Academic literature on the topic 'Pseudoalteromonas'
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Journal articles on the topic "Pseudoalteromonas"
Wang, Xiyan, Thomas Isbrandt, Mikael Lenz Strube, Sara Skøtt Paulsen, Maike Wennekers Nielsen, Yannick Buijs, Erwin M. Schoof, Thomas Ostenfeld Larsen, Lone Gram, and Sheng-Da Zhang. "Chitin Degradation Machinery and Secondary Metabolite Profiles in the Marine Bacterium Pseudoalteromonas rubra S4059." Marine Drugs 19, no. 2 (February 12, 2021): 108. http://dx.doi.org/10.3390/md19020108.
Full textLim, Su-Jin, Dae-jin Min, Sohee Kim, Jihye Lee, Eun-Soo Lee, Hyuk Kim, Sung-Yoen Cho, et al. "Pseudoalteromone A, a Ubiquinone Derivative from Marine Pseudoalteromonas spp., Suppresses Melanogenesis." Marine Drugs 19, no. 11 (October 28, 2021): 612. http://dx.doi.org/10.3390/md19110612.
Full textNam, Young-Do, Ho-Won Chang, Ja Ryeong Park, Hyuk-Yong Kwon, Zhe-Xue Quan, Yong-Ha Park, Jung-Sook Lee, Jung-Hoon Yoon, and Jin-Woo Bae. "Pseudoalteromonas marina sp. nov., a marine bacterium isolated from tidal flats of the Yellow Sea, and reclassification of Pseudoalteromonas sagamiensis as Algicola sagamiensis comb. nov." International Journal of Systematic and Evolutionary Microbiology 57, no. 1 (January 1, 2007): 12–18. http://dx.doi.org/10.1099/ijs.0.64523-0.
Full textPark, Yoon-Dong, Keun Sik Baik, Hana Yi, Kyung Sook Bae, and Jongsik Chun. "Pseudoalteromonas byunsanensis sp. nov., isolated from tidal flat sediment in Korea." International Journal of Systematic and Evolutionary Microbiology 55, no. 6 (November 1, 2005): 2519–23. http://dx.doi.org/10.1099/ijs.0.63750-0.
Full textOh, Yong-Sik, A.-Rum Park, Je-Kwan Lee, Chae-Sung Lim, Jae-Soo Yoo, and Dong-Hyun Roh. "Pseudoalteromonas donghaensis sp. nov., isolated from seawater." International Journal of Systematic and Evolutionary Microbiology 61, no. 2 (February 1, 2011): 351–55. http://dx.doi.org/10.1099/ijs.0.022541-0.
Full textZhao, Chang-Hui, Jing-Jing Luo, Ting Gong, Xiang-Ling Huang, De-Zan Ye, and Zhu-Hua Luo. "Pseudoalteromonas xiamenensis sp. nov., a marine bacterium isolated from coastal surface seawater." International Journal of Systematic and Evolutionary Microbiology 64, Pt_2 (February 1, 2014): 444–48. http://dx.doi.org/10.1099/ijs.0.050229-0.
Full textYu, Zhiliang, Yajuan Ding, Jianhua Yin, Dongliang Yu, Jiadi Zhang, Mengting Zhang, Mengdan Ding, Weihong Zhong, Juanping Qiu, and Jun Li. "Dissemination of Genetic Acquisition/Loss Provides a Variety of Quorum Sensing Regulatory Properties in Pseudoalteromonas." International Journal of Molecular Sciences 19, no. 11 (November 18, 2018): 3636. http://dx.doi.org/10.3390/ijms19113636.
Full textKim, Dockyu, Ha Ju Park, and Hyun Park. "Construction of Pseudoalteromonas - Escherichia coli shuttle vector based on a small plasmid from the marine organism Pseudoalteromonas." Korean Journal of Microbiology 52, no. 1 (March 31, 2016): 110–15. http://dx.doi.org/10.7845/kjm.2016.5054.
Full textNavarro-Torre, Salvadora, Lorena Carro, Ignacio D. Rodríguez-Llorente, Eloísa Pajuelo, Miguel Ángel Caviedes, José Mariano Igual, Hans-Peter Klenk, and Maria del Carmen Montero-Calasanz. "Pseudoalteromonas rhizosphaerae sp. nov., a novel plant growth-promoting bacterium with potential use in phytoremediation." International Journal of Systematic and Evolutionary Microbiology 70, no. 5 (May 1, 2020): 3287–94. http://dx.doi.org/10.1099/ijsem.0.004167.
