Backbone modification of a polypeptide drug alters duration of action in vivo.
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Cyclic and Macrocyclic Peptides as Chemical Tools To Recognise Protein Surfaces and Probe Protein-Protein InteractionsPTH receptor-1 signalling-mechanistic insights and therapeutic prospectsProtein backbone engineering as a strategy to advance foldamers toward the frontier of protein-like tertiary structureEffects of Single α-to-β Residue Replacements on Structure and Stability in a Small Protein: Insights from Quasiracemic CrystallizationProgrammable polyproteams built using twin peptide supergluesPeptide-functionalized semiconductor surfaces: strong surface electronic effects from minor alterations to backbone composition.Administration frequency as well as dosage of PTH are associated with development of cortical porosity in ovariectomized rats.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.Targeting diverse protein-protein interaction interfaces with α/β-peptides derived from the Z-domain scaffold.Selective and potent proteomimetic inhibitors of intracellular protein-protein interactionsProbing Protein Surfaces: QSAR Analysis with Helix Mimetics.A Homozygous [Cys25]PTH(1-84) Mutation That Impairs PTH/PTHrP Receptor Activation Defines a Novel Form of Hypoparathyroidism.Improving the Binding Affinity of in-Vitro-Evolved Cyclic Peptides by Inserting Atoms into the Macrocycle Backbone.Selective VIP Receptor Agonists Facilitate Immune Transformation for Dopaminergic Neuroprotection in MPTP-Intoxicated Mice.Comparison of design strategies for α-helix backbone modification in a protein tertiary fold.Engineering a long-acting, potent GLP-1 analog for microstructure-based transdermal delivery.Prolonged Pharmacokinetic and Pharmacodynamic Actions of a Pegylated Parathyroid Hormone (1-34) Peptide Fragment.New Modalities for Challenging Targets in Drug Discovery.Modulating protein-protein interactions: the potential of peptides.Structure-Based Design of Inhibitors of Protein-Protein Interactions: Mimicking Peptide Binding Epitopes.Characterization of signal bias at the GLP-1 receptor induced by backbone modification of GLP-1.Targeting recognition surfaces on natural proteins with peptidic foldamersIterative Nonproteinogenic Residue Incorporation Yields α/β-Peptides with a Helix-Loop-Helix Tertiary Structure and High Affinity for VEGF.PPII Helical Peptidomimetics Templated by Cation-π Interactions.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.Pharmacodynamic Actions of a Long-Acting PTH Analog (LA-PTH) in Thyroparathyroidectomized (TPTX) Rats and Normal Monkeys.Backbone Modification of a Parathyroid Hormone Receptor-1 Antagonist/Inverse AgonistSelective and Potent Proteomimetic Inhibitors of Intracellular Protein-Protein Interactions.β-Arrestin-Biased Agonists of the GLP-1 Receptor from β-Amino Acid Residue Incorporation into GLP-1 Analogues.Heterochiral Knottin Protein: Folding and Solution Structure.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.Evaluation of β-Amino Acid Replacements in Protein Loops: Effects on Conformational Stability and Structure.Development of Potent, Protease-Resistant Agonists of the Parathyroid Hormone Receptor with Broad β Residue Distribution.Heterogeneous-Backbone Foldamer Mimics of Zinc Finger Tertiary Structure.N-Gemini peptides: cytosolic protease resistance via N-terminal dimerization of unstructured peptides.Self-assembly of diphenylalanine backbone homologues and their combination with functionalized carbon nanotubes.
P2860
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P2860
Backbone modification of a polypeptide drug alters duration of action in vivo.
description
2014 nî lūn-bûn
@nan
2014 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
Backbone modification of a polypeptide drug alters duration of action in vivo.
@ast
Backbone modification of a polypeptide drug alters duration of action in vivo.
@en
Backbone modification of a polypeptide drug alters duration of action in vivo.
@nl
type
label
Backbone modification of a polypeptide drug alters duration of action in vivo.
@ast
Backbone modification of a polypeptide drug alters duration of action in vivo.
@en
Backbone modification of a polypeptide drug alters duration of action in vivo.
@nl
prefLabel
Backbone modification of a polypeptide drug alters duration of action in vivo.
@ast
Backbone modification of a polypeptide drug alters duration of action in vivo.
@en
Backbone modification of a polypeptide drug alters duration of action in vivo.
@nl
P2093
P2860
P356
P1433
P1476
Backbone modification of a polypeptide drug alters duration of action in vivo.
@en
P2093
Akira Maeda
Ross W Cheloha
Samuel H Gellman
Thomas Dean
Thomas J Gardella
P2860
P2888
P304
P356
10.1038/NBT.2920
P577
2014-06-15T00:00:00Z