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Artykuły w czasopismach na temat "Outer membrane protein"
Hazlett, Karsten R. O., David L. Cox, Marc Decaffmeyer, Michael P. Bennett, Daniel C. Desrosiers, Carson J. La Vake, Morgan E. La Vake i in. "TP0453, a Concealed Outer Membrane Protein of Treponema pallidum, Enhances Membrane Permeability". Journal of Bacteriology 187, nr 18 (15.09.2005): 6499–508. http://dx.doi.org/10.1128/jb.187.18.6499-6508.2005.
Pełny tekst źródłaIshikawa, Daigo, Hayashi Yamamoto, Yasushi Tamura, Kaori Moritoh i Toshiya Endo. "Two novel proteins in the mitochondrial outer membrane mediate β-barrel protein assembly". Journal of Cell Biology 166, nr 5 (23.08.2004): 621–27. http://dx.doi.org/10.1083/jcb.200405138.
Pełny tekst źródłaMayer, A., R. Lill i W. Neupert. "Translocation and insertion of precursor proteins into isolated outer membranes of mitochondria." Journal of Cell Biology 121, nr 6 (15.06.1993): 1233–43. http://dx.doi.org/10.1083/jcb.121.6.1233.
Pełny tekst źródłaDhar, Rik, i Joanna SG Slusky. "Outer membrane protein evolution". Current Opinion in Structural Biology 68 (czerwiec 2021): 122–28. http://dx.doi.org/10.1016/j.sbi.2021.01.002.
Pełny tekst źródłaSlusky, Joanna SG. "Outer membrane protein design". Current Opinion in Structural Biology 45 (sierpień 2017): 45–52. http://dx.doi.org/10.1016/j.sbi.2016.11.003.
Pełny tekst źródłaMurcha, Monika W., Dina Elhafez, A. Harvey Millar i James Whelan. "The C-terminal Region of TIM17 Links the Outer and Inner Mitochondrial Membranes inArabidopsisand Is Essential for Protein Import". Journal of Biological Chemistry 280, nr 16 (18.02.2005): 16476–83. http://dx.doi.org/10.1074/jbc.m413299200.
Pełny tekst źródłaHoffmann, Juliane J., i Thomas Becker. "Crosstalk between Mitochondrial Protein Import and Lipids". International Journal of Molecular Sciences 23, nr 9 (9.05.2022): 5274. http://dx.doi.org/10.3390/ijms23095274.
Pełny tekst źródłaCourt, Deborah A., Roland Lill i Walter Neupert. "The protein import apparatus of the mitochondrial outer membrane". Canadian Journal of Botany 73, S1 (31.12.1995): 193–97. http://dx.doi.org/10.1139/b95-245.
Pełny tekst źródłaPon, L., T. Moll, D. Vestweber, B. Marshallsay i G. Schatz. "Protein import into mitochondria: ATP-dependent protein translocation activity in a submitochondrial fraction enriched in membrane contact sites and specific proteins." Journal of Cell Biology 109, nr 6 (1.12.1989): 2603–16. http://dx.doi.org/10.1083/jcb.109.6.2603.
Pełny tekst źródłaBraun, Volkmar. "The Outer Membrane Took Center Stage". Annual Review of Microbiology 72, nr 1 (8.09.2018): 1–24. http://dx.doi.org/10.1146/annurev-micro-090817-062156.
Pełny tekst źródłaRozprawy doktorskie na temat "Outer membrane protein"
Barlow, Ann Katherine. "Neisseria meningitidis : the class 1 outer membrane protein". Thesis, University of Southampton, 1989. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.280415.
Pełny tekst źródłaMcBride, Heidi May. "Protein import into and across the mitochondrial outer membrane". Thesis, McGill University, 1996. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=40395.
Pełny tekst źródłaConsistent with this model, the signal-anchor sequence of the outer membrane protein yTom70 is also capable of importing into the inner membrane of mitochondria when the outer membrane is selectively removed. Import into the inner membrane requires the presence of an electrochemical potential across the lipid bilayer. Import proceeds in the absence of $ Delta Psi$ only when constructs are used which lack the positively-charged amino terminal region of the signal-anchor sequence. These results suggest that the positively-charged presequence leads the transmembrane domain into the import machinery and that $ Delta Psi$ is required to clear this region in order that the distal transmembrane region can enter the translocation pathway.
