Littérature scientifique sur le sujet « Bacterial proteome »
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Articles de revues sur le sujet "Bacterial proteome"
Tjalsma, Harold, Haike Antelmann, Jan D. H. Jongbloed, Peter G. Braun, Elise Darmon, Ronald Dorenbos, Jean-Yves F. Dubois et al. « Proteomics of Protein Secretion by Bacillus subtilis : Separating the “Secrets” of the Secretome ». Microbiology and Molecular Biology Reviews 68, no 2 (juin 2004) : 207–33. http://dx.doi.org/10.1128/mmbr.68.2.207-233.2004.
Texte intégralTruong, Thuyen, Li Mei Pang, Suhasini Rajan, Sarah Sze Wah Wong, Yi Man Eva Fung, Lakshman Samaranayake et Chaminda Jayampath Seneviratne. « The Proteome of Community Living Candida albicans Is Differentially Modulated by the Morphologic and Structural Features of the Bacterial Cohabitants ». Microorganisms 8, no 10 (7 octobre 2020) : 1541. http://dx.doi.org/10.3390/microorganisms8101541.
Texte intégralMeng, Wenshu, Chenyang Zhao et Youhe Gao. « Comparison of urine proteome among rat models by intraperitoneal injection with single bacteria and co-injection with two bacteria ». PLOS ONE 16, no 12 (31 décembre 2021) : e0261488. http://dx.doi.org/10.1371/journal.pone.0261488.
Texte intégralWang, Liang, Jianye Yang, Yaping Xu, Xue Piao et Jichang Lv. « Domain-based Comparative Analysis of Bacterial Proteomes : Uniqueness, Interactions, and the Dark Matter ». Current Genomics 20, no 2 (22 mai 2019) : 115–23. http://dx.doi.org/10.2174/1389202920666190320134438.
Texte intégralFels, Ursula, Patrick Willems, Margaux De Meyer, Kris Gevaert et Petra Van Damme. « Shift in vacuolar to cytosolic regime of infecting Salmonella from a dual proteome perspective ». PLOS Pathogens 19, no 8 (3 août 2023) : e1011183. http://dx.doi.org/10.1371/journal.ppat.1011183.
Texte intégralJungblut, Peter R. « Proteome analysis of bacterial pathogens ». Microbes and Infection 3, no 10 (août 2001) : 831–40. http://dx.doi.org/10.1016/s1286-4579(01)01441-1.
Texte intégralPappa, Eftychia, Heleni Vastardis, Manousos Makridakis, Jerome Zoidakis, Konstantinos Vougas, George Stamatakis, Martina Samiotaki et Christos Rahiotis. « Analysis of Human and Microbial Salivary Proteomes in Children Offers Insights on the Molecular Pathogenesis of Molar-Incisor Hypomineralization ». Biomedicines 10, no 9 (24 août 2022) : 2061. http://dx.doi.org/10.3390/biomedicines10092061.
Texte intégralMarin, Lina Maria, Yizhi Xiao, Jaime Aparecido Cury et Walter Luiz Siqueira. « Modulation of Streptococcus mutans Adherence to Hydroxyapatite by Engineered Salivary Peptides ». Microorganisms 10, no 2 (20 janvier 2022) : 223. http://dx.doi.org/10.3390/microorganisms10020223.
Texte intégralJabbour, Rabih E., Samir V. Deshpande, Mary Margaret Wade, Michael F. Stanford, Charles H. Wick, Alan W. Zulich, Evan W. Skowronski et A. Peter Snyder. « Double-Blind Characterization of Non-Genome-Sequenced Bacteria by Mass Spectrometry-Based Proteomics ». Applied and Environmental Microbiology 76, no 11 (2 avril 2010) : 3637–44. http://dx.doi.org/10.1128/aem.00055-10.
Texte intégralRohmer, Laurence, Tina Guina, Jinzhi Chen, Byron Gallis, Greg K. Taylor, Scott A. Shaffer, Samuel I. Miller, Mitchell J. Brittnacher et David R. Goodlett. « Determination and Comparison of theFrancisella tularensissubsp.novicidaU112 Proteome to Other Bacterial Proteomes ». Journal of Proteome Research 7, no 5 (2 mai 2008) : 2016–24. http://dx.doi.org/10.1021/pr700760z.
Texte intégralThèses sur le sujet "Bacterial proteome"
Encheva, Vesela. « Proteome analysis of bacterial pathogens ». Thesis, University of East London, 2005. http://roar.uel.ac.uk/1301/.
