Jackson, Daniel John

[["dc.bibliographiccitation.journal","MRS Online Proceedings Library"],["dc.bibliographiccitation.volume","1187"],["dc.contributor.author","Marie, Benjamin"],["dc.contributor.author","Le Roy, Nathalie"],["dc.contributor.author","Marie, Arul"],["dc.contributor.author","Dubost, Lionel"],["dc.contributor.author","Milet, Christian"],["dc.contributor.author","Bedouet, Laurent"],["dc.contributor.author","Becchi, Michel"],["dc.contributor.author","Zanella-Cléon, Isabelle"],["dc.contributor.author","Jackson, Daniel John"],["dc.contributor.author","Degnan, Bernard"],["dc.contributor.author","Luquet, Gilles"],["dc.contributor.author","Marin, Frederic"],["dc.date.accessioned","2021-12-06T15:46:18Z"],["dc.date.available","2021-12-06T15:46:18Z"],["dc.date.issued","2011"],["dc.identifier.doi","10.1557/PROC-1187-KK01-03"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/95273"],["dc.relation.issn","0272-9172"],["dc.relation.issn","1946-4274"],["dc.relation.orgunit","Abteilung Geobiologie"],["dc.title","Nacre Evolution : A Proteomic Approach"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["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"]]

[["dc.bibliographiccitation.firstpage","214"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","FEBS Journal"],["dc.bibliographiccitation.lastpage","232"],["dc.bibliographiccitation.volume","280"],["dc.contributor.author","Marie, Benjamin"],["dc.contributor.author","Jackson, Daniel John"],["dc.contributor.author","Ramos-Silva, Paula"],["dc.contributor.author","Zanella-Cleon, Isabelle"],["dc.contributor.author","Guichard, Nathalie"],["dc.contributor.author","Marin, Frederic"],["dc.date.accessioned","2018-11-07T09:30:46Z"],["dc.date.available","2018-11-07T09:30:46Z"],["dc.date.issued","2013"],["dc.description.abstract","Proteins that are occluded within the molluscan shell, the so-called shell matrix proteins (SMPs), are an assemblage of biomolecules attractive to study for several reasons. They increase the fracture resistance of the shell by several orders of magnitude, determine the polymorph of CaCO3 deposited, and regulate crystal nucleation, growth initiation and termination. In addition, they are thought to control the shell microstructures. Understanding how these proteins have evolved is also likely to provide deep insight into events that supported the diversification and expansion of metazoan life during the Cambrian radiation 543 million years ago. Here, we present an analysis of SMPs isolated form the CaCO3 shell of the limpet Lottia gigantea, a gastropod that constructs an aragonitic cross-lamellar shell. We identified 39 SMPs by combining proteomic analysis with genomic and transcriptomic database interrogations. Among these proteins are various low-complexity domain-containing proteins, enzymes such as peroxidases, carbonic anhydrases and chitinases, acidic calcium-binding proteins and protease inhibitors. This list is likely to contain the most abundant SMPs of the shell matrix. It reveals the presence of both highly conserved and lineage-specific biomineralizing proteins. This mosaic evolutionary pattern suggests that there may be an ancestral molluscan SMP set upon which different conchiferan lineages have elaborated to produce the diversity of shell microstructures we observe nowadays. Database Novel protein sequences reported in this article have been deposited in Swiss-Prot database under accession nos. B3A0P1B3A0S4"],["dc.description.sponsorship","ANR Accro-Earth [BLAN06-2_159971]; BIOMINTEC; INTERRVIE program; DFG"],["dc.identifier.doi","10.1111/febs.12062"],["dc.identifier.isi","000312995400017"],["dc.identifier.pmid","23145877"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31386"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Wiley-blackwell"],["dc.relation.issn","1742-464X"],["dc.title","The shell-forming proteome of Lottia gigantea reveals both deep conservations and lineage-specific novelties"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","GigaScience"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Herlitze, Ines"],["dc.contributor.author","Marie, Benjamin"],["dc.contributor.author","Marin, Frederic"],["dc.contributor.author","Jackson, Daniel J."],["dc.date.accessioned","2020-05-06T10:54:07Z"],["dc.date.available","2020-05-06T10:54:07Z"],["dc.date.issued","2018"],["dc.description.abstract","Conchiferan molluscs construct a biocalcified shell that likely supported much of their evolutionary success. However, beyond broad proteomic and transcriptomic surveys of molluscan shells and the shell-forming mantle tissue, little is known of the spatial and ontogenetic regulation of shell fabrication. In addition, most efforts have been focused on species that deposit nacre, which is at odds with the majority of conchiferan species that fabricate shells using a crossed-lamellar microstructure, sensu lato."],["dc.identifier.doi","10.1093/gigascience/giy056"],["dc.identifier.pmid","29788257"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/64895"],["dc.language.iso","en"],["dc.relation.issn","2047-217X"],["dc.title","Molecular modularity and asymmetry of the molluscan mantle revealed by a gene expression atlas"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]