@article {2360,
	title = {Metabolic abnormalities in fronto-striatal-thalamic white matter tracts in schizophrenia},
	journal = {Schizophrenia Research},
	volume = {109},
	number = {1-3},
	year = {2009},
	note = {ISI Document Delivery No.: 437VZTimes Cited: 3Cited Reference Count: 52Beasley, Clare L. Dwork, Andrew J. Rosoklija, Gorazd Mann, J. John Mancevski, Branislav Jakovski, Zlatko Davceva, Natasa Tait, Andrew R. Straus, Suzana K. Honer, William G.},
	month = {Apr},
	pages = {159-166},
	type = {Article},
	abstract = {{The anterior limb of the internal capsule (ALIC) is the major white matter tract providing reciprocal connections between the frontal cortex, striatum and thalamus. Mounting evidence suggests that this tract may be affected in schizophrenia, with brain imaging studies reporting reductions in white matter volume and density, changes in fractional anisotropy and reduced asymmetry. However, the molecular correlates of these deficits are currently unknown. The aim of this study was to identify alterations in protein and metabolite levels in the ALIC in schizophrenia. Samples were obtained post-mortem from individuals with schizophrenia (n = 15) and non-psychiatric controls (n = 13). Immunoreactivity for the myelin-associated protein myelin basic protein (MBP), and the axonal-associated proteins phosphorylated neurofilament and SNAP-25 was measured by enzyme-linked immunoadsorbent assay (ELISA). Metabolite concentrations were quantified by proton nuclear magnetic resonance (H-1 NMR) spectroscopy. Levels of myelin- or axonal-associated proteins did not differ between groups. Overall differences in metabolite concentrations were observed between the two groups (MANOVA F=2.685},
	keywords = {ANTERIOR CINGULATE CORTEX, Axon, BASAL GANGLIA, composition, CORPUS-CALLOSUM, EXPRESSION, fiber, HUMAN INTERNAL CAPSULE, Internal capsule, LACTATE, MENTAL-ILLNESS, METABOLITE, myelin, POLARIZED-LIGHT, POSTMORTEM BRAINS, PREFRONTAL CORTEX, SEVERE},
	isbn = {0920-9964},
	url = {<Go to ISI>://000265516300023},
	author = {Beasley, C. L. and Dwork, A. J. and Rosoklija, G. and Mann, J. J. and Mancevski, B. and Jakovski, Z. and Davceva, N. and Tait, A. R. and Straus, S. K. and Honer, W. G.}
}
@article {2277,
	title = {Phosphorylation of U24 from Human Herpes Virus type 6 (HHV-6) and its potential role in mimicking myelin basic protein (MBP) in multiple sclerosis},
	journal = {Febs Letters},
	volume = {582},
	number = {18},
	year = {2008},
	note = {ISI Document Delivery No.: 332UKTimes Cited: 2Cited Reference Count: 31Tait, Andrew R. Straus, Suzana K.},
	month = {Aug},
	pages = {2685-2688},
	type = {Article},
	abstract = {Myelin basic protein (MBP) from multiple sclerosis ( MS) patients contains lower levels of phosphorylation at Thr97 than normal individuals. The significance of phosphorylation at this site is not fully understood, but it is proposed to play a role in the normal functioning of MBP. Human Herpesvirus Type 6 encodes the protein U24, which has tentatively been implicated in the pathology of MS. U24 shares a 7 amino acid stretch encompassing the Thr97 phosphorylation site of MBP: PRTPPPS. We demonstrate using a combination of mass spectrometry, thin layer chromatography and autoradiography, that U24 can be phosphorylated at the equivalent threonine. Phospho-U24 may confound signalling or other pathways in which phosphorylated MBP may participate, precipitating a pathological process.},
	keywords = {BINDING, EXPRESSION, HUMAN-HERPESVIRUS-6, IDENTIFICATION, KINASE, MEMBRANE MICRODOMAINS, mimicry, myelin, PHOSPHORYLATION, POSTTRANSLATIONAL MODIFICATIONS, SITE, T-ANTIGEN, U24},
	isbn = {0014-5793},
	url = {<Go to ISI>://000258108400002},
	author = {Tait, A. R. and Straus, S. K.}
}