Texte intégralLalanne, Jean-Benoît. « Multiscale dissection of bacterial proteome optimization ». Thesis, Massachusetts Institute of Technology, 2020. https://hdl.handle.net/1721.1/130217.
Texte intégralCataloged from student-submitted PDF version of thesis.
Includes bibliographical references (pages 315-348).
The quantitative composition of proteomes results from biophysical and biochemical selective pressures acting under system-level resource allocation constraints. The nature and strength of these evolutionary driving forces remain obscure. Through the development of analytical tools and precision measurement platforms spanning biological scales, we found evidence of optimization in bacterial gene expression programs. We compared protein synthesis rates across distant lineages and found tight conservation of in-pathway enzyme expression stoichiometry, suggesting generic selective pressures on expression setpoints. Beyond conservation, we used high-resolution transcriptomics to identify numerous examples of stoichiometry preserving cis-elements compensation in pathway operons. Genome-wide mapping of transcription termination sites also led to the discovery of a phylogenetically widespread mode of bacterial gene expression, 'runaway transcription', whereby RNA polymerases are functionally uncoupled from pioneering ribosomes on mRNAs. To delineate biophysical rationales underlying these pressures, we formulated a parsimonious ribosome allocation model capturing the trade-off between reaction flux and protein production cost. The model correctly predicts the expression hierarchy of key translation factors. We then directly measured the quantitative relationship between expression and fitness for specific translation factors in the Gram-positive species Bacillus subtilis. These precision measurements confirmed that endogenous expression maximizes growth rate. Idiosyncratic transcriptional changes in regulons were however observed away from endogenous expression. The resulting physiological burdens sharpened the fitness landscapes. Spurious system-level responses to targeted expression perturbations, called 'regulatory entrenchment', thus exacerbate the requirement for precisely set expression stoichiometry.
by Jean-Benoît Lalanne.
Ph. D.
Ph.D. Massachusetts Institute of Technology, Department of Physics
Casas, López Mª Vanessa. « Proteome characterization of Brachyspira strains. Identification of bacterial antigens ». Doctoral thesis, Universitat Autònoma de Barcelona, 2017. http://hdl.handle.net/10803/454775.
Texte intégralThe genus Brachyspira includes several pathogenic species affecting pigs, dogs, birds and human. In pigs, Brachyspira (formerly Serpulina and Treponema) hyodysenteriae and Brachyspira pilosicoli are well known intestinal pathogens. These species are flagellated, anaerobic, gram negative spirochetes which inhabit the large intestine and have an intimate association with the colonic mucosa. Brachyspira hyodysenteriae is the causative agent of Swine dysentery, while Brachyspira pilosicoli is associated with Intestinal spirochetosis, a milder, non–haemorrhagic colitis. Swine dysentery is a disease with an important impact on pig production due to the costs associated with mortality, morbidity, inefficient production and medication of the animals. Although the disease can affect animals of all ages, it is rarely detected in piglets younger than three weeks old; occurring more frequently during growing/finishing periods, which aggravates the economic losses. Strategies to treat these diseases rely mainly in the use of antibiotics such as Tiamulin, Valnemulin, Tylosin, Tylvalosin or Lincomycin. Unfortunately, antibiotic resistant strains have been detected for both species in many countries around the world. Despite it is long been known that pigs generate resistance against B. hyodysenteriae after recovering from infection, no vaccine is available yet. The genomes of these species are available since 2009-2010 but proteome information is still scarce. In this work, a large-scale characterization of the proteomes of these pathogens is presented. The work provides experimental evidence of the protein expression profile in these pathogens, including PTMs and SAS and is carried out in the context of the search for potential vaccine candidates. This characterization has been performed through the study of the total proteome, the exposed proteome and the immunoproteome of commercial and environmental strains of these species. - The total proteome was studied through a shotgun proteomics strategy, using a range sofware tools directed to optimize the amount of sequence information extractable from the spectrometric data. In a first stage, spectra were analysed with a combination of six different search engines using the PeptideShaker application. Unmatched spectra were analysed by a combination of de novo and database search engines using the PEAKS application. Unmatched sequence tags after this stage were further BLASTed against Brachyspira and mammals databases. Overall, more than 1500 proteins were identified for each species. The estimated proteome coverage was 67-70%. In addition their PTM profile was described, being methylation the more frequent modification. Specific enrichment allowed identification of 79 and 91 phosphorylation sites and 3221 and 5579 acetylation sites for B. hyodysenteriae and B. pilosicoli, respectively. - The exposed proteome was studied using cell culture supernatants and samples obtained after a controlled enzymatic treatment of intact cells. Among the most abundant exposed proteins are proteins related to movement/chemotaxis, ribosomal proteins, enolase, NADH oxidase and Heat Shock Proteins. - The immunoproteome was characterized immunoblotting the bacterial proteins with sera from challenged pigs. Eleven immunoreactive proteins for B. hyodysenteriae and 8 for B. pilosicoli were identified. Two of these proteins, enolase and PEPCK, were found immunoreactive in the two species.