Full textDoghri, Ibtissem, Emilie Portier, Florie Desriac, Jean Michel Zhao, Alexis Bazire, Alain Dufour, Vincent Rochette, Sophie Sablé, and Isabelle Lanneluc. "Anti-Biofilm Activity of a Low Weight Proteinaceous Molecule from the Marine Bacterium Pseudoalteromonas sp. IIIA004 against Marine Bacteria and Human Pathogen Biofilms." Microorganisms 8, no. 9 (August 25, 2020): 1295. http://dx.doi.org/10.3390/microorganisms8091295.
Full textDissertations / Theses on the topic "Pseudoalteromonas"
Sousa, Thiciana da Silva. "Micro-organismos marinhos produtores de metabólitos secundários biologicamente ativos." reponame:Repositório Institucional da UFC, 2013. http://www.repositorio.ufc.br/handle/riufc/14106.
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This work describe the chemical and biological investigation of the extracts from the marine bacterias Pseudoalteromonas sp., Micromonospora sp., Streptomyces sp. and Kocuria sp., aiming the isolation and structural elucidation of new bioactive constituents. The chemical investigation carried out with the bacteria Pseudoalteromonas sp. lead to the isolation a red pigment identified as prodigiosin and two bile acids derivatives known as deoxycholic acid and cholic acid. The prodigiosin was evaluated against four tumor cell lines showing IC50 values similar to the positive control doxorubicin. The chemical study of Micromonospora sp. Resulted in the isolation of four new anthracyclinones designed as 4,6,11-trihydroxy-9-propryltetracene-5,12-dione; 4-methoxy-9-propyltetracene-6,11-dione; 7,8,9,10 - tetrahydro-9-hydroxy-4-methoxy-9-propiltetra-cene-6,11-dione and 10β-Carbomethoxy-7,8,9,10-tetrahydro-4,6,7α,9α,11-pentahydroxy-9-propyltetracene-5,12-dione . The cytotoxic potential of these compounds were evaluated against HCT-8cell line, two of which showed moderate cytotoxicity with IC50 values of 12.74 and 6.18 M, respectively. From Streptomyces sp. strain was isolated a ditiolpyrrolidin, established as 5-oxo-6-(N-methylformamide) -4,5 - dihydro-1,2-dithiol [4,3-b] pyrrole. This secondary metabolite was tested against six tumor cell lines, shown IC50 values of 1.66, 1.05 and 1.52 mM for the metastatic prostate lines, ovarium carcinoma and glioblastoma, respectively. The study of Kocuria sp. lead to the isolation of a new peptide, which was designed as kocurin. This compound was subjected to the tested its antimicrobial assays against several pathogens bacteria and fungal including Staphylococcus aureus strains methicillin resistant (MRSA) and Staphylococcus aureus strains tiazomicin resistant. Kocurin was strongly active against MRSA MB5393 exhibiting a MIC of 0,25µg/mL, moreover showed antibacterial activity against Bacillus subtilis and Enterococcus faecium. The structures of all isolated compounds in this work were stabilized employing spectroscopic methods such as 1H and 13C NMR (1D and 2D), mass spectrometry and infrared.
