Classification of masked image data.

Data classification is one of the most commonly used applications of machine learning. The are many developed algorithms that can work in various environments and for different data distributions that perform this task with excellence. Classification algorithms, just like other machine learning algorithms have one thing in common: in order to operate on data, they must see the data. In the present world, where concerns about privacy, GDPR (General Data Protection Regulation), business confidentiality and security are growing bigger and bigger; this requirement to work directly on the original data might become, in some situations, a burden. In this paper, an approach to the classification of images that cannot be directly accessed during training has been made. It has been shown that one can train a deep neural network to create such a representation of the original data that i) without additional information, the original data cannot be restored, and ii) that this representation-called a masked form-can still be used for classification purposes. Moreover, it has been shown that classification of the masked data can be done using both classical and neural network-based classifiers.

Some of the most interesting CASP11 targets through the eyes of their authors.

The Critical Assessment of protein Structure Prediction (CASP) experiment would not have been possible without the prediction targets provided by the experimental structural biology community. In this article, selected crystallographers providing targets for the CASP11 experiment discuss the functional and biological significance of the target proteins, highlight their most interesting structural features, and assess whether these features were correctly reproduced in the predictions submitted to CASP11. Proteins 2016; 84(Suppl 1):34-50. © 2015 The Authors. Proteins: Structure, Function, and Bioinformatics Published by Wiley Periodicals, Inc.

STAC--A New Domain Associated with Transmembrane Solute Transport and Two-Component Signal Transduction Systems.

Transmembrane receptors are integral components of sensory pathways in prokaryotes. These receptors share a common dimeric architecture, consisting in its basic form of an N-terminal extracellular sensor, transmembrane helices, and an intracellular effector. As an exception, we have identified an archaeal receptor family--exemplified by Af1503 from Archaeoglobus fulgidus--that is C-terminally shortened, lacking a recognizable effector module. Instead, a HAMP domain forms the sole extension for signal transduction in the cytosol. Here, we examine the gene environment of Af1503-like receptors and find a frequent association with transmembrane transport proteins. Furthermore, we identify and define a closely associated new protein domain family, which we characterize structurally using Af1502 from A. fulgidus. Members of this family are found both as stand-alone proteins and as domains within extant receptors. In general, the latter appear as connectors between the solute carrier 5 (SLC5)-like transmembrane domains and two-component signal transduction (TCST) domains. This is seen, for example, in the histidine kinase CbrA, which is a global regulator of metabolism, virulence, and antibiotic resistance in Pseudomonads. We propose that this newly identified domain family mediates signal transduction in systems regulating transport processes and name it STAC, for SLC and TCST-Associated Component.

The thalidomide-binding domain of cereblon defines the CULT domain family and is a new member of the ß-tent fold.

Despite having caused one of the greatest medical catastrophies of the last century through its teratogenic side-effects, thalidomide continues to be an important agent in the treatment of leprosy and cancer. The protein cereblon, which forms an E3 ubiquitin ligase compex together with damaged DNA-binding protein 1 (DDB1) and cullin 4A, has been recently indentified as a primary target of thalidomide and its C-terminal part as responsible for binding thalidomide within a domain carrying several invariant cysteine and tryptophan residues. This domain, which we name CULT (cereblon domain of unknown activity, binding cellular ligands and thalidomide), is also found in a family of secreted proteins from animals and in a family of bacterial proteins occurring primarily in δ-proteobacteria. Its nearest relatives are yippee, a highly conserved eukaryotic protein of unknown function, and Mis18, a protein involved in the priming of centromeres for recruitment of CENP-A. Searches for distant homologs point to an evolutionary relationship of CULT, yippee, and Mis18 to proteins sharing a common fold, which consists of two four-stranded ß-meanders packing at a roughly right angle and coordinating a zinc ion at their apex. A ß-hairpin inserted into the first ß-meander extends across the bottom of the structure towards the C-terminal edge of the second ß-meander, with which it forms a cradle-shaped binding site that is topologically conserved in all members of this fold. We name this the ß-tent fold for the striking arrangement of its constituent ß-sheets. The fold has internal pseudosymmetry, raising the possibility that it arose by duplication of a subdomain-sized fragment.