D. Pinon

Ruben Abagyan, Laurence J Miller, Patrick M Sexton, 2012, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

Interaction among four residues distributed through the secretin pharmacophore and a focused region of the secretin receptor amino terminus.

T. Lybrand, Zhijun Li, Mengwei Zang, 2002, Molecular endocrinology.

Identification of Two Pairs of Spatially Approximated Residues within the Carboxyl Terminus of Secretin and Its Receptor*

Y. Asmann, Mengwei Zang, L. Miller, 2000, The Journal of Biological Chemistry.

Role of Receptor Phosphorylation in Desensitization and Internalization of the Secretin Receptor*

L. Miller, M. Holtmann, D. Pinon, 1996, The Journal of Biological Chemistry.

Physicochemical determinants in hepatic extraction of small peptides

N. LaRusso, L. Miller, L. Kost, 1990, Hepatology.

Differential docking of high-affinity peptide ligands to type A and B cholecystokinin receptors demonstrated by photoaffinity labeling.

L. Miller, M. Dong, D. Pinon, 2005, Biochemistry.

Refinement of the conformation of a critical region of charge-charge interaction between cholecystokinin and its receptor.

T. Lybrand, L. Miller, D. Pinon, 2002, Molecular pharmacology.

Importance of each residue within secretin for receptor binding and biological activity.

L. Miller, A. Bordner, M. Dong, 2011, Biochemistry.

Spatial Approximation between the Amino Terminus of a Peptide Agonist and the Top of the Sixth Transmembrane Segment of the Secretin Receptor*

T. Lybrand, Zhijun Li, L. Miller, 2004, Journal of Biological Chemistry.

Regulation of lateral mobility and cellular trafficking of the CCK receptor by a partial agonist.

L. Miller, T. Burghardt, D. Pinon, 1999, American journal of physiology. Cell physiology.

Regulation of lateral mobility and cellular trafficking of the CCK receptor by a partial agonist.

L. Miller, T. Burghardt, D. Pinon, 1999, The American journal of physiology.

Spatial approximation between a photolabile residue in position 13 of secretin and the amino terminus of the secretin receptor.

T. Lybrand, Zhijun Li, Mengwei Zang, 2003, Molecular pharmacology.

Differential spatial approximation between secretin and its receptor residues in active and inactive conformations demonstrated by photoaffinity labeling.

L. Miller, M. Dong, N. Muthukumaraswamy, 2006, Molecular endocrinology.

Importance of the Amino Terminus in Secretin Family G Protein-coupled Receptors

L. Miller, M. Dong, D. Pinon, 2004, Journal of Biological Chemistry.

Spatial Approximations between Residues 6 and 12 in the Amino-terminal Region of Glucagon-like Peptide 1 and Its Receptor

Laurence J Miller, Maoqing Dong, L. Miller, 2010, The Journal of Biological Chemistry.

Molecular Basis of Glucagon-like Peptide 1 Docking to Its Intact Receptor Studied with Carboxyl-terminal Photolabile Probes*

Laurence J Miller, Maoqing Dong, L. Miller, 2009, The Journal of Biological Chemistry.

Spatial Approximation between Secretin Residue Five and the Third Extracellular Loop of Its Receptor Provides New Insight into the Molecular Basis of Natural Agonist Binding

R. Abagyan, P. Sexton, P. Lam, 2008, Molecular Pharmacology.

Insights into the structure and molecular basis of ligand docking to the G protein-coupled secretin receptor using charge-modified amino-terminal agonist probes.

L. Miller, M. Dong, D. Pinon, 2005, Molecular endocrinology.

Development of a biologically active secretin analogue incorporating a radioiodinatable photolabile p-(4-hydroxybenzoyl)phenylalanine in position 10

L. Miller, M. Dong, D. Pinon, 2002, Regulatory Peptides.

Identification of Peptide Ligand-binding Domains within the Human Motilin Receptor Using Photoaffinity Labeling*

L. Miller, B. Coulie, B. Matsuura, 2001, The Journal of Biological Chemistry.

Refinement of the Structure of the Ligand-occupied Cholecystokinin Receptor Using a Photolabile Amino-terminal Probe*

T. Lybrand, L. Miller, E. Hadac, 2001, The Journal of Biological Chemistry.

Identification of an Interaction between Residue 6 of the Natural Peptide Ligand and a Distinct Residue within the Amino-terminal Tail of the Secretin Receptor*

L. Miller, Yan Wang, M. Dong, 1999, The Journal of Biological Chemistry.

Direct Identification of a Second Distinct Site of Contact between Cholecystokinin and Its Receptor*

T. Lybrand, L. Miller, E. Hadac, 1998, The Journal of Biological Chemistry.

Refinement of the pharmacophore of an agonist ligand of the secretin receptor using conformationally constrained cyclic hexapeptides

L. Miller, A. Bordner, M. Dong, 2010, Peptides.

Formyl peptide chemoattractants: a model of the receptor on rabbit neutrophils.

A. Day, H. Showell, R. Freer, 1982, Biochemistry.

Demonstration of a Direct Interaction between Residue 22 in the Carboxyl-terminal Half of Secretin and the Amino-terminal Tail of the Secretin Receptor Using Photoaffinity Labeling*

L. Miller, Yan Wang, M. Dong, 1999, The Journal of Biological Chemistry.

Use of multidimensional fluorescence resonance energy transfer to establish the orientation of cholecystokinin docked at the type A cholecystokinin receptor.

L. Miller, K. Harikumar, D. Pinon, 2008, Biochemistry.

Measurement of intermolecular distances for the natural agonist Peptide docked at the cholecystokinin receptor expressed in situ using fluorescence resonance energy transfer.

T. Lybrand, L. Miller, K. Harikumar, 2004, Molecular pharmacology.

Relationship Between Native and Recombinant Cholecystokinin Receptors: Role of Differential Glycosylation

L. Miller, D. Pinon, R. Dougherty, 1996, Pancreas.

Elucidation of the active conformation of the amino terminus of receptor-bound secretin using intramolecular disulfide bond constraints.

L. Miller, A. Bordner, M. Dong, 2010, Bioorganic & medicinal chemistry letters.

Secretin Occupies a Single Protomer of the Homodimeric Secretin Receptor Complex

R. Abagyan, P. Sexton, P. Lam, 2010, The Journal of Biological Chemistry.

Molecular Approximations between Residues 21 and 23 of Secretin and Its Receptor: Development of a Model for Peptide Docking with the Amino Terminus of the Secretin Receptor

R. Abagyan, P. Sexton, P. Lam, 2007, Molecular Pharmacology.

Erratum: Spatial approximation between a photolabile residue in position 13 of secretin and the amino terminus of the secretin receptor (Molecular Pharmacology (2003) 63 (993-1001))

T. Lybrand, Zhijun Li, Mengwei Zang, 2003 .

Characterization of Protein Serine/Threonine Phosphatases in Rat Pancreas and Development of an Endogenous Substrate‐Specific Phosphatase Assay

L. Miller, M. Lutz, D. Pinon, 1994, Pancreas.

Development of magnetic beads for rapid and efficient metal-chelate affinity purifications.

L. Miller, D. Pinon, Z Ji, 1996, Analytical biochemistry.

Molecular Basis of Secretin Docking to Its Intact Receptor Using Multiple Photolabile Probes Distributed throughout the Pharmacophore*

R. Abagyan, P. Sexton, P. Lam, 2011, The Journal of Biological Chemistry.