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The term data mining is used to describe a large range of techniques used to extract information from biological data. The dictionary definition defines data mining as 'methods to look for trends or anomalies in data without knowledge of the meaning of the data', and this type of analysis is heavily exploited within the retail and financial world. This article presents a discovery-driven data mining technique used on protein structure data to highlight features of interest that would be difficult find using hypothesis-based analysis. [ABSTRACT FROM AUTHOR]

Although some sectors have made significant progress in learning from failure, there is currently limited consensus on how a similar transition could best be achieved in conservation and what is required to facilitate this. One of the key enabling conditions for other sectors is a widely accepted and standardized classification system for identifying and analyzing root causes of failure. We devised a comprehensive taxonomy of root causes of failure affecting conservation projects. To develop this, we solicited examples of real-life conservation efforts that were deemed to have failed in some way, identified their underlying root causes of failure, and used these to develop a generic, 3-tier taxonomy of the ways in which projects fail, at the top of which are 6 overarching cause categories that are further divided into midlevel cause categories and specific root causes. We tested the taxonomy by asking conservation practitioners to use it to classify the causes of failure for conservation efforts they had been involved in. No significant gaps or redundancies were identified during this testing phase. We then analyzed the frequency that particular root causes were encountered by projects within this test sample, which suggested that some root causes were more likely to be encountered than others and that a small number of root causes were more likely to be encountered by projects implementing particular types of conservation action. Our taxonomy could be used to improve identification, analysis, and subsequent learning from failed conservation efforts, address some of the barriers that currently limit the ability of conservation practitioners to learn from failure, and contribute to establishing an effective culture of learning from failure within conservation., (© 2022 The Authors. Conservation Biology published by Wiley Periodicals LLC on behalf of Society for Conservation Biology.)

Background: Gastrointestinal symptoms are commonly associated with acute Plasmodium spp infection. Malaria-associated enteritis may provide an opportunity for enteric pathogens to breach the intestinal mucosa, resulting in life-threatening systemic infections. Methods: To investigate whether intestinal pathology also occurs during infection with a murine model of mild and resolving malaria, C57BL/6J mice were inoculated with recently mosquito-transmitted Plasmodium chabaudi AS. At schizogony, intestinal tissues were collected for quantification and localisation of immune mediators and malaria parasites, by PCR and immunohistochemistry. Inflammatory proteins were measured in plasma and faeces and intestinal permeability was assessed by FITC-dextran translocation after oral administration. Results: Parasitaemia peaked at approx. 1.5% at day 9 and resolved by day 14, with mice experiencing significant and transient anaemia but no weight loss. Plasma IFNγ, TNFα and IL10 were significantly elevated during peak infection and quantitative RT-PCR of the intestine revealed a significant increase in transcripts for ifng and cxcl10 . Histological analysis revealed parasites within blood vessels of both the submucosa and intestinal villi and evidence of mild crypt hyperplasia. In faeces, concentrations of the inflammatory marker lactoferrin were significantly raised on days 9 and 11 and FITC-dextran was detected in plasma on days 7 to 14. At day 11, plasma FITC-dextran concentration was significantly positively correlated with peripheral parasitemia and faecal lactoferrin concentration. Conclusions: In summary, using a relevant, attenuated model of malaria, we have found that acute infection is associated with intestinal inflammation and increased intestinal permeability. This model can now be used to explore the mechanisms of parasite-induced intestinal inflammation and to assess the impact of increased intestinal permeability on translocation of enteropathogens., Competing Interests: Competing interests: ABP is an Editorial Assistant for F1000 Research Ltd. Wellcome Open Research is controlled by Wellcome, using services provided by F1000Research. ABP was involved in the data generation and analysis for the article, but had no involvement following submission of the final version for publication, nor the post publication peer review of the article., (Copyright: © 2022 Mooney JP et al.)

