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  • 1
    Language: English
    In: Nature communications, 2018-02-22, Vol.9 (1), p.756-12
    Description: Thermobia domestica belongs to an ancient group of insects and has a remarkable ability to digest crystalline cellulose without microbial assistance. By investigating the digestive proteome of Thermobia, we have identified over 20 members of an uncharacterized family of lytic polysaccharide monooxygenases (LPMOs). We show that this LPMO family spans across several clades of the Tree of Life, is of ancient origin, and was recruited by early arthropods with possible roles in remodeling endogenous chitin scaffolds during development and metamorphosis. Based on our in-depth characterization of Thermobia's LPMOs, we propose that diversification of these enzymes toward cellulose digestion might have endowed ancestral insects with an effective biochemical apparatus for biomass degradation, allowing the early colonization of land during the Paleozoic Era. The vital role of LPMOs in modern agricultural pests and disease vectors offers new opportunities to help tackle global challenges in food security and the control of infectious diseases.
    Subject(s): Animals ; Arthropods ; Arthropods - enzymology ; Arthropods - genetics ; Arthropods - growth & development ; Biochemistry ; Biochemistry, Molecular Biology ; Biodegradation ; Biodegradation, Environmental ; Biomass ; Cellulose ; Cellulose - metabolism ; Chitin ; Chitin - metabolism ; Colonization ; Crystalline cellulose ; Digestion ; Environmental degradation ; Evolution, Molecular ; Food security ; Genes, Insect ; Infectious diseases ; Insect Proteins - chemistry ; Insect Proteins - genetics ; Insect Proteins - metabolism ; Insecta - enzymology ; Insecta - genetics ; Insecta - growth & development ; Insects ; Life Sciences ; Metamorphosis ; Microorganisms ; Mixed Function Oxygenases - chemistry ; Mixed Function Oxygenases - genetics ; Mixed Function Oxygenases - metabolism ; Models, Molecular ; Paleozoic ; Pests ; Phylogeny ; Polysaccharides - metabolism ; Proteomes ; Proteomics ; Thermobia ; Vectors
    ISSN: 2041-1723
    E-ISSN: 2041-1723
    Source: Nature Open Access
    Source: PubMed Central
    Source: DOAJ Directory of Open Access Journals - Not for CDI Discovery
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  • 2
    Article
    Article
    2015
    ISSN: 1479-8360 
    Language: English
    In: Museum and society, 2015-11-01, Vol.13 (4), p.503-521
    Description: This article complements an identified ‘cultural turn’ in military history, which emphasizes the potency of perception and the extent to which successes, failures, opportunities and threats are culturally conditioned (Black 2004: 233-35). It will deal with issues surrounding ‘collective remembrance’, a concept which Joanna Bourke identifies as problematic. For Bourke, ‘collectivememory’ has been characterized by a ‘museal sensibility’ in which mass narratives ‘wallow’ in a nostalgic world of community, stability and certainty (Bourke 2004: 473). She argues that collective memory is an exclusive script, which imposes unity on individual experiences and overlooks conscious acts of cultural selection (Bourke 2004: 473). Whilst scholarship on the relationship of present with past rightly takes issue with collective, or public, memory, precluding individual, or private, memories, Bourke usefully draws attention to the mythical qualities of collective remembrance. Military history, integral as it is to national identity yet harbouring inherently difficult histories, is particularly susceptible to cultural, social and political mediation. This article traces nineteenth-century treatments of two Crimean failures and the legacy ofthese attitudes today in museums, which to a large extent echo some of the dominant myths and silences of Victorian Britain.
    ISSN: 1479-8360
    E-ISSN: 1479-8360
    Source: DOAJ Directory of Open Access Journals - Not for CDI Discovery
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  • 3
    Language: English
    In: Science signaling, 2020-07-21, Vol.13 (641)
    Description: Calcium/calmodulin-dependent protein kinase II (CaMKII) plays a central role in Ca signaling throughout the body. In the hippocampus, CaMKII is required for learning and memory. Vertebrate genomes encode four CaMKII homologs: CaMKIIα, CaMKIIβ, CaMKIIγ, and CaMKIIδ. All CaMKIIs consist of a kinase domain, a regulatory segment, a variable linker region, and a hub domain, which is responsible for oligomerization. The four proteins differ primarily in linker length and composition because of extensive alternative splicing. Here, we report the heterogeneity of CaMKII transcripts in three complex samples of human hippocampus using deep sequencing. We showed that hippocampal cells contain a diverse collection of over 70 CaMKII transcripts from all four CaMKII-encoding genes. We characterized the Ca /CaM sensitivity of hippocampal CaMKII variants spanning a broad range of linker lengths and compositions. The effect of the variable linker on Ca /CaM sensitivity depended on the kinase and hub domains. Moreover, we revealed a previously uncharacterized role for the hub domain as an allosteric regulator of kinase activity, which may provide a pharmacological target for modulating CaMKII activity. Using small-angle x-ray scattering and single-particle cryo-electron microscopy (cryo-EM), we present evidence for extensive interactions between the kinase and the hub domains, even in the presence of a 30-residue linker. Together, these data suggest that Ca /CaM sensitivity in CaMKII is homolog dependent and includes substantial contributions from the hub domain. Our sequencing approach, combined with biochemistry, provides insights into understanding the complex pool of endogenous CaMKII splice variants.
