A. Lourbakos

发表

Evidence for the activation of PAR‐2 by the sperm protease, acrosin: expression of the receptor on oocytes

Roy Jones, D. Johnson, V. Ramakrishnan, 2000, FEBS letters.

Expression of protease-activated receptor-2 by osteoblasts.

R. Pike, E. Mackie, A. Jenkins, 2000, Bone.

Preferential Efflux of Phytosterols over Cholesterol from Macrophages

G. Duchateau, E. Trautwein, E. Tareilus, 2007, Lipids.

Arginine-Specific Protease fromPorphyromonas gingivalis Activates Protease-Activated Receptors on Human Oral Epithelial Cells and Induces Interleukin-6 Secretion

M. D'Andrea, J. Potempa, R. Pike, 2001, Infection and Immunity.

A randomized placebo-controlled phase 3 trial of an antisense oligonucleotide, drisapersen, in Duchenne muscular dystrophy

J. J. Padilla, C. Palermo, M. Pane, 2018, Neuromuscular Disorders.

Activation of protease-activated receptors by gingipains from Porphyromonas gingivalis leads to platelet aggregation: a new trait in microbial pathogenicity.

J. Potempa, R. Pike, J. Travis, 2001, Blood.

Cleavage and activation of proteinase‐activated receptor‐2 on human neutrophils by gingipain‐R from Porphyromonas gingivalis

J. Potempa, R. Pike, E. Mackie, 1998, FEBS letters.

P1.6 The incidence of revertant and trace dystrophin expression in muscle biopsies of Duchenne Muscular Dystrophy patients with different exon deletions

C. Beekman, G. Campion, A. Janson, 2011, Neuromuscular Disorders.

Safety and efficacy of drisapersen for the treatment of Duchenne muscular dystrophy (DEMAND II): an exploratory, randomised, placebo-controlled phase 2 study

V. Ricotti, F. Muntoni, L. Servais, 2014, The Lancet Neurology.

A novel fluorescent marker for assembled mitochondria ATP synthase of yeast

M. Prescott, M. Bateson, P. Nagley, 1997, FEBS letters.

Protein hydrolysates induce CCK release from enteroendocrine cells and act as partial agonists of the CCK1 receptor.

C. Gerhardt, J. Schwarz, M. Foltz, 2008, Journal of agricultural and food chemistry.

Dystrophin quantification

F. Muntoni, K. Flanigan, K. Anthony, 2014, Neurology.

Long-Term Efficacy, Safety, and Pharmacokinetics of Drisapersen in Duchenne Muscular Dystrophy: Results from an Open-Label Extension Study

N. Goemans, M. Van den Hauwe, J. V. van Deutekom, 2016, PloS one.

A Sensitive, Reproducible and Objective Immunofluorescence Analysis Method of Dystrophin in Individual Fibers in Samples from Patients with Duchenne Muscular Dystrophy

C. Beekman, J. V. van Deutekom, G. Campion, 2014, PloS one.

Hypersensitive mousetraps, alpha1-antitrypsin deficiency and dementia.

D. Lomas, D. Belorgey, S. Cumming, 2002, Biochemical Society transactions.

Hypersensitive mousetraps, α1-antitrypsin deficiency and dementia

D. Lomas, D. Belorgey, S. Cumming, 2001 .

Universal Updated Phase 1 Data Validates the Feasibility of Allogeneic Anti-BCMA ALLO-715 Therapy for Relapsed/Refractory Multiple Myeloma

S. Jagannath, D. Siegel, P. Hari, 2021, Blood.

Placebo‐controlled Phase 2 Trial of Drisapersen for Duchenne Muscular Dystrophy

Ching H. Wang, B. Wong, A. Pestronk, 2018, Annals of clinical and translational neurology.

Evaluation of serum MMP-9 as predictive biomarker for antisense therapy in Duchenne

P. Nilsson, F. Muntoni, R. Wolterbeek, 2017, Scientific Reports.

Activation of protease-activated receptors by gingipains from Porphyromonas gingivalis leads to platelet aggregation: a new trait in microbial pathogenicity.

J. Potempa, R. Pike, J. Travis, 2001, Blood.

A randomized placebo-controlled phase 3 trial of an antisense oligonucleotide, drisapersen, in Duchenne muscular dystrophy

C. Palermo, M. Pane, E. Mercuri, 2018, Neuromuscular Disorders.

Disruption of a gene in Saccharonomyces cerevisiae encoding a putative homologue of subunit g of mammalian ATP synthase

G. Boyle, M. Prescott, P. Nagley, 1997 .