Este trabalho descreve o estudo químico e biológico dos extratos das bactérias marinhas Pseudoalteromonas sp., Micromonospora sp., Streptomyces sp. e Kocuria sp., visando o isolamento e a elucidação estrutural de novos constituintes bioativos. A investigação química realizada com a bactéria Pseudoalteromonas sp. resultou no isolamento de um pigmento vermelho identificado como prodigiosina e de dois ácidos biliares conhecidos como ácido desoxicólico e ácido cólico. A prodigiosina foi testada frente a quatro linhagens de células tumorais e apresentou valores de IC50 semelhantes ao padrão positivo. O estudo químico de Micromonospora sp. resultou no isolamento de quatro novas antraciclinonas: 4,6,11-triidroxi-9-propriltetraceno-5,12-diona; 4-metoxi-9-propiltetraceno-6,11-diona; 7,8,9,10-tetraidro-9-hidroxi-4-metoxi-9-propiltetra-ceno-6,11-diona e 10β-metoxicarbonil-7,8,9,10-tetraidro-4,6,7α,9α,11–pentaidroxi–9–propil-tetraceno-5,12-diona. Esses compostos foram avaliados quanto a sua atividade anti-tumoral frente a linhagem celular HCT-8, dois dos quais mostraram citotoxidade moderada com valores de IC50 de 12,74 e 6,18 M. O estudo da bactéria Streptomyces sp. possibilitou o isolamento de uma ditiolpirrolidina cuja estrutura foi estabelecida como 5-oxo-6-(N-metilformamida)-4,5- diidro-1,2-ditiol[4,3-b]pirrol. Esse metabólito teve sua atividade citotóxica testada frente a seis linhagens celulares tumorais, mostrando forte atividade com IC50 de 1,66, 1,05 e 1,52 µM para as linhagens de próstata metastática, carcinoma de ovário e glioblastoma, respectivamente. O estudo de Kocuria sp. resultou no isolamento de um novo peptídeo denominado como kocurina. Esse composto teve sua atividade antimicrobiana testada frente a várias bactérias e fungos patogênicos, incluindo cepas de Staphylococcus aureus resistentes a meticilina (MRSA) e cepas de Staphylococcus aureus resistentes a tiazomicina. Kocurina inibiu fortemente o crescimento de MRSA MB5393 com valores de CIM de 0,25µg/mL, além de exibir atividade antibacteriana contra as bactérias Bacillus subtilis e Enterococcus faecium. As estruturas de todos os compostos isolados neste trabalho foram determinadas empregando métodos espectroscópicos tais como RMN 1H e 13C (1D e 2D), espectrometria de massas e infravermelho.
Evans, Flavia F. Biotechnology & Biomolecular Sciences Faculty of Science UNSW. "Analysis of the secretome and type II secretion in pseudoalteromonas tunicata." Awarded by:University of New South Wales. Biotechnology & Biomolecular Sciences, 2007. http://handle.unsw.edu.au/1959.4/40449.
Full textSijerčić, Ada. "Kinetics of siderophore production by a marine bacterium, Pseudoalteromonas haloplanktis." Thesis, McGill University, 2008. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=116077.
Full textEVANGELISTA, Giovanna. "Caratterizzazione molecolare e funzionale della Polinucleotide fosforilasi dall'eubatterio antartico Pseudoalteromonas Haloplanktis." Doctoral thesis, Università degli studi del Molise, 2010. http://hdl.handle.net/11695/66405.
Full textPolynucleotide phosphorylase (PNPase) is involved in the nucleotide metabolism pathway of both eukaryotes and prokaryotes. The enzyme catalyzes the phosphorolytic degradation of RNA, releasing nucleoside 5’-diphosphates from the 3’ end of the substrate, and the reverse reaction of nucleoside 5’-diphosphate polymerization. In this work it’s described the procedure of isolation and the characterization of PNPase from the psychrophilic eubacterium Pseudoalteromonas haloplanktis (Ph, optimal growth condition 4-20°C), identified for its ability to catalyse the following reversible reaction: RNA(n) + Pi ↔ RNA(n-1) + ppN PhPNPase showed a homotrimeric structure of 255 kDa, as evaluated by molecular mass analysis under native and denatured conditions. Using bioinformatic software, starting from the amino acid sequence, a prediction of the secondary and tertiary monomer structure have been obtained. Besides, studies on the amino acid composition have been carried out, thus evidencing that PhPNPase shows the typical adaptation of proteins isolated from psychrophilic organisms. The kinetic parameters have been determined at 15°C, using poly(A) as a primer and [3H]GDP as substrate. The effect of increasing concentration of [3H]GDP on the activity has been evaluated, thus allowing the determination of the kinetic parameters of the polymerization reaction. The activity of PhPNPase is stimulated by selected monovalent cations added in the reaction mixture, a feature already observed for other enzymes isolated from P. haloplanktis. Among the cations tested, CsCl, added to 0.9 M final concentration, has resulted the most effective, enhancing PhPNPase activity of about 7-fold. The effect of temperature on the activity and stability of PhPNPase has also been tested. In particular, the activity of PhPNPase increases with increasing temperature, reaching a maximum at 40°C; beyond this temperature a straight decay of the activity has been observed, due to thermal inactivation of the enzyme. In the 0-40°C interval, a value of 87 kJ/mol for the energy of activation of the reaction (Ea) has been calculated. Studies about the effect of temperature on PhPNPase stability have shown that this enzyme is a quite thermolabile protein; in fact, the Ea of the thermal inactivation reaction in the 30-70°C interval, is 96.7 kJ/mol, a value significantly lower than those observed for other proteins isolated from mesophilic and thermophilic sources. The thermostability of this enzyme has also been investigated by spectroscopic analysis. UV-melting curves have shown a temperature for half-denaturation of 46°C, a value significantly higher than that found for the maximum catalytic activity. These results indicate that the catalitic centre of PhPNPase is less stable of the overall protein structure.