Wilson, Kimberly M. Wilson. « Characterizing the Impact of Select Bacterial Isolates on Perinatal Pioneer Microbial Colonization and GIT Development ». The Ohio State University, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=osu1531832465230743.
Texte intégralNaujoks, Jan. « Type I and II IFNs modify the proteome of bacterial vacuoles to restrict infections via IRG1 ». Doctoral thesis, Humboldt-Universität zu Berlin, Lebenswissenschaftliche Fakultät, 2015. http://dx.doi.org/10.18452/17367.
Texte intégralThe study presented here systemically examines the innate immune response against L. pneumophila on whole organism level as well as on a molecular level within macrophages, L. pneumophilas’ host cell. In vivo transcriptome analyses identify type I and II interferons (IFNs) as master regulators of the early pulmonary gene expression during L. pneumophila infection. Infection experiments in wild-type mice and mice lacking type I and/or II IFN signaling reveal a severe defect of antibacterial defense when IFN signaling is absent. CD11c+ cells were found to be the main targets of IFNs to restrict infection in the lung, and IFNs inhibited bacterial growth in CD11c+ alveolar macrophages ex vivo. Subcellular quantitative mass spectrometry shows that both IFNs substantially modify the protein composition of Legionella-containing vacuoles. Comparative network analysis, combining these proteome data with transcriptome data as well as public database data reveals distinct subsets of transcriptionally regulated IFN-stimulated genes (ISGs) on the one hand, but interestingly also exclusively spatially IFN-regulated vacuolar proteins. Among IFN-regulated vacuolar proteins, Immunoresponsive gene 1 (IRG1) was identified as a central effector that restricts growth of L. pneumophila through production of the antibacterial metabolite itaconic acid in macrophages. Collectively, this study provides a comprehensive resource of IFN-mediated effects on gene expression and the bacterial vacuolar proteome, and uncovers a cell-autonomous defense pathway against L. pneumophila, which is mediated by IFNs, IRG1 and itaconic acid.
McWilliams, Tracy. « Proteome comparison of helicobacter pylori isolates associated with four disease groups ». Thesis, Curtin University, 2006. http://hdl.handle.net/20.500.11937/1114.
Texte intégralCogo, Karina 1980. « Avaliação in vitro dos efeitos da nicotina e cotinina sobre a expressão de proteinas e capacidade de adesão e invasão de Porphyromonas gingivalis ». [s.n.], 2009. http://repositorio.unicamp.br/jspui/handle/REPOSIP/288971.