    Subject(s): Activation ; Allosteric properties ; Alternative splicing ; Ca2+/calmodulin-dependent protein kinase II ; Calcium ; Calcium ions ; Calcium signalling ; Calcium-binding protein ; Calmodulin ; Composition effects ; Domains ; Electron microscopy ; Genomes ; Heterogeneity ; Hippocampus ; Homology ; Kinases ; Long term memory ; Oligomerization ; Proteins ; Sensitivity ; Serine ; Small angle X ray scattering ; Splicing ; Structure-function relationships ; Therapeutic applications ; Threonine ; Vertebrates ; X ray scattering
    ISSN: 1945-0877
    E-ISSN: 1937-9145
    Source: Science Magazine
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  • 4
    Article
    Article
    2015
    ISSN: 1755-1560 
    Language: English
    In: 19: interdisciplinary studies in the long nineteenth century, 2015-05-13, Vol.2015 (20)
    Description: The Crimean War occurred during a formative period of ‘civic publicness’, a term used by John Plunkett to describe the press-mediated public duties undertaken by Victoria and Albert to affirm the monarchy’s popular constitution. The war triggered significant royal intervention into the condition of the army, one of the few sites of royal prerogative. At a time when aristocratic governance was being attacked and the privations of soldiers exposed to an unprecedented extent, the monarchy was keen both to legitimize its role as head of the army and to demonstrate its sensitivity to popular concern for the suffering of ordinary soldiers. This manifested in a highly publicized leaked letter from the Queen expressing her regard for ‘her troops’, the royal family’s visits to wounded soldiers, and the distribution of the Crimean Medal at a special ceremony, which portrayed the accessibility of the Queen through the use of touch. This article explores the symbolism and impetus of these occurrences and assesses the reception of royal intervention in the press. The few assessments of royal influence during the Crimean War have focused largely on Victoria’s personal fascination with the progress of the war and her soldiers. This article explores instead the wider, political significance of the army as extension of the royal family. The Liberal press and artists responded favourably to demonstrations of the Queen’s maternal sympathy for the troops, but my article will point to a hidden struggle to assert the Crown’s authority.
    Subject(s): Affect ; Armed forces ; Army ; Books ; Crimean War ; Families & family life ; Military personnel ; monarchy ; Ordinary soldier ; Politics ; Queen Victoria ; Symbolism ; Tactility ; War
    ISSN: 1755-1560
    E-ISSN: 1755-1560
    Source: Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals
    Source: DOAJ Directory of Open Access Journals - Not for CDI Discovery
    Source: ProQuest Central
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  • 5
    Language: English
    In: Science (American Association for the Advancement of Science), 2015-07-17, Vol.349 (6245), p.309-312
    Description: Morphinan alkaloids from the opium poppy are used for pain relief. The direction of metabolites to morphinan biosynthesis requires isomerization of (S)- to (R)-reticuline. Characterization of high-reticuline poppy mutants revealed a genetic locus, designated STORR [(S)- to (R)-reticuline] that encodes both cytochrome P450 and oxidoreductase modules, the latter belonging to the aldo-keto reductase family. Metabolite analysis of mutant alleles and heterologous expression demonstrate that the P450 module is responsible for the conversion of (S)-reticuline to 1,2-dehydroreticuline, whereas the oxidoreductase module converts 1,2-dehydroreticuline to (R)-reticuline rather than functioning as a P450 redox partner. Proteomic analysis confirmed that these two modules are contained on a single polypeptide in vivo. This modular assembly implies a selection pressure favoring substrate channeling. The fusion protein STORR may enable microbial-based morphinan production.
