Our Health:Exploring interdisciplinarity and community-based participatory research in a higher education science shop

This paper presents a qualitative case study of the experiences of student and community partners involved in collaborative health research in the context of an extra-curricular higher education science shop: Our Health. Our Health community partners set research questions around health and well-being, and conduct research with interdisciplinary groups of students using a community-based participatory research model. Our case study explores the benefits and challenges that this approach raises for students and community partners as they navigate the complexities of stepping beyond disciplinary boundaries and relationships to develop new research insights and methodologies. This qualitative case study draws on: grounded theory to analyse online focus groups with participating undergraduate students and community partners; semi-structured interviews with graduate students and key university staff members; and online project meetings. For the latter, we used non-participant observation to observe community members and students at work in online meetings, co-creating evolving knowledge around the lived experiences of health issues. Through these methods, we developed a deeper understanding of the relational modes of community–student collaboration in community-based participatory research. Our findings demonstrate the key role played by interdisciplinarity in the context of a community-based participatory research approach in enabling students and community partners to develop their intrapersonal skills, health research skills and knowledge integration skills, while strengthening connections between the academy and wider communities

Demonstrating the Use of Optical Fibres in Biomedical Sensing:A Collaborative Approach for Engagement and Education

This paper demonstrates how research at the intersection of physics, engineering, biology and medicine can be presented in an interactive and educational way to a non-scientific audience. Interdisciplinary research with a focus on prevalent diseases provides a relatable context that can be used to engage with the public. Respiratory diseases are significant contributors to avoidable morbidity and mortality and have a growing social and economic impact. With the aim of improving lung disease understanding, new techniques in fibre-based optical endomicroscopy have been recently developed. Here, we present a novel engagement activity that resembles a bench-to-bedside pathway. The activity comprises an inexpensive educational tool ($70) adapted from a clinical optical endomicroscopy system and tutorials that cover state-of-the-art research. The activity was co-created by high school science teachers and researchers in a collaborative way that can be implemented into any engagement development process

Genetic mechanisms of critical illness in COVID-19.

Host-mediated lung inflammation is present1, and drives mortality2, in the critical illness caused by coronavirus disease 2019 (COVID-19). Host genetic variants associated with critical illness may identify mechanistic targets for therapeutic development3. Here we report the results of the GenOMICC (Genetics Of Mortality In Critical Care) genome-wide association study in 2,244 critically ill patients with COVID-19 from 208 UK intensive care units. We have identified and replicated the following new genome-wide significant associations: on chromosome 12q24.13 (rs10735079, P = 1.65 × 10-8) in a gene cluster that encodes antiviral restriction enzyme activators (OAS1, OAS2 and OAS3); on chromosome 19p13.2 (rs74956615, P = 2.3 × 10-8) near the gene that encodes tyrosine kinase 2 (TYK2); on chromosome 19p13.3 (rs2109069, P = 3.98 ×  10-12) within the gene that encodes dipeptidyl peptidase 9 (DPP9); and on chromosome 21q22.1 (rs2236757, P = 4.99 × 10-8) in the interferon receptor gene IFNAR2. We identified potential targets for repurposing of licensed medications: using Mendelian randomization, we found evidence that low expression of IFNAR2, or high expression of TYK2, are associated with life-threatening disease; and transcriptome-wide association in lung tissue revealed that high expression of the monocyte-macrophage chemotactic receptor CCR2 is associated with severe COVID-19. Our results identify robust genetic signals relating to key host antiviral defence mechanisms and mediators of inflammatory organ damage in COVID-19. Both mechanisms may be amenable to targeted treatment with existing drugs. However, large-scale randomized clinical trials will be essential before any change to clinical practice

The TriTryp Phosphatome: analysis of the protein phosphatase catalytic domains-2

<p><b>Copyright information:</b></p><p>Taken from "The TriTryp Phosphatome: analysis of the protein phosphatase catalytic domains"</p><p>http://www.biomedcentral.com/1471-2164/8/434</p><p>BMC Genomics 2007;8():434-434.</p><p>Published online 26 Nov 2007</p><p>PMCID:PMC2175518.</p><p></p>d as markers. Phosphatase domains are indicated by systematic gene IDs. Sequences are colour-coded by organism: blue for (), () and (F); red for human (); brown for () and green for (). Protein names replace Swiss-Prot IDs for some human, yeast and plant sequences. Results of the four phylogenetic methods are shown: bootstrap values > 70 are black for Neighbour-Joining, brown for Bayesian and purple for Maximum Parsimony. Asterisks (*) show Maximum Likelihood support

The TriTryp Phosphatome: analysis of the protein phosphatase catalytic domains-5

<p><b>Copyright information:</b></p><p>Taken from "The TriTryp Phosphatome: analysis of the protein phosphatase catalytic domains"</p><p>http://www.biomedcentral.com/1471-2164/8/434</p><p>BMC Genomics 2007;8():434-434.</p><p>Published online 26 Nov 2007</p><p>PMCID:PMC2175518.</p><p></p>man, and as markers. Phosphatase domains are indicated by systematic gene IDs. Sequences are colour-coded by organism: blue for (), () and (F); red for human (); brown for () and green for (). Protein names replace Swiss-Prot IDs for some human, yeast and plant sequences. The results of the four phylogenetic methods are shown: bootstrap values > 70 are black for Neighbour-Joining, brown for Bayesian and purple for Maximum Parsimony. Asterisks (*) show Maximum Likelihood support