The charged N-terminal 10 residues of yTom70 are incapable of directing import into intact mammalian mitochondria, however, are able to efficiently direct import into the matrix of yeast mitochondria or mammalian mitoplasts. This potentially cryptic signal is excluded from intact mammalian mitochondria due to the presence of the receptor protein Tom20, since replacement of yeast Tom20 with mammalian Tom20 confers the mammalian phenotype onto yeast. These results suggest that receptor proteins may also have the ability to screen potentially cryptic signals from distal components of the outer and inner membrane translocation machinery.
See, Sarah Bihui. "Outer membrane protein immunity to Pasteurella pneumotropica and the interaction of allergy". University of Western Australia. School of Paediatrics and Child Health, 2010. http://theses.library.uwa.edu.au/adt-WU2010.0103.
Pełny tekst źródłaJuodeikis, Rokas. "Engineering membranes in Escherichia coli : the magnetosome, LemA protein family and outer membrane vesicles". Thesis, University of Kent, 2016. https://kar.kent.ac.uk/61062/.
Pełny tekst źródłaMenon, Sailesh. "Characterization of a Fusobacterium necrophorum subspecies necrophorum outer membrane protein". Kansas State University, 2014. http://hdl.handle.net/2097/18128.
Pełny tekst źródłaDepartment of Biomedical Sciences
Sanjeev K. Narayanan
Fusobacterium necrophorum is an anaerobic Gram-negative non spore forming rod shaped bacteria that is a normal inhabitant of the alimentary tract of humans and animals. Two subspecies of F. necrophorum have been recognized- subspecies necrophorum and subspecies funduliforme. Subspecies necrophorum is an opportunistic pathogen in animals causing diseases such as bovine hepatic abscesses and sheep foot rot while as subspecies funduliforme is linked with human oral and hepatic infections such as sore throats, Lemierre’s syndrome and hepatic abscesses. The pathogenic mechanisms of F. necrophorum are complex and are not well understood or defined. Several virulence factors such as leukotoxin, haemolysin, haemagglutinin and adhesin have been described. One of the most important factors in F. necrophorum bacterial pathogenesis is the adhesion of the bacteria to the host cell. The adhesion of the bacteria to the host cell helps it colonize the host tissue and this is followed by intracellular multiplication with dissemination to other tissues, which could ultimately lead to septicemia and death. Bacteria use adhesins which are proteins found in the outer membrane which help them bind with host receptors and this helps with the adhesion of the bacteria to the host cell. Not much is known about F. necrophorum adhesins. Here, we describe and characterize a novel adhesin.
Shand, Geoffrey H. "Antibiotic resistance and outer membrane protein antigens of Pseudomonas aeruginosa". Thesis, Aston University, 1985. http://publications.aston.ac.uk/12475/.
Pełny tekst źródłaKaye, Elena Cortizas. "The Function of Outer Membrane Protein A (OmpA) in Yersinia pestis". Scholarly Repository, 2010. http://scholarlyrepository.miami.edu/oa_theses/58.
Pełny tekst źródłaFerris, Shirley. "Antibody responses to the major outer membrane protein of Chlamydia trachomatis". Thesis, University of Southampton, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.295880.
Pełny tekst źródłaSchiffrin, Robert. "Roles of periplasmic chaperones and BamA in outer membrane protein folding". Thesis, University of Leeds, 2016. http://etheses.whiterose.ac.uk/15952/.
Pełny tekst źródłaHuysmans, Gerard Herman Marleen. "On the folding mechanism of the bacterial outer membrane protein PagP". Thesis, University of Leeds, 2008. http://etheses.whiterose.ac.uk/6752/.
Pełny tekst źródłaKsiążki na temat "Outer membrane protein"
Shand, Geoffrey Harold. Antibiotic resistance and outer membrane protein antigens of Pseudomonas aeruginasa. Birmingham: University of Aston. Department of Pharmaceutical Sciences, 1985.
Znajdź pełny tekst źródłaKraak, Wilma A. G. Outer membrane protein typing of Haemophilus influenzae: An epidemiological tool in type b and non-encapsulated strains. Oxford: Oxford Polytechnic, 1990.