Texte intégralTese (doutorado) - Universidade Estadual de Campinas, Faculdade de Odontologia de Piracicaba
Made available in DSpace on 2018-08-12T19:00:41Z (GMT). No. of bitstreams: 1 Cogo_Karina_D.pdf: 3355648 bytes, checksum: d8afd799c6d162cda6cbb9bad9d225a5 (MD5) Previous issue date: 2009
Resumo: O uso do cigarro tem sido associado com a progressão da periodontite bem como com a redução da resposta à terapia aplicada a essa doença. Porphyromonas gingivalis é um importante colonizador do biofilme subgengival além de ser um dos principais patógenos envolvidos no estabelecimento e progressão da doença periodontal. No entanto, os possíveis efeitos dos principais derivados do cigarro sobre P. gingivalis ainda não foram totalmente investigados. Dessa forma, os objetivos deste estudo foram avaliar os efeitos da nicotina e cotinina sobre a expressão de proteínas e sobre a capacidade de adesão e invasão celular de P. gingivalis. A fim de avaliar a expressão de proteínas, culturas de P. gingivalis W83 foram expostas à nicotina e cotinina nas concentrações de 6 e 600µg/mL, as proteínas foram extraídas, separadas por eletroforese bidimensional em gel de poliacrilamida (12.5% SDS-PAGE) e identificadas por LC-MS/MS. Os géis e suas corridas eletroforéticas foram feitas em triplicatas e a detecção de proteínas nos mesmos foi feita através de coloração com corante Coomassie. Proteínas diferentemente expressas foram digeridas com tripsina e as amostras de peptídeos sequenciadas utilizando um sistema Q-TOF API LC-MS/MS. A busca MS/MS foi realizada utilizando os bancos de dados MSDB e NCBI através do programa Mascot. Para examinar a capacidade de adesão e invasão de P. gingivalis, monocamadas de células KB e culturas de P. gingivalis ATCC 33277 foram expostas às concentrações de 0.1, 10 e 100 µg/mL de nicotina e cotinina. As células epiteliais foram incubadas por 24 h enquanto P. gingivalis foi exposta a essas substâncias até atingir a fase logarítmica. Após o período de incubação, P. gingivalis foi submetida aos ensaios de adesão e invasão às células KB. O número de bactérias associadas às células foi obtido através de contagem de unidades formadoras de colônia. Os resultados obtidos da análise expressão de proteínas mostraram que a adição de nicotina e cotinina promoveram alterações no proteoma de P. gingivalis. Entre os ± 430 spots de proteínas reproduzíveis detectados em cada gel, 20 proteínas foram menos expressas e 42 foram mais expressas em pelo menos um dos tratamentos (p<0.05; ANOVA - Tukey). Entre as proteínas identificadas, muitas estavam envolvidas em processos como produção de energia celular, síntese de proteínas, estresse oxidativo, virulência, transporte, etc. Em relação aos resultados obtidos nos ensaios de adesão e invasão, foi evidenciado que, quando as células epiteliais foram inoculadas com nicotina e cotinina, nenhuma diferença significativa na colonização de P. gingivalis foi encontrada. Quando P. gingivalis foi exposta à maior concentração de cotinina, sua capacidade de adesão e invasão às células epiteliais aumentou de forma expressiva (p<0.05; ANOVA - Tukey). No entanto, a nicotina e as outras concentrações de cotinina testadas não alteraram a capacidade de colonização. Esses achados indicam que a nicotina e a cotinina podem afetar a expressão de proteínas de P. gingivalis. Ainda, a cotinina pode alterar positivamente a eficiência de adesão e invasão de P. gingivalis.
Abstract: Cigarette smoking is associated with the development of periodontitis and the decreased response to periodontal therapy. P. gingivalis is an important colonizer of the subgingival biofilm and is one of the major pathogens involved in the initiation and progression of periodontal disease. However, the possible effects of major cigarette's derivatives on P. gingivalis were not fully investigated. Thus, the purpose of the present study was to evaluate the effects of nicotine and cotinine on the protein expression and cellular adhesion and invasion abilities of P. gingivalis. To evaluate protein expression, P. gingivalis W83 cultures were exposed to nicotine and cotinine 6 and 600µg/mL concentrations, the proteins were extracted, separated by two-dimensional polyacrylamide gel electrophoresis (12.5% PAGE) and identified with LC-MS/MS. The gels were run in triplicates and detection of proteins was obtained by staining the gels with Coomassie blue. Proteins differentially expressed were digested with trypsin, and the peptide samples sequenced using a Q-TOF API LC-MS/MS system. The MS/MS was searched against the MSDB and NCBI databank using Mascot program. In order to assess P. gingivalis adhesion and invasion abilities, KB cells monolayers and P. gingivalis ATCC 33277 cultures were exposed to 0.1, 10 and 100 µg/mL nicotine and cotinine concentrations. The epithelial cells were incubated for 24 h while P. gingivalis was exposed to these substances until early logarithmic phase. After incubation period, P. gingivalis were submitted to assays to evaluate adhesion to and invasion of KB cells. The number of bacteria associated with these cells was assessed by counting the colony-forming unities. The results from protein expression analyses showed that addition of nicotine and cotinine promoted alterations in proteome profile of P. gingivalis. Among ± 430 protein spots reproducibly detected on each gel, 20 protein spots were downregulated, and 42 were upregulated at least in one treatment (p<0.05; ANOVA - Tukey test). The identified proteins are involved in several processes, i.e. energy production, protein synthesis, oxidative stress, virulence, transport and binding activities. Data obtained from adhesion and invasion assays evidenced that epithelial cells inoculated with nicotine and cotinine did not show any significant differences in P. gingivalis colonization. When P. gingivalis was exposed to the higher concentration of cotinine, adherence and invasion of this bacterium to the epithelial cells markedly increased (p<0.05; ANOVA - Tukey test). However, nicotine and the other concentrations of cotinine did not alter the colonization ability. These findings indicate that nicotine and cotinine may affect P. gingivalis protein expression. In addition, cotinine may alter positively P. gingivalis adhesion and invasion efficiencies.
