Jackson, Daniel John

[["dc.bibliographiccitation.artnumber","54"],["dc.bibliographiccitation.journal","Proteome Science"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Marie, Benjamin"],["dc.contributor.author","Marie, Arul"],["dc.contributor.author","Jackson, Daniel John"],["dc.contributor.author","Dubost, Lionel"],["dc.contributor.author","Degnan, Bernard M."],["dc.contributor.author","Milet, Christian"],["dc.contributor.author","Marin, Frederic"],["dc.date.accessioned","2018-11-07T08:37:05Z"],["dc.date.available","2018-11-07T08:37:05Z"],["dc.date.issued","2010"],["dc.description.abstract","Background: The formation of the molluscan shell is regulated to a large extent by a matrix of extracellular macromolecules that are secreted by the shell forming tissue, the mantle. This so called \"calcifying matrix\" is a complex mixture of proteins and glycoproteins that is assembled and occluded within the mineral phase during the calcification process. While the importance of the calcifying matrix to shell formation has long been appreciated, most of its protein components remain uncharacterised. Results: Recent expressed sequence tag (EST) investigations of the mantle tissue from the tropical abalone (Haliotis asinina) provide an opportunity to further characterise the proteins in the shell by a proteomic approach. In this study, we have identified a total of 14 proteins from distinct calcified layers of the shell. Only two of these proteins have been previously characterised from abalone shells. Among the novel proteins are several glutamine-and methionine-rich motifs and hydrophobic glycine-, alanine-and acidic aspartate-rich domains. In addition, two of the new proteins contained Kunitz-like and WAP (whey acidic protein) protease inhibitor domains. Conclusion: This is one of the first comprehensive proteomic study of a molluscan shell, and should provide a platform for further characterization of matrix protein functions and interactions."],["dc.identifier.doi","10.1186/1477-5956-8-54"],["dc.identifier.isi","000284483200001"],["dc.identifier.pmid","21050442"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/5735"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/18450"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Biomed Central Ltd"],["dc.relation.issn","1477-5956"],["dc.rights","CC BY 2.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.0"],["dc.title","Proteomic analysis of the organic matrix of the abalone Haliotis asinina calcified shell"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","36978"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Sleight, Victoria A."],["dc.contributor.author","Marie, Benjamin"],["dc.contributor.author","Jackson, Daniel John"],["dc.contributor.author","Dyrynda, Elisabeth A."],["dc.contributor.author","Marie, Arul"],["dc.contributor.author","Clark, Melody S."],["dc.date.accessioned","2018-11-07T10:05:49Z"],["dc.date.available","2018-11-07T10:05:49Z"],["dc.date.issued","2016"],["dc.description.abstract","The Antarctic clam Laternula elliptica lives almost permanently below 0 degrees C and therefore is a valuable and tractable model to study the mechanisms of biomineralisation in cold water. The present study employed a multidisciplinary approach using histology, immunohistochemistry, electron microscopy, proteomics and gene expression to investigate this process. Thirty seven proteins were identified via proteomic extraction of the nacreous shell layer, including two not previously found in nacre; a novel T-rich Mucin-like protein and a Zinc-dependent metalloprotease. In situ hybridisation of seven candidate biomineralisation genes revealed discrete spatial expression patterns within the mantle tissue, hinting at modular organisation, which is also observed in the mantle tissues of other molluscs. All seven of these biomineralisation candidates displayed evidence of multifunctionality and strong association with vesicles, which are potentially involved in shell secretion in this species."],["dc.description.sponsorship","NERC DTG studentship [NE/J500173/1]; NERC core"],["dc.identifier.doi","10.1038/srep36978"],["dc.identifier.isi","000387551400001"],["dc.identifier.pmid","27833129"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13955"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38975"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","2045-2322"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0/"],["dc.title","An Antarctic molluscan biomineralisation tool-kit"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","75"],["dc.bibliographiccitation.journal","Frontiers in Zoology"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Le Roy, Nathalie"],["dc.contributor.author","Jackson, Daniel John"],["dc.contributor.author","Marie, Benjamin"],["dc.contributor.author","Ramos-Silva, Paula"],["dc.contributor.author","Marin, Frederic"],["dc.date.accessioned","2018-11-07T09:33:31Z"],["dc.date.available","2018-11-07T09:33:31Z"],["dc.date.issued","2014"],["dc.description.abstract","The carbonic anhydrase (CA; EC 4.2.1.1) superfamily is a class of ubiquitous metallo-enzymes that catalyse the reversible hydration of carbon dioxide. The alpha-CA family, present in all metazoan clades, is a key enzyme involved in a wide range of physiological functions including pH regulation, respiration, photosynthesis, and biocalcification. This paper reviews the evolution of the alpha-CA family, with an emphasis on metazoan alpha-CA members involved in biocalcification. Phylogenetic analyses reveal a complex evolutionary history of alpha-CAs, and suggest alpha-CA was independently co-opted into a variety of skeleton forming roles (e.g. as a provider of HCO3- ions, a structural protein, a nucleation activator, etc.) in multiple metazoan lineages. This evolutionary history is most likely the result of multiple gene duplications coupled with the insertion of repetitive or non-repetitive low-complexity domains (RLCDs/LCDs). These domains, of largely unknown function, appear to be lineage-specific, and provide further support for the hypothesis of independent recruitment of alpha-CAs to diverse metazoan biocalcification processes. An analysis of alpha-CA sequences associated with biocalcification processes indicates that the domains involved in the activity and conformation of the active site are extremely conserved among metazoans."],["dc.identifier.doi","10.1186/s12983-014-0075-8"],["dc.identifier.isi","000345800700001"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/12104"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31982"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Biomed Central Ltd"],["dc.relation.issn","1742-9994"],["dc.relation.orgunit","Fakultät für Geowissenschaften und Geographie"],["dc.rights","CC BY 4.0"],["dc.rights.uri","http://creativecommons.org/licenses/by/4.0"],["dc.title","The evolution of metazoan alpha-carbonic anhydrases and their roles in calcium carbonate biomineralization"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]