The Language Function Analysis 2011 Corpus (LFA-11) is a German text corpus of promotional text, reviews and blog posts on music and smartphones. The texts were manually classified with respect to their topic relevance, language function, and sentiment polarity.

The purpose of the corpus is to provide textual data for the development and evaluation of approaches to language function analysis and sentiment analysis. Therefore, each text is classified by language function (personal, commercial, or informational) as well as by sentiment (positive, negative, neutral).

The corpus consists of two separated collections, which contain the texts about music and smartphones respectively. The music collection consists of 2,713 promotional texts and reviews from both users and professionals. The smartphone collection contains 2,093 blog posts on smartphones from the Spinn3r corpus.

LFA-1 (CD11a-CD18) - BioCentury Target Profiles for the biopharma industry

Sample ID: LFA_Rd6t08_A11

X-ray tomography (CT) image data of a Ti6Al4V disc. The 3D image was generated with an X-ray tomography scan performed by Dr Llion Evans with Swansea University, Advanced Imaging of Materials (AIM) equipment.

The dataset includes: raw radiographs; scan & reconstruction parameter settings file; reconstructed 3D volume. To visualise the 3D volume use software such as ImageJ (https://imagej.net/Fiji/Downloads). The volume image data (.raw file) is in binary format and has the following characteristics: 1920 x 1920 x 1536; 16-bit; little-endian byte order.

This data is part of a 'virtual testing' benchmark study, where samples are tested physically in the lab and their microscale accurate digital equivalent are tested virtually through simulation. The technique of converting 3D volumetric images directly into finite element method (FEM) meshes is part of the Image-Based Simulation (IBSim) approach.

This data is part of a batch of samples for thermal testing via laser flash analysis (LFA), following the standards ASTM E1461 / ASTM E2585. As part of the study, controlled defects were introduced into the samples. This was achieved by machining a disc shaped recess (of defined diameter and depth) into one disc which is bonded onto another disc, so that the defect is located internally within the final sample.

The samples in the batch are named as follows.

Sample ID Diameter Thickness Recess d Recess t
LFA_RNA_### 12.6 2.5 N/A N/A
LFA_Rd0t00_### 12.6 1.25 x 2 N/A N/A
LFA_Rd8t02_### 12.6 1.25 x 2 8.0 0.2
LFA_Rd8t08_### 12.6 1.25 x 2 8.0 0.8
LFA_Rd6t02_### 12.6 1.25 x 2 6.0 0.2
LFA_Rd6t08_### 12.6 1.25 x 2 6.0 0.8
LFA_Rd4t02_### 12.6 1.25 x 2 4.0 0.2
LFA_Rd4t08_### 12.6 1.25 x 2 4.0 0.8

Where ### denotes the furnace bonding batch (A-C and N for no bonding cycle) and sample number (01-30). Values in mm.

The Bordetella adenylate cyclase toxinhemolysin (CyaA) and the α-hemolysin (HlyA) of Escherichia coli both belong to the family of cytolytic pore-forming Repeats in ToXin (RTX) cytotoxins. HlyA preferentially binds the αLβ2 integrin LFA-1 (CD11a/CD18) of leukocytes and can promiscuously bind and permeabilize also a variety of other cells. CyaA bears an Nterminal adenylyl cyclase enzyme (AC) domain linked to a pore-forming RTX cytolysin (Hly) moiety and binds the complement receptor 3 (CR3, αMβ2, CD11b/CD18 or Mac-1) of myeloid phagocytes, penetrates their plasma membrane and delivers into cytosol the AC enzyme. We constructed a set of CyaA/HlyA chimeras and show that the CyaC-acylated segment and the CR3-binding RTX domain of CyaA can be functionally replaced by the much shorter HlyCacylated and LFA-1-binding RTX moiety of HlyA. Instead of binding CR3, a CyaA1710/HlyA411-1024 chimera bound the LFA-1 receptor and effectively delivered the AC enzyme into Jurkat lymphoblastoma T cells. At high chimera concentrations (25 nM), the interaction with LFA-1 was not required for CyaA1-710/HlyA411-1024 binding to CHO cells. However, interaction with the LFA-1 receptor strongly enhanced the specific capacity of the bound CyaA1-710/HlyA411-1024 chimera to penetrate cells and deliver the AC enzyme into their cytosol. Hence, interaction of the acylated RTX moiety of HlyA with LFA-1 promoted a productive membrane interaction of the chimera. These results allow to delimit the residues 400 to 710 of CyaA as the 'AC translocon' sufficient for translocation of the AC enzyme polypeptide across the plasma membrane of target cells