Doutorado
Farmacologia, Anestesiologia e Terapeutica
Doutor em Odontologia
Kupper, Maria [Verfasser], Roy [Gutachter] Gross et Heike [Gutachter] Feldhaar. « The immune transcriptome and proteome of the ant Camponotus floridanus and vertical transmission of its bacterial endosymbiont Blochmannia floridanus / Maria Kupper ; Gutachter : Roy Gross, Heike Feldhaar ». Würzburg : Universität Würzburg, 2017. http://d-nb.info/1123505934/34.
Texte intégralNaujoks, Jan Verfasser], Bastian [Akademischer Betreuer] Opitz, Thomas F. [Akademischer Betreuer] [Meyer et Bernd [Akademischer Betreuer] Lepenies. « Type I and II IFNs modify the proteome of bacterial vacuoles to restrict infections via IRG1 / Jan Naujoks. Gutachter : Bastian Opitz ; Thomas F. Meyer ; Bernd Lepenies ». Berlin : Lebenswissenschaftliche Fakultät, 2015. http://d-nb.info/1079901205/34.
Texte intégralNaujoks, Jan [Verfasser], Bastian Akademischer Betreuer] Opitz, Thomas F. [Akademischer Betreuer] [Meyer et Bernd [Akademischer Betreuer] Lepenies. « Type I and II IFNs modify the proteome of bacterial vacuoles to restrict infections via IRG1 / Jan Naujoks. Gutachter : Bastian Opitz ; Thomas F. Meyer ; Bernd Lepenies ». Berlin : Lebenswissenschaftliche Fakultät, 2015. http://d-nb.info/1079901205/34.
Texte intégralLivres sur le sujet "Bacterial proteome"
Leather, Robert Victor. Peptide synthesis mediated by a bacterial high alkaline protease. Birmingham : University of Birmingham, 1991.
Trouver le texte intégralBridge, Paul, David Smith et Erko Stackebrandt, dir. Trends in the systematics of bacteria and fungi. Wallingford : CABI, 2021. http://dx.doi.org/10.1079/9781789244984.0000.
Texte intégralKalbhenn, Eva Maria. Bacterial Adaptive Response to Osmotic Stress. Proteome Alterations. GRIN Verlag GmbH, 2017.
Trouver le texte intégralWilson, Van G. Sumoylation : Molecular Biology and Biochemistry (Horizonbioscience). Taylor & Francis, 2004.
Trouver le texte intégralChapitres de livres sur le sujet "Bacterial proteome"
Raschdorf, Oliver, Dirk Schüler et René Uebe. « Preparation of Bacterial Magnetosomes for Proteome Analysis ». Dans Methods in Molecular Biology, 45–57. New York, NY : Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8695-8_5.
Texte intégralCash, Phillip. « Analyzing Bacterial Pathogenesis at Level of Proteome ». Dans Methods of Biochemical Analysis, 209–35. Hoboken, NJ, USA : John Wiley & Sons, Inc., 2005. http://dx.doi.org/10.1002/0471973165.ch13.
Texte intégralNyström, Thomas. « Oxidation of Bacterial Proteome in Response to Starvation ». Dans Methods of Biochemical Analysis, 89–95. Hoboken, NJ, USA : John Wiley & Sons, Inc., 2005. http://dx.doi.org/10.1002/0471973165.ch7.
Texte intégralSlonczewski, Joan L., et Darcy Blankenhorn. « Acid and Base Regulation in the Proteome of Escherichia Coli ». Dans Novartis Foundation Symposium 221 - Bacterial Responses to pH, 75–92. Chichester, UK : John Wiley & Sons, Ltd., 2007. http://dx.doi.org/10.1002/9780470515631.ch6.
