https://nova.newcastle.edu.au/vital/access/ /manager/Index ${session.getAttribute("locale")} 5 https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:46767 HIST1H3B/C and H3F3A), altering the epigenetic landscape of primitive oligodendrocyte or astrocyte precursor cells of the pontine region of the brainstem. Lysine‐to‐methionine point mutations at amino acid 27 (H3K27M) co‐occur with alterations in signaling genes, including the receptor tyrosine kinases (PDGFR/KIT/VEGFR/MET/EGFR), activin A receptor (ACVR1), intracellular kinases (PI3K/AKT/mTOR), cyclin‐dependent kinases (CDKs1/4/6), transcriptional regulators (MYCN), and tumor suppressors (PTEN/TP53). This cooperation drives gene expression signatures that inhibit cellular differentiation (ID1/2, Hedgehog) and promotes malignant transformation. Unique to DIPG, is the frequency of co‐occurring sets of genomic insults. However, mapping of the oncogenic signaling pathways activated in response to recurring mutations is unresolved. Herein, known oncogenic signal pathways activated in response to recurring somatic mutations and gene amplifications in DIPG are reviewed. Additionally, an important role for high‐resolution quantitative proteomics/phosphoproteomics in the characterization of signaling cascades are highlighted. These regulate the cell cycle, epigenetics and anti‐apoptotic processes, information critical for the development of improved treatment strategies for DIPG.]]> Wed 30 Nov 2022 11:45:04 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:51195 Wed 28 Feb 2024 15:48:19 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:52876 Wed 28 Feb 2024 11:01:07 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:50443 Wed 26 Jul 2023 08:33:30 AEST ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:46956 Wed 19 Jul 2023 14:21:24 AEST ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:2940 Wed 11 Apr 2018 16:05:16 AEST ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:28369 Wed 11 Apr 2018 14:08:08 AEST ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:25253 Wed 11 Apr 2018 11:30:48 AEST ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:2982 Wed 11 Apr 2018 11:06:16 AEST ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:15406 Wed 11 Apr 2018 10:30:28 AEST ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:14499 Wed 11 Apr 2018 10:21:55 AEST ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:41655 Wed 10 Aug 2022 10:07:33 AEST ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:28661 Wed 09 Mar 2022 16:03:03 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:50850 Wed 09 Aug 2023 09:39:07 AEST ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:35918 Wed 07 Jul 2021 12:41:58 AEST ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:46915 Wed 07 Dec 2022 09:37:40 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:54081 Wed 06 Mar 2024 14:35:48 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:43968 Wed 05 Oct 2022 14:15:31 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:36671 Tue 23 Jun 2020 12:57:42 AEST ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:51128 6,000 proteins, encompassing the selective loss and gain of several hundred proteins. Further, we demonstrate epididymal-driven activation of RHOA-mediated signaling pathways is an important component of sperm maturation. These data contribute molecular insights into the complexity of proteomic changes associated with epididymal sperm maturation.]]> Tue 22 Aug 2023 15:52:22 AEST ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:43823 Tue 04 Oct 2022 11:04:24 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:33031 Tue 03 Sep 2019 17:55:22 AEST ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:45231 Thu 27 Oct 2022 12:56:33 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:49981 Thu 22 Jun 2023 11:59:40 AEST ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:31076 Thu 13 Jan 2022 10:30:18 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:47101 Thu 06 Jul 2023 14:06:28 AEST ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:36366 Thu 02 Apr 2020 13:13:30 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:8340 Sat 24 Mar 2018 10:47:11 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:8464 Sat 24 Mar 2018 08:42:09 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:15320 Sat 24 Mar 2018 08:26:36 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:13040 Sat 24 Mar 2018 08:16:38 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:9963 Sat 24 Mar 2018 08:14:26 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:17528 Sat 24 Mar 2018 08:03:55 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:5193 Sat 24 Mar 2018 07:47:44 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:27299 Sat 24 Mar 2018 07:38:31 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:27778 Staphylococcus aureus is thought to be due to its extraordinary capacity to rapidly adapt to changes in environmental conditions. This study was carried out to investigate whether the cytoplasmic profiles of metabolites and proteins of S. aureus were altered in response to prolonged exposure to cold stress. Metabolic profiling and proteomics were used to characterise alterations in cytoplasmic proteins and metabolites in cells from the mid-exponential phase of growth under ideal conditions at 37 °C and compared with