U. Petäjä‐Repo

发表

Expression of the mature luteinizing hormone receptor in rodent urogenital and adrenal tissues is developmentally regulated at a posttranslational level.

U. Petäjä-Repo, H. Rajaniemi, Pirjo M. Apaja, 2005, Endocrinology.

Characterization of apela, a novel endogenous ligand of apelin receptor, in the adult heart

O. Vuolteenaho, J. Ulvila, U. Petäjä-Repo, 2015, Basic Research in Cardiology.

The endoplasmic reticulum Ca2+-pump SERCA2b interacts with G protein-coupled receptors and enhances their expression at the cell surface.

U. Petäjä-Repo, Piia Markkanen, J. Tuusa, 2007, Journal of molecular biology.

Cysteine 27 Variant of the δ-Opioid Receptor Affects Amyloid Precursor Protein Processing through Altered Endocytic Trafficking

H. Soininen, R. Tanzi, M. Hiltunen, 2011, Molecular and Cellular Biology.

Phe27Cys polymorphism of the human delta opioid receptor predisposes cells to compromised calcium signaling

J. Tuusa, U. Petäjä‐Repo, 2011, Molecular and Cellular Biochemistry.

Ecto-GPR37: a potential biomarker for Parkinson’s disease

P. Svenningsson, F. Ciruela, I. Ferrer, 2021, Translational neurodegeneration.

Internalization of N-formyl peptide chemotactic receptor-ligand complex by human neutrophils. The role of the receptor's 2-kDa external domain and carbohydrates.

U. Petäjä-Repo, H. Rajaniemi, J. Remes, 1994, Journal of receptor research.

Covalent cross-linking of radiolabeled N-formylated hexapeptide to its specific receptor on rat and human neutrophils: evidence for a ligand induced complex formation.

K. Keinänen, U. Petäjä-Repo, H. Rajaniemi, 1992, Journal of receptor research.

G Protein-Coupled Receptors in the Sweet Spot: Glycosylation and other Post-translational Modifications.

M. Rosenkilde, U. Petäjä-Repo, C. Goth, 2020, ACS pharmacology & translational science.

Pharmacological chaperones: a new twist on receptor folding.

D. Bichet, M. Bouvier, U. Petäjä-Repo, 2000, Trends in pharmacological sciences.

Ligands act as pharmacological chaperones and increase the efficiency of δ opioid receptor maturation

M. Bouvier, M. Hogue, S. Bhalla, 2002, The EMBO journal.

Pharmacological chaperones rescue cell-surface expression and function of misfolded V2 vasopressin receptor mutants.

S. Angers, D. Bichet, M. Bouvier, 2000, The Journal of clinical investigation.

The N-terminal domain of unknown function (DUF959) in collagen XVIII is intrinsically disordered and highly O-glycosylated.

T. Pihlajaniemi, P. Kursula, U. Petäjä-Repo, 2018, The Biochemical journal.

Opioid Receptor Pharmacological Chaperones Act by Binding and Stabilizing Newly Synthesized Receptors in the Endoplasmic Reticulum*

U. Petäjä-Repo, Tarja T. Leskelä, Piia Markkanen, 2007, Journal of Biological Chemistry.

Rat and human neutrophil N-formyl-peptide chemotactic receptors. Species difference in the glycosylation of similar 35-38 kDa polypeptide cores.

H. Rajaniemi, J. Remes, U. Petäjä‐Repo, 1991, The Biochemical journal.

Export from the Endoplasmic Reticulum Represents the Limiting Step in the Maturation and Cell Surface Expression of the Human δ Opioid Receptor*

M. Bouvier, M. Hogue, U. Petäjä-Repo, 2000, The Journal of Biological Chemistry.

Identification and Structural Characterization of the Neuronal Luteinizing Hormone Receptor Associated with Sensory Systems*

U. Petäjä-Repo, H. Rajaniemi, Kirsi Harju, 2004, Journal of Biological Chemistry.

Site-specific O-Glycosylation by Polypeptide N-Acetylgalactosaminyltransferase 2 (GalNAc-transferase T2) Co-regulates β1-Adrenergic Receptor N-terminal Cleavage*

C. Overall, Yoshiki Narimatsu, H. Clausen, 2017, The Journal of Biological Chemistry.

Targeting opioid receptors with pharmacological chaperones.

U. Petäjä-Repo, Jarkko J. Lackman, U. Petäjä‐Repo, 2014, Pharmacological research.

A homogeneous single-label quenching resonance energy transfer assay for a δ-opioid receptor-ligand using intact cells.

P. Hänninen, H. Härmä, U. Petäjä-Repo, 2013, The Analyst.

Human β1-Adrenergic Receptor Is Subject to Constitutive and Regulated N-terminal Cleavage*

U. Petäjä-Repo, J. Tuusa, E. Kumpula, 2010, The Journal of Biological Chemistry.

G Protein-Coupled Receptors in the Sweet Spot: Glycosylation and other Post-translational Modifications.

M. Rosenkilde, U. Petäjä-Repo, C. Goth, 2020, ACS Pharmacology & Translational Science.

Altered O-glycosylation of β1-adrenergic receptor N-terminal single-nucleotide variants modulates receptor processing and functional activity.

S. Vakhrushev, Katrine T. Schjoldager, Zilu Ye, 2024, The FEBS journal.

N-Glycan-dependent and -independent Quality Control of Human δ Opioid Receptor N-terminal Variants*

M. Bouvier, M. Hogue, U. Petäjä-Repo, 2014, The Journal of Biological Chemistry.

β-Adrenergic Agonists Mediate Enhancement of β1-Adrenergic Receptor N-terminal Cleavage and Stabilization In Vivo and In Vitro

J. Ulvila, U. Petäjä-Repo, H. Khan, 2013, Molecular Pharmacology.

N-Glycan-mediated Quality Control in the Endoplasmic Reticulum Is Required for the Expression of Correctly Folded δ-Opioid Receptors at the Cell Surface*

U. Petäjä-Repo, Piia Markkanen, U. Petäjä‐Repo, 2008, Journal of Biological Chemistry.

Significance of the carbohydrate moiety of the rat ovarian luteinizing-hormone/chorionic-gonadotropin receptor for ligand-binding specificity and signal transduction.

U. Petäjä-Repo, H. Rajaniemi, W. Merz, 1993, The Biochemical journal.

Site-specific O-glycosylation of N-terminal serine residues by polypeptide GalNAc-transferase 2 modulates human δ-opioid receptor turnover at the plasma membrane.

A. Halim, S. Vakhrushev, H. Clausen, 2018, Cellular signalling.

Genetic Variation in δ-Opioid Receptor Associates with Increased β- and γ-Secretase Activity in the Late Stages of Alzheimer's Disease.

H. Soininen, M. Hiltunen, S. Helisalmi, 2015, Journal of Alzheimer's disease : JAD.