Texte intégralLeontiadou, Fotini, Christina Matragkou, Filippos Kottakis, Dimitrios L. Kalpaxis, Ioannis S. Vizirianakis, Sofia Kouidou, Asterios S. Tsiftsoglou et Theodora Choli-Papadopoulou. « Genetic Engineering of Bacterial and Eukaryotic Ribosomal Proteins for Investigation on Elongation Arrest of Nascent Polypeptides and Cell Differentiation ». Dans Methods in Proteome and Protein Analysis, 251–59. Berlin, Heidelberg : Springer Berlin Heidelberg, 2004. http://dx.doi.org/10.1007/978-3-662-08722-0_16.
Texte intégralCassin, Erin K., et Boo Tseng. « The Matrix Proteome : Protein Actors in the Extracellular Bacterial Biofilm ». Dans Springer Series on Biofilms, 91–130. Cham : Springer Nature Switzerland, 2024. http://dx.doi.org/10.1007/978-3-031-70476-5_3.
Texte intégralZhou, Jianwei, Lu Zhang, Huixia Chuan, Angela Sloan, Raymond Tsang et Keding Cheng. « Mass Spectrometry to Study the Bacterial Proteome from a Single Colony ». Dans Methods in Molecular Biology, 113–21. New York, NY : Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9199-0_10.
Texte intégralBrychta, Martin, et Ivona Pávková. « Proteome Analysis of Bacterial Protein Expression after Ingestion of Microbes by Macrophages ». Dans BSL3 and BSL4 Agents, 223–31. Weinheim, Germany : Wiley-VCH Verlag GmbH & Co. KGaA, 2011. http://dx.doi.org/10.1002/9783527638192.ch19.
Texte intégralNorais, Nathalie, Ignazio Garaguso, Germano Ferrari et Guido Grandi. « In Vitro Transcription and Translation Coupled to Two-Dimensional Electrophoresis for Bacterial Proteome Analysis ». Dans In Vitro Transcription and Translation Protocols, 183–209. Totowa, NJ : Humana Press, 2007. http://dx.doi.org/10.1007/978-1-59745-388-2_10.
Texte intégralKan, Jinjun, Thomas E. Hanson et Feng Chen. « Synchronicity Between Population Structure and Proteome Profiles : A Metaproteomic Analysis of Chesapeake Bay Bacterial Communities ». Dans Handbook of Molecular Microbial Ecology I, 637–44. Hoboken, NJ, USA : John Wiley & Sons, Inc., 2011. http://dx.doi.org/10.1002/9781118010518.ch68.
Texte intégralActes de conférences sur le sujet "Bacterial proteome"
Arias-Rojas, Tatiana, Silvia Mau-Incháustegui, J. J. Saavedra-Arias et Stefany Solano-González. « Computational Proteomic Profiling of Putative Magnetotactic Bacterial Proteins ». Dans 2024 IEEE 6th International Conference on BioInspired Processing (BIP), 1–6. IEEE, 2024. https://doi.org/10.1109/bip63158.2024.10885381.
Texte intégralConstantinescu, Rodica Roxana, Mariana Ferdes, Madalina Ignat, Ciprian Chelaru, Ana-Maria Ciobanu et Denis-Andrei Drusan. « Isolation and Characterization of Bacterial Protease Enzyme of Leather Waste ». Dans The 9th International Conference on Advanced Materials and Systems. INCDTP - Leather and Footwear Research Institute (ICPI), Bucharest, Romania, 2022. http://dx.doi.org/10.24264/icams-2022.ii.6.
Texte intégralToplaghaltsyan, Anna, Zhaneta Karapetyan, Susanna Keleshyan, G. Avetisova, L. Melkonyan, G. Tsarukyan et V. Ghochikyan. « Enzymatic activity of nitrogen-fixing soil bacteria ». Dans 5th International Scientific Conference on Microbial Biotechnology. Institute of Microbiology and Biotechnology, Republic of Moldova, 2022. http://dx.doi.org/10.52757/imb22.37.
Texte intégralBroeseker, T. A., M. D. P. Boyle et R. Lottenberg. « PATHOGENIC BACTERIA HAVE HIGH AFFINITY RECEPTORS SPECIFIC FOR PLASMIN ». Dans XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644391.
Texte intégralEgbring, R., R. Seitz, M. Wolf, L. Lerch et T. Menges. « PROTEINASE-INHIBITOR COMPLEXES (PIC) IN SEPTIC AND NON-SEPTIC SHOCK. COAGULATION ; LEUKOCYTE AND BACTERIAL PROTEASE INHIBITION BY MEANS OF PLASMA-INHIBITOR REPLACEMENT ». Dans XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644244.