    Subject(s): Biosynthesis ; Enzymes ; Metabolites ; Modules ; Morphine ; Narcotics ; Pathways ; Poppies ; Proteins ; REPORTS
    ISSN: 0036-8075
    E-ISSN: 1095-9203
    Source: JSTOR Life Sciences
    Source: Academic Search Ultimate
    Source: Alma/SFX Local Collection
    Source: Get It Now
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  • 6
    Language: English
    In: Archives of disease in childhood, 2019-06, Vol.104 (Suppl 3), p.A216
    Description: BackgroundTic Disorder is a common problem that affects 1:1000 children. Tics can either be an isolated phenomenon, causing minimal stress or can be functionally significant causing interference with day to day life.Within the Belfast trust many children are referred by General Practitioners to general paediatricians in the Royal Belfast Hospital for Sick Children because of concerns about tics. It was noted after discussion with the general paediatric team that investigations, management and referral patterns differed among general paediatricians.AimsThe authors therefore concluded it would be helpful to develop a guideline toencourage a consistent investigation and management approach for Tic disorder andclarify referral pathways from Belfast Trust general paediatrics to psychology, neurology and community based services including Child & Adult Mental Health Services (CAHMS)MethodologyIn 2018, a small working group was established in RBHSC, consisting of two general paediatricians, one consultant paediatric neurologist, the lead paediatric psychologist and a paediatric trainee. An initial draft, based on information and evidence from current medical literature, was produced. It was subsequently amended several times after working group meetings and regular email correspondence. Belfast Trust Community paediatricians and the CAHMS lead were consulted, with particular attention to the referral pathways. The wider general paediatric medical team was asked to review the final draft. Help was obtained from a quality improvement manager to ensure the guideline met Trust quality and formatting standards.ResultsThe guideline is now complete and awaiting final approval from the Belfast Trust. It contains advice on structured approach to the history and examinations of a child with possible tic disorder and when investigations are indicated. Management is discussed under two categories of (a) Simple tics and (b) Tics with co-morbidities. Advice is given on who will benefit from psychology input and what to do when co-morbidities are noted. Indications for paediatric neurology and CAHMS referral are discussed. The Appendix includes community referral forms, the Yale tic questionnaire and some links to information for carers.ConclusionThe authors are hopeful this guideline has fulfilled the aims outlined. Consideration will be given to seeking feedback from users when it is formally adopted. Paediatricians from other Trusts may also find much of the guidance helpful though caution would be needed with the referral pathways which are different in different Trusts.
    Subject(s): Children ; Childrens health ; Management ; Mental disorders ; Pediatrics ; Quality control ; Working groups
    ISSN: 0003-9888
    E-ISSN: 1468-2044
    Source: Hellenic Academic Libraries Link
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  • 7
    Language: English
    In: Biotechnology for biofuels, 2018, Vol.11 (1), p.59-59
    Description: Lignocellulose forms the structural framework of woody plant biomass and represents the most abundant carbon source in the biosphere. Turnover of woody biomass is a critical component of the global carbon cycle, and the enzymes involved are of increasing industrial importance as industry moves away from fossil fuels to renewable carbon resources. Shipworms are marine bivalve molluscs that digest wood and play a key role in global carbon cycling by processing plant biomass in the oceans. Previous studies suggest that wood digestion in shipworms is dominated by enzymes produced by endosymbiotic bacteria found in the animal's gills, while little is known about the identity and function of endogenous enzymes produced by shipworms. Using a combination of meta-transcriptomic, proteomic, imaging and biochemical analyses, we reveal a complex digestive system dominated by uncharacterized enzymes that are secreted by a specialized digestive gland and that accumulate in the cecum, where wood digestion occurs. Using a combination of transcriptomics, proteomics, and microscopy, we show that the digestive proteome of the shipworm is mostly composed of enzymes produced by the animal itself, with a small but significant contribution from symbiotic bacteria. The digestive proteome is dominated by a novel 300 kDa multi-domain glycoside hydrolase that functions in the hydrolysis of β-1,4-glucans, the most abundant polymers in wood. These studies allow an unprecedented level of insight into an unusual and ecologically important process for wood recycling in the marine environment, and open up new biotechnological opportunities in the mobilization of sugars from lignocellulosic biomass.