The TriTryp Phosphatome: analysis of the protein phosphatase catalytic domains-7

<p><b>Copyright information:</b></p><p>Taken from "The TriTryp Phosphatome: analysis of the protein phosphatase catalytic domains"</p><p>http://www.biomedcentral.com/1471-2164/8/434</p><p>BMC Genomics 2007;8():434-434.</p><p>Published online 26 Nov 2007</p><p>PMCID:PMC2175518.</p><p></p>tase domains are indicated by systematic gene IDs. Sequences are colour-coded by organism: blue for (Tc), (Tb) and (LmjF); red for human (Hs); brown for S. cerevisiae (Sc) and green for A. thaliana (At). Protein names replace Swiss-Prot IDs for some human, yeast and plant sequences and systematic IDs for the parasites. Results of the four phylogenetic methods are shown: bootstrap values > 70 are black for Neighbour-Joining, brown for Bayesian and purple for Maximum Parsimony. Asterisks (*) show Maximum Likelihood support. The symbol '+' marks kinetoplastid sequences with catalytic mutations (listed in Additional file )

The TriTryp Phosphatome: analysis of the protein phosphatase catalytic domains-8

<p><b>Copyright information:</b></p><p>Taken from "The TriTryp Phosphatome: analysis of the protein phosphatase catalytic domains"</p><p>http://www.biomedcentral.com/1471-2164/8/434</p><p>BMC Genomics 2007;8():434-434.</p><p>Published online 26 Nov 2007</p><p>PMCID:PMC2175518.</p><p></p>ains are indicated by systematic gene IDs. Sequences are colour-coded by organism: blue for (), () and (F); red for human (); brown for () and green for (). Most sequence IDs are from the Swiss-Prot database but there are also NCBI database accession numbers used (beginning 'NP'). Results of the four phylogenetic methods are shown: bootstrap values > 70 are black for Neighbour-Joining, brown for Bayesian and purple for Maximum Parsimony. Asterisks (*) show Maximum Likelihood support. Dashed lines show phylogenetic relationships as indicated in an initial tree from an ungapped alignment. Each clade was analysed separately to obtain robust phylogenetic analysis and these were then combined to show the whole PPM family

The TriTryp Phosphatome: analysis of the protein phosphatase catalytic domains-1

<p><b>Copyright information:</b></p><p>Taken from "The TriTryp Phosphatome: analysis of the protein phosphatase catalytic domains"</p><p>http://www.biomedcentral.com/1471-2164/8/434</p><p>BMC Genomics 2007;8():434-434.</p><p>Published online 26 Nov 2007</p><p>PMCID:PMC2175518.</p><p></p>sphatase subfamilies. PTP, protein tyrosine phosphatase; DSP, dual-specificity phosphatase (crossed means pseudophosphatase); kinase, protein kinase domain (crossed means pseudokinase); TPR, Tetratricopeptide repeat; LRR, Leucine rich repeat; CaLB, Calcium lipid binding; GRAM, glucosyltransferases, Rab-like GTPases activators and myotubularins domain (plasma membrane protein-binding domain); FYVE, Fab1p/YOTB, Vac1p/EEA1 (PI3P binding domain); EF-hand, calcium binding domain; S/T phosphatase, serine/threonine phosphatase catalytic domain; FCP, CTD protein phosphatase. Note that many InterPro domains are variations representing the same biological function and sometimes they overlap. Only one domain is represented for these regions in this figure. Numbers of each domain type are listed for the kinetoplastids and '-' shows where one of the parasites lacks a particular architecture. ACR2/cdc25-like are included in the DSP group

The TriTryp Phosphatome: analysis of the protein phosphatase catalytic domains-4

<p><b>Copyright information:</b></p><p>Taken from "The TriTryp Phosphatome: analysis of the protein phosphatase catalytic domains"</p><p>http://www.biomedcentral.com/1471-2164/8/434</p><p>BMC Genomics 2007;8():434-434.</p><p>Published online 26 Nov 2007</p><p>PMCID:PMC2175518.</p><p></p> essential conserved residues for catalysis marked above. Analysis of the both kinase domains from the three kinatases is shown underneath. Fully conserved motifs are boxed in black and conserved residues from partially conserved regions are in bold type

The TriTryp Phosphatome: analysis of the protein phosphatase catalytic domains-9

<p><b>Copyright information:</b></p><p>Taken from "The TriTryp Phosphatome: analysis of the protein phosphatase catalytic domains"</p><p>http://www.biomedcentral.com/1471-2164/8/434</p><p>BMC Genomics 2007;8():434-434.</p><p>Published online 26 Nov 2007</p><p>PMCID:PMC2175518.</p><p></p>ifferent families: S/T Phosphatases, Protein tyrosine phosphatases, Dual-specificity phosphatases and PTEN/MTM lipid phosphatases. Phosphatase complements are shown for , , , in comparison with those for the Human [24, 26, 29, 128], [129, 130] and [76, 131] genomes. ACR2/cdc25-like are included in the DSP group