(PDF) A Peptoid Antagonist of VEGF Receptor 2 Recognizes a

A Peptoid Antagonist of VEGF Receptor 2 Recognizes a ‘Hotspot’ in the Extracellular Domain Distinct From the Hormone-Binding Site

Bioorganic and Medicinal Chemistry - United Kingdom

doi 10.1016/j.bmc.2008.05.015

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Date

June 1, 2008

Authors

D. Gomika Udugamasooriya

Caroline Ritchie

Rolf A. Brekken

Thomas Kodadek

Publisher

Elsevier BV

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A Peptoid Antagonist of VEGF Receptor 2 Recognizes a ‘Hotspot’ in the Extracellular Domain Distinct From the Hormone-Binding Site

Bioorganic and Medicinal Chemistry - United Kingdom

doi 10.1016/j.bmc.2008.05.015

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

An Extended U2af65–rna-Binding Domain Recognizes the 3′ Splice Site Signal

Development of a Rat Parathyroid Hormone 2 Receptor Antagonist

Relative Antagonism of Mutants of the CGRP Receptor Extracellular Loop 2 Domain (ECL2) Using a Truncated Competitive Antagonist (CGRP8–37): Evidence for the Dual Involvement of ECL2 in the Two-Domain Binding Model

Inhibition of Tumor Metastasis by a Growth Factor Receptor Bound Protein 2 SRC Homology 2 Domain-Binding Antagonist

Tyrosine 220 in the 5th Transmembrane Domain of the Neuromedin B Receptor Is Critical for the High Selectivity of the Peptoid Antagonist PD168368

The Agonist Binding Site on the Bovine Bradykinin B2 Receptor Is Adjacent to a Sulfhydryl and Is Differentiated From the Antagonist Binding Site by Chemical Cross-Linking

Generalized Resistance to Thyroid Hormone Associated With a Mutation in the Ligand-Binding Domain of the Human Thyroid Hormone Receptor Beta.

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Photolabelling the Rat Urotensin II/GPR14 Receptor Identifies a Ligand-Binding Site in the Fourth Transmembrane Domain