Aye, Armande Mireille. "Mise en évidence du système de communication "Quorum Sensing" impliquant les AHLs chez des bactéries marines isolées de la Méditerranée." Thesis, Toulon, 2015. http://www.theses.fr/2015TOUL0002/document.
Full textThe biofouling control on immersed inert surfaces or in moist atmosphere is a necessity in the marine sector for both economic and environmental reasons. Microbial biofilm formation, the initial step of biofouling development, is intrinsically linked to the communication system “Quorum sensing” (QS). In some Gram negative bacteria, QS is based on the perception of small diffusible signaling molecules called Acyl Homoserine Lactones (AHLs). The inhibition of bacterial QS is part of the different antifouling strategies currently developed. This present work focused on the detection of AHLs molecules involved in this communication system in bacteria isolated from Toulon harbor and the study of modulation of some phenotypes, including biofilm formation, by these molecules as well as the development of a preliminary anti-QS assay. Three marine bacteria isolated from Toulon harbor (TC8, TC14 and TC15), belonging to the Pseudoalteromonas genus, known to synthesize many active molecules, have been tested for their ability to produce AHLs. Only Pseudoalteromonas sp. TC15 produced the C12-HSL. P. ulvae TC14 a violacein-producing and biofilm-forming bacteria, did not secrete any AHLs. Few marine bacteria are used as an anti-QS screening tool, especially by interfering with AHLs with the goal of studying the consequences on biofilm formation. In order to evaluate the possibility to use TC14 with this purpose, exogenous AHLs were tested on the violacein production, the biofilm formation and the motility of TC14. Some AHLs were able to regulate violacein production and biofilm formation suggesting the presence of a functional AHLs receptor in TC14. Preliminary QS inhibition assays were performed with commercial molecules and synthetic analogues. The commercial 3-oxo-C6-HSL as well as esculetin and p-benzoquinone, known to interfere with bacterial QS, were able to inhibit QS and biofilm formation at a non-toxic concentration. Overall, this study suggests that the marine strain P. ulvae TC14 may be used as a tool for the detection of anti-QS molecules in conditions closed to the marine environment. These molecules may subsequently be tested on the biofilm formation of marine bacteria. The long term objective is to find a way to limit biofilm formation, using non-toxic molecules for the environment
Wilmes, Boris [Verfasser]. "Proteomanalyse und Bioprozessentwicklung des psychrophilen, marinen Bakteriums Pseudoalteromonas haloplanktis TAC125 / Boris Wilmes." Greifswald : Universitätsbibliothek Greifswald, 2011. http://d-nb.info/1010980351/34.
Full textJouault, Albane. "Altérocine : une protéine antibiofilm secrétée par la bactérie marine Pseudoalteromonas sp. 3J6." Electronic Thesis or Diss., Lorient, 2019. http://www.theses.fr/2019LORIS588.
