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  • 1
    Online Resource
    Online Resource
    Springer Science and Business Media LLC ; 1993
    In:  Zoomorphology Vol. 113, No. 1 ( 1993-3), p. 47-60
    In: Zoomorphology, Springer Science and Business Media LLC, Vol. 113, No. 1 ( 1993-3), p. 47-60
    Type of Medium: Online Resource
    ISSN: 0720-213X , 1432-234X
    RVK:
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 1993
    detail.hit.zdb_id: 1462021-2
    SSG: 12
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  • 2
    Online Resource
    Online Resource
    Frontiers Media SA ; 2021
    In:  Frontiers in Mechanical Engineering Vol. 7 ( 2021-5-24)
    In: Frontiers in Mechanical Engineering, Frontiers Media SA, Vol. 7 ( 2021-5-24)
    Abstract: To attach to surfaces in the sea, sea stars produce proteinaceous adhesive secretions. Sfp1 is a major constituent of this adhesive, where it is present in the form of four subunits (named Sfp1α to δ) displaying specific protein-, carbohydrate- and metal-binding domains. Recently, two recombinant proteins inspired from Sfp1 have been produced: one corresponding to the C-terminal part of Sfp1β and the other to the full-length Sfp1δ. Adsorption ability tests showed that both recombinant proteins were able to adsorb and to form coatings on different surfaces in artificial seawater as well as in Tris buffer supplemented with NaCl or CaCl 2 . In this study, we used Atomic Force Microscopy (AFM) to characterize the nanomechanical properties of these coatings with an emphasis on functional characteristics such as adhesive properties and modulus of elasticity. We used AFM techniques which are the most appropriate to characterize the coating microstructure combined with the mapping of its nanomechanical properties.
    Type of Medium: Online Resource
    ISSN: 2297-3079
    Language: Unknown
    Publisher: Frontiers Media SA
    Publication Date: 2021
    detail.hit.zdb_id: 2835636-6
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  • 3
    Online Resource
    Online Resource
    University of Chicago Press ; 2006
    In:  The Biological Bulletin Vol. 211, No. 2 ( 2006-10), p. 172-182
    In: The Biological Bulletin, University of Chicago Press, Vol. 211, No. 2 ( 2006-10), p. 172-182
    Type of Medium: Online Resource
    ISSN: 0006-3185 , 1939-8697
    Language: English
    Publisher: University of Chicago Press
    Publication Date: 2006
    detail.hit.zdb_id: 2056482-X
    detail.hit.zdb_id: 3022817-7
    detail.hit.zdb_id: 1268-3
    SSG: 12
    SSG: 21,3
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  • 4
    Online Resource
    Online Resource
    Frontiers Media SA ; 2021
    In:  Frontiers in Marine Science Vol. 8 ( 2021-4-15)
    In: Frontiers in Marine Science, Frontiers Media SA, Vol. 8 ( 2021-4-15)
    Abstract: The cookie-cutter shark Isistius brasiliensis (Squaliformes: Dalatiidae) is a deep-sea species that emits a blue luminescence ventrally, except at the level of a black band located beneath the jaw. This study aims to ( i ) investigate the distribution and histology of the photophores (i.e., light-emitting organs) along the shark body, ( ii ) describe the tissue-specific transcriptomes of the black band integument region (i.e., non-photogenic) and the ventral integument region (i.e., photogenic), ( iii ) describe the repertoire of enzyme-coding transcripts expressed the two integument regions, and ( iv ) analyze the potential expression of transcripts coding for luciferase-like enzymes (i.e., close homologs of known luciferases involved in the bioluminescence of other organisms). Our analyses confirm the black band’s non-photogenic status and photophore absence within this region. The sub-rostral area is the region where the photophore density is the highest. In parallel, paired-end Illumina sequencing has been used to generate two pilot transcriptomes, from the black band and the ventral integument tissues of one individual. In total, 68,943 predicted unigenes have been obtained (i.e., 64,606 for the black band transcriptome, 43,996 for the ventral integument transcriptome) with 43,473 unigenes showing significant similarities to known sequences from public databases. BLAST search analyses of known luciferases, coupled with comparative predicted gene expression (i.e., photogenic versus non-photogenic), support the hypothesis that the species uses an unknown luciferase system. An enzymatic repertoire was predicted based on the PRIAM database, and Enzyme Commission numbers were assigned for all detected enzyme-coding unigenes. These pilot transcriptomes based on a single specimen, and the predicted enzyme repertoire, constitute a valuable resource for future investigations on the biology of this enigmatic luminous shark.
