G Cagney's research while affiliated with University College Dublin and other places

... To make our findings accessible to other researchers, we have submitted the data from immunohistochemical labeling of KIFAP3 to Human Proteinpedia (HUPA; http://www.humanproteinpedia. org) [22]. The expression of KIFAP3 in normal breast epithelium (http://www.humanproteinpedia.org/Experimental_details?exp_ id=TE-142795) and in breast cancer (http://www.humanproteinpedia. ...

... In addition, the post synaptic density (PSD) protein SHANK3 was significantly increased (↑1.68 fold) in expression. SHANK3 is a major susceptibility gene in schizophrenia (Gauthier et al., 2010) and we have recently observed decreased SHANK3 expression in the PSD in schizophrenia (Föcking et al., 2012). As disturbed CME and synaptic processes are core features in the pathophysiology of psychiatric disorders, this study provides further evidence that n-3 FA deficiency is a risk factor for schizophrenia. ...

... Bioinformatic analysis revealed that mutations in these proteins were related to 133 neurological and psychiatric diseases and were particularly enriched in neural phenotypes involving cognition and motor functions [52]. Moreover, 143 of 700 proteins identified from PSD fractions of anterior cingulate cortex were differentially expressed in patients with schizophrenia, implicating NMDA-interacting and endocytosis-related proteins in the pathophysiology of schizophrenia [53]. These authors also identified 288 differentially expressed proteins in bipolar disorder, highlighting the important role of synaptic function and energy pathways in psychiatric diseases [54]. ...

... Munc18-1 is a key regulatory protein of transmission and its physiological function has been increasingly studied (6). The abnormal expression of Munc18-1 is involved in the pathogenesis of various neurological diseases and is closely associated with epileptic encephalopathy, autism, schizophrenia (SCZ), Parkinson's disease, Alzheimer's disease (AD), multiple sclerosis (MS), Duchenne's muscular dystrophy and neuronal ceroid lipofuscinosis (Table I) (42)(43)(44)(45)(46)(47)(48)(49)(50). ...

... In addition, there are evidence of proteomic alterations related to other spliceosome proteins [61,63] and overall protein synthesis [64] in schizophrenia. These processes have been linked to control the proper formation of the myelin sheath by oligodendrocytes [65]. ...

... Moreover, 143 of 700 proteins identified from PSD fractions of anterior cingulate cortex were differentially expressed in patients with schizophrenia, implicating NMDA-interacting and endocytosis-related proteins in the pathophysiology of schizophrenia [53]. These authors also identified 288 differentially expressed proteins in bipolar disorder, highlighting the important role of synaptic function and energy pathways in psychiatric diseases [54]. The role of PSD components in neurodevelopmental and neurodegenerative disorders has also been investigated [55,56]. ...

... Autism and autism spectrum disorders are known to have some similarity with schizophrenia development mechanisms (Gao and Penzes, 2015). A number of studies have found the translation changes and the protein synthesis increase in the neuronal cells of the schizophrenia patients (Topol et al., 2015;Darby et al., 2016). A hypothesis was proposed that the rDNA CN, determining the quantity of available ribosomes in the dendrites, modulates the level of local dendritic translation and, therefore, may be considered a risk and severity factor of neuropsychiatric disorders caused by aberrant dendritic translation (Porokhovnik, 2019). ...

... Mass spectrometry is also used to identify phosphorylation events specific to mitosis and even specific to mitotic structures, such as the mitotic spindle, mitotic chromosomes and centrosomes (Dephoure et al., 2008;Daub et al., 2008;Olsen et al., 2010;Nousiainen et al., 2006;Ohta et al., 2016;Andersen et al., 2003;Syred et al., 2013;Özlü et al., 2010). Phosphorylated sites reported in various studies, are deposited in public databases, such as PHOSIDA (Gnad et al., 2011), PhosphoELM (Diella et al., 2008), Human Proteinpedia (HPRD1; Mathivanan et al., 2008) and PhosphoSitePlus (Hornbeck et al., 2015). Important limitations of typical mass spectrometry analysis in identifying phosphorylation in proteins are: whether there is a sufficient amount of certain phosphorylated peptides and whether a particular phosphorylation is stable enough during mass spectrometry to be identified ( Cantin and Yates, 2004). ...