The genome of a novel virus, tentatively named bandicoot papillomatosis carcinomatosis virus type 2 (BPCV2), obtained from multicentric papillomatous lesions from an adult male southern brown bandicoot (Isoodon obesulus) was sequenced in its entirety. BPCV2 had a circular double-stranded DNA genome consisting of 7277 bp and open reading frames encoding putative L1 and L2 structural proteins and putative large T antigen and small t antigen transforming proteins. These genomic features, intermediate between Papillomaviridae and Polyomaviridae are most similar to BPCV1, recently described from papillomas and carcinomas in the endangered western barred bandicoot (Perameles bougainville). This study also employed in situ hybridization to definitively demonstrate BPCV2 DNA within lesion biopsies. The discovery of BPCV2 provides evidence of virus-host co-speciation between BPCVs and marsupial bandicoots and has important implications for the phylogeny and taxonomy of circular double-stranded DNA viruses infecting vertebrates.

This report presents three cases of mycobacteriosis in gang gang cockatoos (Callocephalon fimbriatum) that highlight the potential variation in clinical presentation of this important avian disease. The first case was a female gang gang cockatoo with widespread skeletal disease that presented with a chronic history of weight loss and nonpainful, bilaterally symmetric, distal-wing and leg nodular swellings. The second case was a mature female in good muscle condition with a nodular granulomatous pericarditis and myocarditis causing severe hydropericardium and cardiac tamponade; it was presented for respiratory distress. The third case was one of alimentary mycobacteriosis that presented with a chronic history of weight loss. Some difficulties associated with confirming a premortem diagnosis of mycobacteriosis are discussed.

The three-dimensional environments of ligand binding sites have been derived from the parsing and loading of the PDB entries into a relational database. For each bound molecule the biological assembly of the quaternary structure has been used to determine all contact residues and a fast interactive search and retrieval system has been developed. Prosite pattern and short sequence search options are available together with a novel graphical query generator for inter-residue contacts. The database and its query interface are accessible from the Internet through a web server located at: http://www.ebi.ac.uk/msd-srv/msdsite.

A staff midwife describes what it is like to be back on the Maternity Unit after a break of 11 years and a "return to practice" course. It is a steep learning curve but she finds the work fulfilling.

The protein databank contains a vast wealth of structural and functional information. The analysis of this macromolecular information has been the subject of considerable work in order to advance knowledge beyond the collection of molecular coordinates. This article presents a method that determines local structural information within proteins using mathematical data mining techniques. The mine program described returns many known configurations of residues such as the catalytic triad, metal binding sites and the N-linked glycosylation site; as well as many other multiple residue interactions not previously categorized. Because mathematical constructs are used as targets, this method can identify new information not previously known, and also provide unbiased results of typical structure and their expected deviations. Because the results are defined mathematically, they cannot indicate the biological implications of the results. Therefore two support programs are described that provide insight into the biological context for the mine results. The first allows a weighted RMSD search between a template set of coordinates and a list of PDB files, and the second allows the labeling of a protein with the template results from mining to aid in the classification of this protein., (Copyright 2002 Wiley-Liss, Inc.)

The interpretation of macromolecular crystallographic electron-density maps is a difficult and traditionally a manual step in the determination of a protein structure. The visualization of information within an electron-density map can be extremely arduous owing to the amount and complexity of information present. The ability to see the overall fold and structure of the molecule is usually lost among all the detail, particularly with larger structures. This paper describes a novel method of analysis of electron density in real space that can determine the secondary structure of a protein within minutes without any user intervention. The method is able to work with poor data as well as good data at resolutions down to 3.5A and is integral to the functionality of QUANTA. This article describes the methodology of the pattern recognition and its use with a number of sets of experimental data.

This paper describes the implementation of real-space torsion-angle refinement as a tool for model (re)building. The algorithmic details and parameterization for a number of different protocols are presented, as well as the handling of special conditions. Examples illustrating the use of the algorithms show that these tools provide a great advantage over traditional methods for building macromolecular structures. All these algorithms have been implemented in QUANTA (MSI), currently available as version QUANTA98.

The program EXTRACT has been developed to extract accurate three-dimensional coordinates from published stereo alpha-carbon diagrams of protein structures. The approach is based on the display of scanned images of the left and right eye views of the diagram on a stereo-equipped workstation, allowing construction of a molecular model using the diagram as a guide. A number of structural checks assess the building, including probability maps derived for alpha-carbon geometry in protein structures. The procedure has also been extended to produce less accurate models from mono images.