Texte intégralTaguchi, Y., et A. Okamoto. « Principal component analysis for bacterial proteomic analysis ». Dans 2011 IEEE International Conference on Bioinformatics and Biomedicine Workshops (BIBMW). IEEE, 2011. http://dx.doi.org/10.1109/bibmw.2011.6112520.
Texte intégralDomnin, P. A., A. S. Kononikhin, V. A. Parfenov, S. A. Ermolaeva et Yu D. Khesuani. « A COMPARATIVE STUDY OF THE IMPACT OF MICROGRAVITY AND MAGNETIC LEVITATION ON ESCHERICHIA COLI PROTEOME ». Dans X Международная конференция молодых ученых : биоинформатиков, биотехнологов, биофизиков, вирусологов и молекулярных биологов — 2023. Novosibirsk State University, 2023. http://dx.doi.org/10.25205/978-5-4437-1526-1-315.
Texte intégralKusumaningtyas, Eni, et Dwi Endrawati. « Determination of protease-producing bacteria for bioactive peptide production ». Dans THE FIRST INTERNATIONAL CONFERENCE ON NEUROSCIENCE AND LEARNING TECHNOLOGY (ICONSATIN 2021). AIP Publishing, 2023. http://dx.doi.org/10.1063/5.0118419.
Texte intégralVeríssimo, Graciete Soares Libório, Ivanize Barbosa De Souza et Paula Carvalhal Lage Von Buettner Ristow. « BIOFILME : MECANISMO DE VIRULÊNCIA BACTERIANA ». Dans II Congresso Brasileiro de Saúde On-line. Revista Multidisciplinar em Saúde, 2021. http://dx.doi.org/10.51161/rems/1503.
Texte intégralJordan, Robert E., Mark Nedelman et Susan H. Tam. « 734 The bacterial IdeS protease as a strategy for tumor regression ». Dans SITC 39th Annual Meeting (SITC 2024) Abstracts, A837. BMJ Publishing Group Ltd, 2024. http://dx.doi.org/10.1136/jitc-2024-sitc2024.0734.
Texte intégralRapports d'organisations sur le sujet "Bacterial proteome"
Ron, Eliora, et Eugene Eugene Nester. Global functional genomics of plant cell transformation by agrobacterium. United States Department of Agriculture, mars 2009. http://dx.doi.org/10.32747/2009.7695860.bard.
Texte intégralManulis, Shulamit, Christine D. Smart, Isaac Barash, Guido Sessa et Harvey C. Hoch. Molecular Interactions of Clavibacter michiganensis subsp. michiganensis with Tomato. United States Department of Agriculture, janvier 2011. http://dx.doi.org/10.32747/2011.7697113.bard.
Texte intégralAltindis, E., R. Cozzi, B. Di Palo, F. Necchi, R. P. Mishra, M. R. Fontana, M. Soriani et al. Protectome analysis : a new selective bioinformatics tool for bacterial vaccine candidate discovery. Cold Spring Harbor Laboratory, janvier 2014. http://dx.doi.org/10.1101/002089.
Texte intégralSplitter, Gary A., Menachem Banai et Jerome S. Harms. Brucella second messenger coordinates stages of infection. United States Department of Agriculture, janvier 2011. http://dx.doi.org/10.32747/2011.7699864.bard.
Texte intégralAdam, Zach, et Eran Pichersky. Degradation of Abnormal Proteins in Chloroplasts of Higher Plants. United States Department of Agriculture, août 1994. http://dx.doi.org/10.32747/1994.7568768.bard.
Texte intégralSessa, Guido, et Gregory Martin. A functional genomics approach to dissect resistance of tomato to bacterial spot disease. United States Department of Agriculture, janvier 2004. http://dx.doi.org/10.32747/2004.7695876.bard.
Texte intégralChen, Junping, Zach Adam et Arie Admon. The Role of FtsH11 Protease in Chloroplast Biogenesis and Maintenance at Elevated Temperatures in Model and Crop Plants. United States Department of Agriculture, mai 2013. http://dx.doi.org/10.32747/2013.7699845.bard.
Texte intégralGafni, Yedidya, Moshe Lapidot et Vitaly Citovsky. Dual role of the TYLCV protein V2 in suppressing the host plant defense. United States Department of Agriculture, janvier 2013. http://dx.doi.org/10.32747/2013.7597935.bard.
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