Full textThe biofilm lifestyle gives bacteria a protection against antibacterial agents and leads to public health problems that require an alternative to current treatments. The marine bacterium Pseudoalteromonas sp. 3J6 and its exoproducts (SN3J6) display an antibiofilm activity against various bacteria from marine or terrestrial origin. A protein from SN3J6, named alterocin, was partially purified. Although the protein is found in several other Pseudoalteromonas strains, its function remains unknown. In this work, we studied the alterocin. We investigated the protein and gene characteristics at first. The gene alt, coding alterocin, is not part of an operon and several potential promoters were identified. According to our results, its expression seems subject to regulation as it is mainly expressed in stationary phase. It encodes a 139-residue protein with a putative leader peptide, which would allow the secretion of mature alterocin as a 119-residue protein. No sequence homology has been found between alterocin and other proteins of known function in data bases. Anti-alterocin antibodies were produced for an easily detection method. In a second time, we confirmed the antibiofilm activity of alterocin by heterologous production in another Pseudoalteromonas strain and comparing biofilms obtained in the presence of culture supernatants of either this strain or the parental strain. In this work, we showed that the alterocin is a new type of antibiofilm protein whose structure and mechanism of action remain to be elucidated to use it as antibiofilm agent
Egan, Suhelen Microbiology & Immunology UNSW. "Production and regulation of fouling inhibitory compounds by the marine bacterium Pseudoalteromonas tunicata." Awarded by:University of New South Wales. Microbiology and Immunology, 2001. http://handle.unsw.edu.au/1959.4/17838.
Full textStelzer, Sacha Biotechnology & Biomolecular Sciences Faculty of Science UNSW. "WmpR regulation of antifouling compounds and iron uptake in the marine bacterium Pseudoalteromonas tunicata." Awarded by:University of New South Wales. School of Biotechnology and Biomolecular Sciences, 2006. http://handle.unsw.edu.au/1959.4/29354.
Full textTen, Doeschate Kim. "Pseudoalteromonas sp. strain C4 as a probiotic for farmed South African abalone, Haliotis midae." Doctoral thesis, University of Cape Town, 2005. http://hdl.handle.net/11427/4340.
Full textThe objective of this study was to identify a potential probiotic bacterium that increased the growth and decreased the susceptibility of farmed abalone to pathogenic bacterial infection. The mechanism by which the probiotic is able to increase growth rates and reduced susceptibility to pathogen infection was investigated. A number of bacterial strains were isolated from the digestive tract of Haliotis midae that are capable of degrading a wide variety of different polysaccharides (Erasmus, 1996). Strain C4 was selected for further investigation as a result of its ability to degrade alginate since H. midae is predominantly fed a kelp diet of which the major component is alginate.
Book chapters on the topic "Pseudoalteromonas"
Parrilli, Ermenegilda, and Maria Luisa Tutino. "Heterologous Protein Expression in Pseudoalteromonas haloplanktis TAC125." In Psychrophiles: From Biodiversity to Biotechnology, 513–25. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-57057-0_21.
Full textGiuliani, Maria, Ermenegilda Parrilli, Filomena Sannino, Gennaro Apuzzo, Gennaro Marino, and Maria Luisa Tutino. "Soluble Recombinant Protein Production in Pseudoalteromonas haloplanktis TAC125." In Methods in Molecular Biology, 243–57. New York, NY: Springer New York, 2014. http://dx.doi.org/10.1007/978-1-4939-2205-5_13.
Full textRippa, Valentina, Rosanna Papa, Maria Giuliani, Cinzia Pezzella, Ermenegilda Parrilli, Maria Luisa Tutino, Gennaro Marino, and Angela Duilio. "Regulated Recombinant Protein Production in the Antarctic Bacterium Pseudoalteromonas haloplanktis TAC125." In Recombinant Gene Expression, 203–18. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-433-9_10.
Full textParrilli, Ermenegilda, Filomena Sannino, Valeria Citarella, Andrea Colarusso, Annarita Ricciardelli, Gennaro Marino, and Maria Luisa Tutino. "Recombinant Antibody Fragment Production in the Antarctic Marine Bacterium Pseudoalteromonas haloplanktis TAC125." In Microbial Models: From Environmental to Industrial Sustainability, 171–86. Singapore: Springer Singapore, 2016. http://dx.doi.org/10.1007/978-981-10-2555-6_8.
Full textGiuliani, Maria, Ermenegilda Parrilli, Cinzia Pezzella, Valentina Rippa, Angela Duilio, Gennaro Marino, and Maria Luisa Tutino. "A Novel Strategy for the Construction of Genomic Mutants of the Antarctic Bacterium Pseudoalteromonas haloplanktis TAC125." In Recombinant Gene Expression, 219–33. Totowa, NJ: Humana Press, 2011. http://dx.doi.org/10.1007/978-1-61779-433-9_11.
