Sentence examples for prp 1 from inspiring English sources

Secondary antibodies (Dako, Melbourne, VIC, Australia) were used at 1 in 5000 anti-rabbit (SOD1, SOD2), 1 in 10,000 anti-rabbit (PrP), 1 in 2000 anti-mouse (Bcl-2) and 1 in 10,000 anti-mouse (β-tubulin).

Cells were cultured with or without 1 × 10−7  M GH-releasing factor (GHRF), 2 × 10−7  M PRL-releasing peptide (PRP), 1 × 10−7  M LH-releasing hormone (LHRH), 1 × 10−7  M thyrotropin-releasing hormone (TRH), and 1 × 10−7  M corticotropin-releasing hormone (CRH) for 24 h.

The present authors previously performed studies to evaluate this clinical application of PRP, and recorded safety and interesting findings [ 31- 34]: the first one was a prospective study published in 2009 [ 31] on 91 patients (for a total of 115 knees) treated with three injections of PRP (1 every 3 weeks).

Prion diseases, such as bovine spongiform encephalopathy (BSE) in cattle, scrapie in sheep, and Creutzfeldt-Jakob disease (CJD) in humans, are fatal, transmissible, neurodegenerative disorders associated with the aggregation of an infectivity-associated isoform (PrPSc) of the cellular prion protein (PrP) (1 ).

Accordingly, caries resistant subjects coincided with increased adhesion of commensal Actinomyces and the highly prevalent allelic PRP variants PRP-1 and PRP-2 [ 10].

However, under hypoxic conditions, doxorubicin-suppressed HIF-1α attenuated the inhibitory effect on neuron cell death mediated by PrP (106 126).

The wound closure was facilitated by PRP (2 %) and PRF preparations (2 %), but not PPP preparations (2 %).

WBCs were similarly concentrated in these platelet-concentrated preparations (PRP: 5.51-fold, A-PRF: 11.87-fold, CGF: 8.63-fold).

Using baculovirus expression system, wild-type hamster (HaPrP) and human PrP (HuPrP), as well as D178N mutated human PrP (HuPrPm178) were expressed in HIS-fusion form.

A well-known example for the former is the transmissible spongiform encephalopathy (TSE), a group of fatal neurodegenerative diseases caused by misfolding of the prion protein (PrP) [1], [2], [3].

Under conditions in which PrPC exists as a detergent-soluble monomer and is completely degraded by the non-specific protease, proteinase K (PK), PrPSc exists in an aggregated form with the C-terminal two thirds of the protein showing marked resistance to proteolytic degradation leading to the generation of amino-terminally truncated fragments of di-, mono- and non-glycosylated PrP [1], [7].