynamic and structural effects of conformational constraints in protein-ligand interactions. Entropic paradoxy associated with ligand preorganization

Structural basis for specificity of Grb2-SH2 revealed by a novel ligand binding mode

Lowering the entropic barrier for binding conformationally flexible inhibitors to enzymes

Structure-based design of thioether-bridged cyclic phosphopeptides binding to Grb2-SH2 domain.

Utilization of a beta-aminophosphotyrosyl mimetic in the design and synthesis of macrocyclic Grb2 SH2 domain-binding peptides.

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448-452

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scholarly article

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10.1021/ML100142Y

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8

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1

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2010-11-01T00:00:00Z

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49644142

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21116482

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Aagianik kimischri

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2992351

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