    Type of Medium: Online Resource
    ISSN: 2296-7745
    Language: Unknown
    Publisher: Frontiers Media SA
    Publication Date: 2021
    detail.hit.zdb_id: 2757748-X
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  • 5
    Online Resource
    Online Resource
    Springer Science and Business Media LLC ; 2016
    In:  BMC Developmental Biology Vol. 16, No. 1 ( 2016-06-02)
    In: BMC Developmental Biology, Springer Science and Business Media LLC, Vol. 16, No. 1 ( 2016-06-02)
    Abstract: Flatworms possess pluripotent stem cells that can give rise to all cell types, which allows them to restore lost body parts after injury or amputation. This makes flatworms excellent model systems for studying regeneration. In this study, we present the adhesive organs of a marine flatworm as a simple model system for organ regeneration. Macrostomum lignano has approximately 130 adhesive organs at the ventral side of its tail plate. One adhesive organ consists of three interacting cells: one adhesive gland cell, one releasing gland cell, and one modified epidermal cell, called an anchor cell. However, no specific markers for these cell types were available to study the regeneration of adhesive organs. Results We tested 15 commercially available lectins for their ability to label adhesive organs and found one lectin (peanut agglutinin) to be specific to adhesive gland cells. We visualized the morphology of regenerating adhesive organs using lectin- and antibody staining as well as transmission electron microscopy. Our findings indicate that the two gland cells differentiate earlier than the connected anchor cells. Using EdU/lectin staining of partially amputated adhesive organs, we showed that their regeneration can proceed in two ways. First, adhesive gland cell bodies are able to survive partial amputation and reconnect with newly formed anchor cells. Second, adhesive gland cell bodies are cleared away, and the entire adhesive organ is build anew. Conclusion Our results provide the first insights into adhesive organ regeneration and describe ten new markers for differentiated cells and tissues in M. lignano . The position of adhesive organ cells within the blastema and their chronological differentiation have been shown for the first time. M. lignano can regenerate adhesive organs de novo but also replace individual anchor cells in an injured organ. Our findings contribute to a better understanding of organogenesis in flatworms and enable further molecular investigations of cell-fate decisions during regeneration.
    Type of Medium: Online Resource
    ISSN: 1471-213X
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2016
    detail.hit.zdb_id: 2041492-4
    SSG: 12
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  • 6
    In: Journal of Experimental Marine Biology and Ecology, Elsevier BV, Vol. 506 ( 2018-09), p. 61-71
    Type of Medium: Online Resource
    ISSN: 0022-0981
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2018
    detail.hit.zdb_id: 410283-6
    detail.hit.zdb_id: 1483103-X
    SSG: 12
    SSG: 7,20
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  • 7
    In: Chemoecology, Springer Science and Business Media LLC, Vol. 32, No. 3 ( 2022-06), p. 95-104
    Type of Medium: Online Resource
    ISSN: 0937-7409 , 1423-0445
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2022
    detail.hit.zdb_id: 1458504-2
    SSG: 12
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  • 8
    Online Resource
    Online Resource
    The Royal Society ; 2019
    In:  Philosophical Transactions of the Royal Society B: Biological Sciences Vol. 374, No. 1784 ( 2019-10-28), p. 20190195-
    In: Philosophical Transactions of the Royal Society B: Biological Sciences, The Royal Society, Vol. 374, No. 1784 ( 2019-10-28), p. 20190195-
    Abstract: Sea stars use adhesive secretions to attach their numerous tube feet strongly and temporarily to diverse surfaces. After detachment of the tube feet, the adhesive material stays bound to the substrate as so-called ‘footprints’. In the common sea star species Asterias rubens , the adhesive material has been studied extensively and the first sea star footprint protein (Sfp1) has been characterized. We identified Sfp1-like sequences in 17 additional sea star species, representing different taxa and tube foot morphologies, and analysed the evolutionary conservation of this protein. In A. rubens , we confirmed the expression of 34 footprint proteins in the tube foot adhesive epidermis, with 22 being exclusively expressed in secretory cells of the adhesive epidermis and 12 showing an additional expression in the stem epidermis. The sequences were used for BLAST searches in seven asteroid transcriptomes providing a first insight in the conservation of footprint proteins among sea stars. Our results highlighted a high conservation of the large proteins making up the structural core of the footprints, whereas smaller, potential surface-binding proteins might be more variable among sea star species. This article is part of the theme issue ‘Transdisciplinary approaches to the study of adhesion and adhesives in biological systems’.
