about
Structure-Guided Rational Design of α/β-Peptide Foldamers with High Affinity for BCL-2 Family Prosurvival ProteinsTargeting diverse protein-protein interaction interfaces with α/β-peptides derived from the Z-domain scaffold.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.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.Molecular and Physiological Characterization of a Receptor for d-Amino Acid-Containing Neuropeptides.Conformational investigation of the structure-activity relationship of GdFFD and its analogues on an achatin-like neuropeptide receptor of Aplysia californica involved in the feeding circuitAplysia allatotropin-related peptide and its newly identified d-amino acid-containing epimer both activate a receptor and a neuronal targetDifferential Post-Translational Amino Acid Isomerization Found among Neuropeptides in Aplysia californica
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description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
James W Checco
@ast
James W Checco
@en
James W Checco
@es
James W Checco
@nl
type
label
James W Checco
@ast
James W Checco
@en
James W Checco
@es
James W Checco
@nl
prefLabel
James W Checco
@ast
James W Checco
@en
James W Checco
@es
James W Checco
@nl
P106
P31
P496
0000-0003-1165-6163