Site-specific PEGylation of exenatide analogues markedly improved their glucoregulatory activity

Exendin-4 increases blood glucose levels acutely in rats by activation of the sympathetic nervous system

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The major determinant of exendin-4/glucagon-like peptide 1 differential affinity at the rat glucagon-like peptide 1 receptor N-terminal domain is a hydrogen bond from SER-32 of exendin-4

(2010) RJ Mann et al.   BRITISH JOURNAL OF PHARMACOLOGY

High-Purity Discrete PEG-Oligomer Crystals Allow Structural Insight

(2009) Alister C. French et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

Patient characteristics, drug adherence patterns, and hypoglycemia costs for patients with type 2 diabetes mellitus newly initiated on exenatide or insulin glargine

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PEG-modified biopharmaceuticals

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Crystal Structure of the Ligand-bound Glucagon-like Peptide-1 Receptor Extracellular Domain

(2008) Steffen Runge et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

The Pharmacology of PEGylation: Balancing PD with PK to Generate Novel Therapeutics

(2008) C.Simone Fishburn   JOURNAL OF PHARMACEUTICAL SCIENCES

Site-specific modification and PEGylation of pharmaceutical proteins mediated by transglutaminase

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