    Subject(s): Carbon cycle (Biogeochemistry) ; Cellulose ; Digestive organs ; Enzymes ; Physiological aspects ; Properties
    ISSN: 1754-6834
    E-ISSN: 1754-6834
    Source: BioMedCentral Open Access
    Source: Academic Search Ultimate
    Source: PubMed Central
    Source: DOAJ Directory of Open Access Journals - Not for CDI Discovery
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  • 8
    Language: English
    In: mBio, 2019-05-01, Vol.10 (3)
    Description: The physiological role of protein O-glycosylation in prokaryotes is poorly understood due to our limited knowledge of the extent of their glycoproteomes. In Actinobacteria, defects in protein O-mannosyl transferase (Pmt)-mediated protein O-glycosylation have been shown to significantly retard growth (Mycobacterium tuberculosis and Corynebacterium glutamicum) or result in increased sensitivities to cell wall-targeting antibiotics (Streptomyces coelicolor), suggesting that protein O-glycosylation has an important role in cell physiology. Only a single glycoprotein (SCO4142, or PstS) has been identified to date in S. coelicolor. Combining biochemical and mass spectrometry-based approaches, we have isolated and characterized the membrane glycoproteome in S. coelicolor. A total of ninety-five high-confidence glycopeptides were identified which mapped to thirty-seven new S. coelicolor glycoproteins and a deeper understanding of glycosylation sites in PstS. Glycosylation sites were found to be modified with up to three hexose residues, consistent with what has been observed previously in other Actinobacteria. S. coelicolor glycoproteins have diverse roles and functions, including solute binding, polysaccharide hydrolases, ABC transporters, and cell wall biosynthesis, the latter being of potential relevance to the antibiotic-sensitive phenotype of pmt mutants. Null mutants in genes encoding a putative D-Ala-D-Ala carboxypeptidase (SCO4847) and an L, D-transpeptidase (SCO4934) were hypersensitive to cell wall-targeting antibiotics. Additionally, the sco4847 mutants displayed an increased susceptibility to lysozyme treatment. These findings strongly suggest that both glycoproteins are required for maintaining cell wall integrity and that glycosylation could be affecting enzyme function. IMPORTANCE In prokaryotes, the role of protein glycosylation is poorly understood due to our limited understanding of their glycoproteomes. In some Actinobacteria, defects in protein O-glycosylation have been shown to retard growth and result in hypersensitivity to cell wall-targeting antibiotics, suggesting that this modification is important for maintaining cell wall structure. Here, we have characterized the glycoproteome in Streptomyces coelicolor and shown that glycoproteins have diverse roles, including those related to solute binding, ABC transporters, and cell wall biosynthesis. We have generated mutants encoding two putative cell wall-active glycoproteins and shown them to be hypersensitive to cell wall-targeting antibiotics. These findings strongly suggest that both glycoproteins are required for maintaining cell wall integrity and that glycosylation affects enzyme function.
    Subject(s): Actinobacteria ; Anti-Bacterial Agents - pharmacology ; antibiotic resistance ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Cell Wall - physiology ; cell wall biogenesis ; Editor's Pick ; glycopeptides ; Glycoproteins - genetics ; Glycoproteins - metabolism ; Glycosylation ; Life Sciences & Biomedicine ; mass spectrometry ; Microbiology ; Molecular Biology and Physiology ; Organelle Biogenesis ; protein O-glycosylation ; protein O-mannosyltransferase ; Proteome ; Science & Technology ; Streptomyces coelicolor - enzymology ; Streptomyces coelicolor - genetics
    ISSN: 2150-7511
    ISSN: 2161-2129
    E-ISSN: 2150-7511
    Source: HighWire Press (Free Journals)
    Source: Web of Science - Science Citation Index Expanded - 2019〈img src="http://exlibris-pub.s3.amazonaws.com/fromwos-v2.jpg" /〉
    Source: Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals
    Source: PubMed Central
    Source: DOAJ Directory of Open Access Journals - Not for CDI Discovery
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  • 9
    Language: English
    In: 19: interdisciplinary studies in the long nineteenth century, 2015-05-13, Vol.2015 (20)
    Description: The Crimean War (1853–56) is much more culturally significant than its popular mythologies suggest. Now remembered mainly for the Charge of the Light Brigade and the Lady with the Lamp, the Crimean War is a pivotal moment in the history of modern warfare seen as both the last of the old wars and first of the new. The first total war, it inaugurated new forms of weaponry, tactics, communication, war reporting, military medicine, and new attitudes towards soldiers. The introduction outlines this issue of 19’s case for the conflict’s wide-ranging significance, placing the Crimean War in the context of earlier and later nineteenth-century warfare, and considering its varied cultural afterlives.
    Subject(s): Armed forces ; Attitudes ; Crimean War, Victorian Warfare, Military Mythologies, War and Nationhood ; Invasions ; Medicine ; Military history ; Mythology ; War
    ISSN: 1755-1560
    E-ISSN: 1755-1560
    Source: Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals
    Source: DOAJ Directory of Open Access Journals - Not for CDI Discovery
    Source: ProQuest Central
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  • 10
    Article
    Article
    2015
    ISSN: 1755-1560 
    Language: English
    In: 19: interdisciplinary studies in the long nineteenth century, 2015, Vol.20
    Subject(s): 1800-1899 ; British Army ; Crimean War ; English literature ; monarchy ; newspapers ; prose ; sympathy
    ISSN: 1755-1560
    E-ISSN: 1755-1560
    Source: Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals
    Source: DOAJ Directory of Open Access Journals - Not for CDI Discovery
    Source: ProQuest Central
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