Znajdź pełny tekst źródłaSun, Frank. Identification of Porphyromonas (Bacteroides) Gingivalis outer membrane proteins that bind to and degrade human matrix proteins. [Toronto: Faculty of Dentistry, University of Toronto, 1992.
Znajdź pełny tekst źródłaMortimer, Peter G. S. The role of Esherichia coli outer membrane proteins in determining the accumulation of and susceptibility to antibiotics. Birmingham: University of Birmingham, 1991.
Znajdź pełny tekst źródłaMaciver, Isobel. The effect of haem limitation and iron restriction on outer membrane proteins and on respiratory systems of non typable Haemophilus influenzae. Birmingham: Aston University. Department of Pharmaceutical Sciences, 1989.
Znajdź pełny tekst źródłaCharacterization of the maltose regulon of Vibrio cholerae: Involvement of maltose in production of outer membrane proteins and secretion of virulence factors. Uppsala: Swedish University of Agricultural Sciences, Dept. of Molecular Genetics, Uppsala Genetic Center, 1993.
Znajdź pełny tekst źródłaKania, Stephen Anthony. Isolation and characterization of a 78,000 dalton outer membrane protein of Haemophilus somnus. 1987.
Znajdź pełny tekst źródłaThe 2.05 Å crystal structure of LptB, an essential protein in gram-negative bacterial outer membrane biogenesis. 2011.
Znajdź pełny tekst źródłaStructural and Functional Relationships in Prokaryotes. Springer, 2004.
Znajdź pełny tekst źródłaBarton, Larry L. Structural and Functional Relationships in Prokaryotes. Springer London, Limited, 2005.
Znajdź pełny tekst źródłaCzęści książek na temat "Outer membrane protein"
Poolman, J. "Outer Membrane Protein Vaccines". W Vaccines, 225–48. Berlin, Heidelberg: Springer Berlin Heidelberg, 1999. http://dx.doi.org/10.1007/978-3-642-59955-2_9.
Pełny tekst źródłaNanda, Vikas, Daniel Hsieh i Alexander Davis. "Prediction and Design of Outer Membrane Protein–Protein Interactions". W Membrane Proteins, 183–96. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-583-5_10.
Pełny tekst źródłaTommassen, Jan, i Romé Voulhoux. "Biogenesis of Outer Membrane Proteins". W Protein Secretion Pathways in Bacteria, 83–97. Dordrecht: Springer Netherlands, 2003. http://dx.doi.org/10.1007/978-94-010-0095-6_5.
Pełny tekst źródłaPoolman, Jan T. "Bacterial Outer Membrane Protein Vaccines". W Advances in Experimental Medicine and Biology, 73–77. Boston, MA: Springer US, 1996. http://dx.doi.org/10.1007/978-1-4899-1382-1_11.
Pełny tekst źródłaCecil, Jessica D., Natalie Sirisaengtaksin, NEIL M. O'BRIEN-SIMPSON i Anne Marie Krachler. "Outer Membrane Vesicle-Host Cell Interactions". W Protein Secretion in Bacteria, 201–14. Washington, DC, USA: ASM Press, 2019. http://dx.doi.org/10.1128/9781683670285.ch17.
Pełny tekst źródłaMillar, D. G., i G. C. Shore. "Protein Insertion Into The Outer Mitochondrial Membrane". W Molecular Mechanisms of Membrane Traffic, 105–6. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-662-02928-2_21.
Pełny tekst źródłaGrabowicz, Marcin. "Lipoproteins and Their Trafficking to the Outer Membrane". W Protein Secretion in Bacteria, 67–76. Washington, DC, USA: ASM Press, 2019. http://dx.doi.org/10.1128/9781683670285.ch6.
Pełny tekst źródłaTu, Shuh-Long, i Hsou-min Li. "Protein Targeting to the Chloroplast Outer Membrane". W Photosynthesis: Mechanisms and Effects, 3069–73. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-3953-3_719.
Pełny tekst źródłaHeckels, J. E., M. Virji, K. Zak i J. N. Fletcher. "Immunobiology of gonococcal outer membrane protein I". W Gonococci and Meningococci, 369–71. Dordrecht: Springer Netherlands, 1988. http://dx.doi.org/10.1007/978-94-009-1383-7_60.
