From the forest set out like the night

<div>Reprint with permission of an extract from John Anderson, the forest set out like the night, Black Pepper, Melbourne, 1995.</div><div><br></div><div><div>Anderson, J. From the forest set out like the night. PAN : philosophy activism nature. 2000; 1, 16-22</div></div

MOESM2 of Links between DNA methylation and nucleosome occupancy in the human genome

Additional file 2. Detailed bioinformatics procedures and in-house scripts used in this study are enclosed in the zip file

MOESM1 of Links between DNA methylation and nucleosome occupancy in the human genome

Additional file 1. Additional figures

In vivo testing of GD2 CAR.

<p>Balb-C mice were innocultaed with 1x10⁶ CT26 or CT26-GD2 cell mixed in matrigel. 10 days post tumour inoculation, mice were sub-lethally irradiated (200 rads) and two weeks post tumour injection, mice were intravenously transplanted with a total of 1.5x10⁶ transduced splenocytes or non transduced controls by tail vein injection. Wild type CT26 were used as antigen negative controls (a,c) whereas CT26 –GD2 tumors treated with untransduced T cells (b) did not regress whilst CT26-GD2 tumors challenged with CAR T cells regressed. Each line represents one mouse.</p

Consequence and function of iCasp9.

<p>The SAR codon-optimized cassette was taken further and compared with the original cassette without iCasp9. (a) Expression of the CAR was unchanged. Depletion is shown by facs after addition of CID. The function of cassettes with and without iCasp9 were assessed by (b) Killing (c) IFN-γ release and (d) IL-2 release. Data shown as means +/-SEM from 4 independent experiments with different donors.</p

Frontespizio e pagine iniziali

The effect of internal resistivit

Removal of FcR binding motifs in IgG1 spacer.

<p>(a) amino acid sequence of the wild type (top) and mutated (PVAA) CH2 regions responsible for FcγR binding. (b) flow staining with anti-Fc antibody to show comparable level of expression of receptor with or without the PVAA mutation. Identical CARs with and without PVAA were compared side by side in terms of cytotoxicity against GD2 engineered SupT1 and GD2 negative wild type SipT1 cells (c), cytotoxicity against GD2 positive Lan1 cells and FcRγ positive THP-1 cells (d), and IL-1β release on culture with THP-1 cells (e). Data shown as means +/-SEM from 4 independent experiments with different donors.</p

Table S1 from Voltage-dependent K⁺ channels improve the energy efficiency of signalling in blowfly photoreceptors

Total K⁺ conductance and depolarising conductance of the active photoreceptor membrane model at the four levels of membrane depolarisation we modelled, together with the same conductances of the matched passive membranes with the same capacitance and bandwidth

The CELF1 RNA-Binding Protein Regulates Decay of Signal Recognition Particle mRNAs and Limits Secretion in Mouse Myoblasts

<div><p>We previously identified several mRNAs encoding components of the secretory pathway, including signal recognition particle (SRP) subunit mRNAs, among transcripts associated with the RNA-binding protein CELF1. Through immunoprecipitation of RNAs crosslinked to CELF1 in myoblasts and <i>in vitro</i> binding assays using recombinant CELF1, we now provide evidence that CELF1 directly binds the mRNAs encoding each of the subunits of the SRP. Furthermore, we determined the half-lives of the <i>Srp</i> transcripts in control and CELF1 knockdown myoblasts. Our results indicate CELF1 is a destabilizer of at least five of the six <i>Srp</i> transcripts and that the relative abundance of the SRP proteins is out of balance when CELF1 is depleted. CELF1 knockdown myoblasts exhibit altered secretion of a luciferase reporter protein and are impaired in their ability to migrate and close a wound, consistent with a defect in the secreted extracellular matrix. Importantly, similar defects in wound healing are observed when SRP subunit imbalance is induced by over-expression of SRP68. Our studies support the existence of an RNA regulon containing <i>Srp</i> mRNAs that is controlled by CELF1. One implication is that altered function of CELF1 in myotonic dystrophy may contribute to changes in the extracellular matrix of affected muscle through defects in secretion.</p></div

CELF1 binding to 3’UTR of <i>Srp</i> mRNAs <i>in vitro</i>.

<p>CELF1 binding to 3’UTR of <i>Srp</i> mRNAs <i>in vitro</i>.</p