Full textCalvanese, Marzia, Andrea Colarusso, Concetta Lauro, Ermenegilda Parrilli, and Maria Luisa Tutino. "Soluble Recombinant Protein Production in Pseudoalteromonas haloplanktis TAC125: The Case Study of the Full-Length Human CDKL5 Protein." In Methods in Molecular Biology, 219–32. New York, NY: Springer US, 2022. http://dx.doi.org/10.1007/978-1-0716-1859-2_13.
Full textBamford, Dennis H. Bamford Jaana K. H. "Lipid-Containing Bacteriophage PM2, the Type Organism of Corticoviridae." In The Bacteriophages, 171–74. Oxford University PressNew York, NY, 2005. http://dx.doi.org/10.1093/oso/9780195168778.003.0014.
Full textBamford, Dennis H., and Jaana K. H. Bamford. "Lipid-Containing Bacteriophage PM2, the Type Organism of Corticoviridae." In The Bacteriophages, 171–74. Oxford University PressNew York, NY, 2005. http://dx.doi.org/10.1093/oso/9780195148503.003.0014.
Full textPiette, Florence, Caroline Struvay, Amandine Godin, Alexandre Cipolla, and Georges Feller. "Life in the Cold: Proteomics of the Antarctic Bacterium Pseudoalteromonas haloplanktis." In Proteomic Applications in Biology. InTech, 2012. http://dx.doi.org/10.5772/28966.
Full textGiordano, Daniela, Daniela Coppola, Roberta Russo, Mariana Tinajero-Trejo, Guido di Prisco, Federico Lauro, Paolo Ascenzi, and Cinzia Verde. "The Globins of Cold-Adapted Pseudoalteromonas haloplanktis TAC125: From the Structure to the Physiological Functions." In Advances in Microbial Physiology, 329–89. Elsevier, 2013. http://dx.doi.org/10.1016/b978-0-12-407693-8.00008-x.
Full textConference papers on the topic "Pseudoalteromonas"
Iqbal, Faiq, Gires Usup, and Asmat Ahmad. "Anti-biofilm activity of Pseudoalteromonas flavipulchra SktPp1 against Serratia marcescens SMJ-11." In THE 2015 UKM FST POSTGRADUATE COLLOQUIUM: Proceedings of the Universiti Kebangsaan Malaysia, Faculty of Science and Technology 2015 Postgraduate Colloquium. AIP Publishing LLC, 2015. http://dx.doi.org/10.1063/1.4931228.
Full textKristiana, Rhesi, Diah Ayuningrum, Macellyne Yohanna, Dio Dirgantara, Muhammad Hanafi, Ocky Karna Radjasa, Agus Trianto, and Agus Sabdono. "Characterization and identification of antibacterial compound from Pseudoalteromonas piscicida associated with Chromodoris lochi." In INTERNATIONAL CONFERENCE ON BIOLOGY AND APPLIED SCIENCE (ICOBAS). AIP Publishing, 2019. http://dx.doi.org/10.1063/1.5115746.
Full textMa, Jiahao, Guotong Xu, Le Ao, Siqi Chen, and Jingze Liu. "Bioinformatic analysis for structure and function of Glutamine synthetase (GS) from Antarctic sea ice bacterium Pseudoalteromonas." In International Conference on Biomedical and Intelligent Systems (IC-BIS 2022), edited by Ahmed El-Hashash. SPIE, 2022. http://dx.doi.org/10.1117/12.2661100.
Full textWang, Bin, Bin Wang, Baidong Zhang, Baidong Zhang, Yibing Zhou, and Yibing Zhou. "Isolation and Characterization of a Petroleum-Degrading Pseudoalteromonas Haloplanktis Strain from the Digestive Tract of Perinereis Aibuhitensis (Polychaete)." In International Workshop on Environment and Geoscience. SCITEPRESS - Science and Technology Publications, 2018. http://dx.doi.org/10.5220/0007425200240031.
Full textGanguli, Rahul, and Vivek Mehrotra. "Bio Inspired Living Skins for Fouling Mitigation." In ASME 2008 Conference on Smart Materials, Adaptive Structures and Intelligent Systems. ASMEDC, 2008. http://dx.doi.org/10.1115/smasis2008-588.
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