    Type of Medium: Online Resource
    ISSN: 0962-8436 , 1471-2970
    RVK:
    Language: English
    Publisher: The Royal Society
    Publication Date: 2019
    detail.hit.zdb_id: 1462620-2
    SSG: 12
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  • 9
    Online Resource
    Online Resource
    Wiley ; 2019
    In:  Rapid Communications in Mass Spectrometry Vol. 33, No. S2 ( 2019-07), p. 22-33
    In: Rapid Communications in Mass Spectrometry, Wiley, Vol. 33, No. S2 ( 2019-07), p. 22-33
    Abstract: Saponins are natural compounds presenting a high structural diversity whose structural characterization remains extremely challenging. Ideally, saponin structures are best established using nuclear magnetic resonance experiments conducted on isolated molecules. However, saponins are also increasingly characterized using tandem mass spectrometry (MS/MS) coupled with liquid chromatography, even if collision‐induced dissociation (CID) experiments are often quite limited in accurately determining the saponin structure. Methods We consider here ion mobility mass spectrometry (IMMS) as an orthogonal tool for the structural characterization of saponin isomers by comparing the experimental collisional cross sections (CCSs) of saponin ions with theoretical CCSs for candidate ion structures. Indeed, state‐of‐the‐art theoretical calculations perfectly complement the experimental results, allowing the ion structures to be deciphered at the molecular level. Results We demonstrate that ion mobility can contribute to the structural characterization of saponins because different saponin ions present significantly distinct CCSs. Depending on the nature of the cation (in the positive ion mode), the differences in CCSs can also be exacerbated, optimizing the gas‐phase separation. When associated with molecular dynamics simulations, the CCS data can be used to describe the interactions between the cations, i.e. H + , Na + and K + , and the saponin molecules at a molecular level. Conclusions Our work contributes to resolve the relationship between the primary and secondary structures of saponin ions. However, it is obvious that the structural diversity and complexity of the saponins cannot be definitively unraveled by measuring a single numerical value, here the CCS. Consequently, the structural characterization of unknown saponins will be difficult to achieve based on IMMS alone. Nevertheless, we demonstrated that monodesmosidic and bidesmosidic saponins can be distinguished via IMMS.
    Type of Medium: Online Resource
    ISSN: 0951-4198 , 1097-0231
    URL: Issue
    Language: English
    Publisher: Wiley
    Publication Date: 2019
    detail.hit.zdb_id: 2002158-6
    detail.hit.zdb_id: 58731-X
    SSG: 11
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  • 10
    Online Resource
    Online Resource
    Elsevier BV ; 2005
    In:  Journal of Experimental Marine Biology and Ecology Vol. 315, No. 2 ( 2005-2), p. 211-223
    In: Journal of Experimental Marine Biology and Ecology, Elsevier BV, Vol. 315, No. 2 ( 2005-2), p. 211-223
    Type of Medium: Online Resource
    ISSN: 0022-0981
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2005
    detail.hit.zdb_id: 410283-6
    detail.hit.zdb_id: 1483103-X
    SSG: 12
    SSG: 7,20
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