equivalent cells exposed to prolonged cold stress for 2 weeks at 4 °C. Principle component analysis (PCA) of the metabolomic and proteomic data indicated that, at the mid-exponential phase of growth, prolonged cold stress conditions generated cells with different metabolite and protein profiles compared with those grown at 37 °C. Nine ribosomal proteins and citric acid were substantially elevated in the cytoplasmic fractions from the cells adapted to cold-stress but most amino acids showed a reduction in their concentration in cold-stressed samples. The data provided strong evidence supporting the hypothesis that specific changes in metabolic homeostasis and protein composition were critical to the adaptive processes required for survival under cold stress. Biological significance: Work in our laboratory has shown that prolonged exposure of S. aureus to cold stress can result in the formation of small colony variants (SCVs) associated with significant alterations in the cell wall composition [8]. Further studies revealed that S. aureus altered cell size and cell wall thickness in response to exposure to cold temperatures, alterations in pH and exposure to antibiotics [10]. The current study has utilised the prolonged exposure to cold stress as a model system to explore changes in the proteome and associated metabolic homeostasis following environmental challenges. The study provides an improved understanding of how S. aureus adapts to the changing environment whilst in transition between human hosts. The results indicated an unexpected production of 9 ribosomal proteins and citric acid in response to cold stress suggesting specific survival roles for these proteins and citric acid as an adaptation mechanism for empowering survival under these conditions.]]> Sat 24 Mar 2018 07:37:06 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:25432 Sat 24 Mar 2018 07:31:54 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:28945 Sat 24 Mar 2018 07:31:25 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:27256 Sat 24 Mar 2018 07:29:12 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:27253 Sat 24 Mar 2018 07:29:09 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:22257 Sat 24 Mar 2018 07:17:39 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:52857 Mon 30 Oct 2023 10:00:44 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:38436 Mon 29 Jan 2024 18:01:15 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:44457 p < 0.05, n = 5). Relative elongation of axial length and the vitreous chamber depth were also observed. Using pooled samples from all individuals (n = 10) to build a species-specific retinal ion library for SWATH analysis, 3202 non-redundant proteins (with 24,616 peptides) were identified at 1% global FDR. For quantitative analysis, the 10 individual retinal samples (5 pairs) were analyzed using a high resolution Triple-TOF 6600 mass spectrometry (MS) with technical replicates. In total, 37 up-regulated and 21 down-regulated proteins were found significantly changed after LIM treatment (log2 ratio (T/C) > 0.26 or < −0.26; p ≤ 0.05). Data are accepted via ProteomeXchange with identifier PXD025003. Through Ingenuity Pathways Analysis (IPA), “lipid metabolism” was found as the top function associated with the differentially expressed proteins. Based on the protein abundance and peptide sequences, expression patterns of two regulated proteins (SLC6A6 and PTGES2) identified in this pathway were further successfully validated with high confidence (p < 0.05) using a novel Multiple Reaction Monitoring (MRM) assay on a QTRAP 6500+ MS. In summary, through an integrated discovery and targeted proteomic approach, this study serves as the first report to detect and confirm novel retinal protein changes and significant biological functions in the early LIM mammalian guinea pigs. The study provides new workflow and insights for further research to myopia control.]]> Mon 24 Jul 2023 18:11:16 AEST ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:54722 Mon 11 Mar 2024 11:58:32 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:55064 Mon 08 Apr 2024 12:38:40 AEST ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:48007 Mon 01 May 2023 15:17:16 AEST ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:48239 Mon 01 May 2023 14:49:55 AEST ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:30276 Fri 24 Aug 2018 09:02:03 AEST ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:47370 Fri 13 Jan 2023 15:04:37 AEDT ]]> https://nova.newcastle.edu.au/vital/access/ /manager/Repository/uon:41763 p < 0.001), increased further following acrosome reaction (p < 0.01), and was localized to the equatorial region of the sperm head. Testisin was also detected in luminal fluid within the caput and corpus regions of the epididymis, epididymal spermatozoa, and epididymal epithelial cells. Testisin formed several multiprotein complexes; co‐immunoprecipitation revealed interactions of testisin with a multitude of zona pellucida‐binding proteins, including ZPBP, ZAN, acrosin, several heat‐shock proteins, and components of the TCP1 complex. Conclusion: Testisin appears to form part of the zona pellucida‐binding complex in stallion spermatozoa and may be involved in the proteolytic cascade that prepares the sperm surface for interaction with the oocyte.]]> Fri 12 Aug 2022 11:49:34 AEST ]]>