University of Portsmouth APCs 2014

<p>This spreadsheet contains details of article processing charges (APCs) paid by the University of Portsmouth during 2014. The data is being collected as part of Jisc's APC data collection project to address the Total Cost of Ownership of scholarly communication (https://www.jisc-collections.ac.uk/Jisc-Monitor/APC-data-collection/) and has been released with permission of the University of Portsmouth Library.</p

University of Portsmouth APCs 2015 (Jan-June)

<p>This spreadsheet contains details of article processing charges (APCs) paid by the University of Portsmouth during the first half of 2015. The data is being collected as part of Jisc's APC data collection project to address the Total Cost of Ownership of scholarly communication (https://www.jisc-collections.ac.uk/Jisc-Monitor/APC-data-collection/).</p

Additional file 1: of Binary-state speciation and extinction method is conditionally robust to realistic violations of its assumptions

Speciation extinction simulation model. Source code (in C) for the simulation program used to generate the data used in this study. This file is also available via Dryad. (ZIP 12 kb

MAGE–KAP1 binding induces ZNF382 ubiquitination in HEK293T cells.

<p>HEK293T cells were transiently transfected with His tagged wild-type MAGE-C2 (WT), mutant (non-binding) MAGE-C2^{L152A L153A} , or empty vectors (Mock) and co-transfected with ZNF382, KAP1, and HA tagged ubiquitin. Cells were incubated for 5 hours in the presence of 25 µM MG132 (C2211, SIGMA). Top two panels: ZNF382 (around 55 kDa), MAGE-C2 (around 50 KD) and KAP1 (110 KD) were detected in whole lysates by immunoblotting with anti-KAP1 (upper panel) and anti-FLAG antibodies (lower panel). Third panel: His tagged ubiquitinated proteins were immunoprecipitated with anti-His and detected with anti-HA. High-molecular-weight ubiquitinated species were seen only in blots of cells transfected with both ZNF382 and MAGE-C2. Note that no ubiquitination occurred when wild type MAGE-C2 was replaced with MAGE-C2^{L152A L153A} which does not bind to KAP1, indicating MAGE–KAP1 binding is required for ZNF382 ubiquitination. Also please note an ubiquitinated ZNF382 degradation product of lesser molecular weight in the presence of wild type MAGE-C2 and KAP1. Lowest panel: immunoprecipitation and immunoblotting confirms expression of ZNF382.</p

Proposed model of MAGE-KAP1 interactions.

<p>KAP1 performs diverse functions by serving as a molecular scaffold that binds multiple proteins which allow it to regulate chromatin environments. KAP1 has an N terminal RING-B-box coiled-coil (RBCC) domain that binds to the KRAB domains of KZNFs, which target KAP1 to specific DNA sequences through their zinc finger DNA binding motifs. KAP1 mediates localized compaction of euchromatin to heterochromatin that is necessary for suppression of specific gene transcription, and that is associated with chromatin modifications including histone de-acetylation, histone 3 tri-methylation on K9, and HP1 binding to both DNA and histones. In some cases, MAGE expression enhances KAP1 E3 ubiquitin ligase activity, resulting in KZNF ubiquitination and degradation, thereby de-repressing KZNF mediated gene repression, shown as (-). In other cases, MAGE enhances KZNF and KAP1 localization to specific gene loci, shown as (+) (After A. Ivanov <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0023747#pone.0023747-Ivanov1" target="_blank">[22]</a>).</p

A schematic representation of Connaught Hospital EHU.

<p>A schematic representation of Connaught Hospital EHU.</p