The polypeptide of a protein molecule can be considered as a chain of C alpha atoms linked by pseudobonds between the C alpha atoms of successive amino acid residues. This paper presents an analysis of the angle and dihedral angles made by these pseudobonds in protein structures determined at high resolution by X-ray crystallography. This analysis reveals a strong correlation between C alpha geometry and the protein fold. The regular features of protein secondary structure such as alpha-helix and beta-sheet are very clearly defined. In addition, it is possible to identify with some confidence the discrete populations of particular conformations of beta-turn. Comparison with the traditional Ramachandran type of plot demonstrates that an analysis of protein structure on the basis of C alpha geometry provides a richer description of protein conformation. In addition, the characteristics of this geometry could be a useful guide in model building of protein structure.

A comparison has been made between the homology and hydrophobicity profiles of six interleukin amino acid sequences and that of the human interleukin 1 beta (IL-1 beta) for which a crystal structure exists. The resulting sequence alignment was used to build model structures for the sequences for three IL-1 alpha, two IL-1 beta and an interleukin receptor antagonist. Analysis of these structures demonstrates that the interleukin molecule has a strong electric dipole which is generated by the topological position of the amino acids in the sequence. Electrostatic surface calculations implicate a particular residues (Lys145) as being fundamental to interleukin activity and this supports site-directed mutation evidence that this residue is required for activity.

SQUID is a flexible computer program that allows the analysis and display of molecular coordinates from crystallography, NMR, and molecular dynamics. The program can also display two-dimensional and three-dimensional data using many graph types, as well as perform array processing of data with numerous intrinsic functions. Graphics are based on the use of "move" and "draw" instructions, allowing easy development of new device drivers, including vector plotters.

The structure of pig aquometmyoglobin has been refined to a crystallographic R-factor of 19.8% against X-ray diffraction data between 10- and 1.75-A spacing. The final structural model comprises two molecules of pig myoglobin, 233 water molecules, and two sulfate ions. A water molecule is coordinated to each of the heme iron atoms with an average Fe-OH2 bond distance of 2.19 A, and the mean Fe-N epsilon (proximal histidine-93) distance is 2.20 A. In contrast to the structure of sperm whale metmyoglobin, the iron is not significantly displaced from the plane of the heme. At the entrance to the heme pocket, the side-chain amino group of lysine-45 (CD3) is well-defined in the electron density map and forms salt-bridging interactions with the heme 6-propionate and with a sulfate ion. Serine and arginine replacements have been made previously at position 45 to examine the proposal that the CD3 side chain acts as a barrier to ligand entry into the protein. Crystal structures of the arginine-45 and serine-45 mutant metmyoglobins have been solved to 1.9 and 2.0 A resolution, respectively. In both cases the structural changes are confined to the site of mutation. Arginine-45 takes up a conformation closely similar to that observed for this residue in wild-type sperm whale myoglobin, in which it makes more extensive charge-charge and charge-dipole interactions and appears to restrict the movement of the distal histidine away from the ligand. The hydroxyl group of serine-45 is disordered, but it is clear that the effect of the mutation is to open up the solvent-exposed face of the heme pocket.

Recombinant porcine myoglobin has been produced in Escherichia coli using the lambda cII fusion expression system of Nagai and Thøgersen [Nature, 309, 810-812 (1984)]. After processing and reconstitution with haem, the protein is gel-electrophoretically and spectrophotometrically indistinguishable from native pig myoglobin. Large crystals of both native and recombinant porcine myoglobin were grown from 50 mM sodium phosphate, pH 7.1, 80% ammonium sulphate. The crystals belong to space group C2 (a = 156.9 A, b = 42.0 A, c = 92.2 A, beta = 127.9 degrees) and diffract to a nominal 2.5 A resolution. We plan to explore apomyoglobin as a binding surface in studies combining site-directed mutagenesis and X-ray analysis. These experiments will be extended by studying the binding of haem analogues to the mutant apoproteins.