ORCID Profile
0000-0001-9733-2404
Current Organisations
The University of Edinburgh
,
UCL Institute of Neurology, University College London
,
University of Dundee
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Publisher: Oxford University Press (OUP)
Date: 28-10-2003
DOI: 10.1093/HMG/DDH012
Publisher: Cold Spring Harbor Laboratory
Date: 25-07-2023
DOI: 10.1101/2023.07.25.550405
Abstract: To facilitate analysis and sharing of mass spectrometry (MS)-based proteomics data we created tools called CURTAIN ( curtain.proteo.info ) and CURTAIN-PTM ( curtainptm.proteo.info ). These enable the non-MS expert to interactively peruse volcano plots deconvolute primary experimental data to in idual replicates that can be visualized in bar charts or violin plots allowing statistical analysis and export of plots in SVG format. They also permit assessment of experimental quality by correlation matrix and profile plot. Within CURTAIN, the user can analyze domain structure, AlphaFold predicted structure, reported interactors, relative expression, disease and pharmaceutical links, and mutagenesis information on all selected hits. Moreover, CURTAIN-PTM permits the comparison of all identified PTM sites on protein(s) of interest with PTM information contained within selected databases. For phosphorylation site analysis CURTAIN-PTM links with the kinase library to predict upstream kinases that phosphorylate sites of interest. We provide ex les of the utility of CURTAIN and CURTAIN-PTM in analyzing how targeted degradation of the PPM1H Rab phosphatase that counteracts the Parkinson’s LRRK2 kinase impacts cellular protein levels and phosphorylation sites. We reanalyzed a ubiquitylation dataset, characterizing the PINK1-Parkin pathway activation in primary neurons, revealing new data of interest not highlighted previously. CURTAIN and CURTAIN-PTM are free to use and open-source and will enable researchers to share and maximize the analysis and impact of their proteomics data. We advocate that differential expression proteomic data should be published containing a shareable CURTAIN web-link, allowing readers to better explore their data. To enable non-experts to better share and explore mass spectrometry data, we have generated using open-source software, interactive tools termed CURTAIN and CURTAIN-PTM. These tools enable users’ to save their analysis sessions with a sharable unique web-link, enabling other researchers to visualize and further analyze these datasets. These links can also be reported in publications allowing readers to further survey the reported data. We discuss benefits for the research community of publishing proteomic data containing a shareable web-link.
Publisher: Wiley
Date: 10-2006
DOI: 10.1002/ANA.20960
Abstract: To investigate the significance of PINK1 mutations in sporadic Parkinson's disease (PD). We determined the frequency of PINK1 mutations by direct sequencing in a large series of PD patients with apparently sporadic disease (n = 768). Twelve heterozygous mutations were identified, nine in PD patients and three in control subjects. Given the difficulty in interpreting the pathogenic significance of the heterozygous mutations that have already been reported in parkin and DJ-1, we first determined the frequency of heterozygous PINK1 mutations in the general population by sequencing a large number of control subjects (n = 768), then subsequently assessed their functional significance by examining their effects on stress-induced alterations to the mitochondrial membrane potential (DeltaPsim). We demonstrate an enrichment of heterozygous mutations in sporadic PD patients compared with matched control subjects (1.2% in PD vs 0.4% in control subjects). Furthermore, we show that they adversely affect DeltaPsim in a similar way to the familial G309D mutation. Although it remains difficult to conclusively demonstrate the pathogenicity of heterozygous mutations, the results of this study and the previously reported subclinical nigrostriatal dysfunction in carriers of heterozygous PINK1 mutations suggest the possibility that these heterozygous mutations are a significant risk factor in the development of later onset PD.
Publisher: Elsevier BV
Date: 11-2005
DOI: 10.1016/J.NBD.2005.03.021
Abstract: Lewy bodies (LBs) are the characteristic inclusions of Parkinson's disease brain but the mechanism responsible for their formation is obscure. Lewy bodies (LBs) are composed of a number of proteins of which alpha-synuclein (alpha-SYN) is a major constituent. In this study, we have investigated the distribution patterns of synphilin-1 and parkin proteins in control and sporadic PD brain tissue by immunohistochemistry (IH), immunoblotting, and immunoelectron microscopy (IEM). We demonstrate the presence of synphilin-1 and parkin in the central core of a majority of LBs using IH and IEM. Using IH, we show an overlapping distribution profile of the two proteins in central neurons. Additionally, we show sensitivity of both endogenous synphilin-1 and parkin to proteolytic dysfunction and their co-localization in aggresomes formed in response to the proteasome inhibitor MG-132. We confirm that synphilin-1 and parkin are components of majority of LBs in Parkinson's disease and that both proteins are susceptible to proteasomal degradation.
Location: United Kingdom of Great Britain and Northern Ireland
Location: No location found
Location: United Kingdom of Great Britain and Northern Ireland
Location: United Kingdom of Great Britain and Northern Ireland
No related grants have been discovered for Miratul Muqit.