Pełny tekst źródłaRicci, Dante P., i Thomas J. Silhavy. "Outer Membrane Protein Insertion by the β-barrel Assembly Machine". W Protein Secretion in Bacteria, 91–101. Washington, DC, USA: ASM Press, 2019. http://dx.doi.org/10.1128/9781683670285.ch8.
Pełny tekst źródłaStreszczenia konferencji na temat "Outer membrane protein"
Wilkinson, J. M., N. Hack, L. I. Thorsen i J. A. Thomas. "MONOCLONAL ANTIBODIES RECOGNISING PROTEINS OF THE OUTER AND INNER SURFACE OF THE PLATELET PLASMA MEMBRANE". W XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644493.
Pełny tekst źródłaHarasztosi, Csaba, Emese Harasztosi i Anthony W. Gummer. "Membrane recycling at the infranuclear pole of the outer hair cell". W MECHANICS OF HEARING: PROTEIN TO PERCEPTION: Proceedings of the 12th International Workshop on the Mechanics of Hearing. AIP Publishing LLC, 2015. http://dx.doi.org/10.1063/1.4939332.
Pełny tekst źródłaPires, Inês, i Miguel Machuqueiro. "pH-dependent permeability of outer membrane protein G: an in silico study". W MOL2NET 2018, International Conference on Multidisciplinary Sciences, 4th edition. Basel, Switzerland: MDPI, 2018. http://dx.doi.org/10.3390/mol2net-04-06077.
Pełny tekst źródłaVoigt, W., W. Rabsch i H. Tschäpe. "Differences in the outer membrane protein pattern of Salmonella typhimurium DT8, DT10 and DT104 strains". W Fourth International Symposium on the Epidemiology and Control of Salmonella and Other Food Borne Pathogens in Pork. Iowa State University, Digital Press, 2001. http://dx.doi.org/10.31274/safepork-180809-201.
Pełny tekst źródłaShen, Dandan, Anchun Cheng i Mingshu Wang. "Analysis of synonymous codon usage in the outer membrane efflux protein gene of Riemerella anatipestifer". W 2012 5th International Conference on Biomedical Engineering and Informatics (BMEI). IEEE, 2012. http://dx.doi.org/10.1109/bmei.2012.6513098.
Pełny tekst źródłaHandayani, Tri, Dadang Priyoatmojo i Afi Candra Trinugraha. "Outer Membrane Protein (OMP) Profiles of Brucella abortus Local Isolate by SDS-PAGE Procedure". W International Conference on Improving Tropical Animal Production for Food Security (ITAPS 2021). Paris, France: Atlantis Press, 2022. http://dx.doi.org/10.2991/absr.k.220309.006.
Pełny tekst źródłaSalamon, Zdzislaw, Gordon Tollin, Angus Macleod i Ian C. Stevenson. "Spectroscopic studies of membrane protein-lipid bilayer systems deposited on multilayer thin film coatings". W Optical Interference Coatings. Washington, D.C.: Optica Publishing Group, 1997. http://dx.doi.org/10.1364/oic.1998.thd.1.
Pełny tekst źródłaMcBride, S., M. Ferguson, M. Kelly, K. Hawley, A. Luthra, H. Driscoll, J. Montezuma-Rusca i in. "P401 Development and Utilization of Antibodies Specific for Extracellular Loops of the Treponema pallidum outer membrane protein BamA (TP0326)". W Abstracts for the STI & HIV World Congress, July 14–17 2021. BMJ Publishing Group Ltd, 2021. http://dx.doi.org/10.1136/sextrans-2021-sti.431.
Pełny tekst źródła"Evaluation of 36 KDa Outer Membrane Protein (OMP’s) by Latex Dri-dot of Salmonella Enterica Serovar Typhi For The Diagnosis Of Typhoid Fever". W April 17-18, 2018 Kyoto (Japan). International Institute of Chemical, Biological and Environmental Engineering, 2018. http://dx.doi.org/10.17758/iicbe1.c0418154.
Pełny tekst źródłaSoares, T. A., T. P. Straatsma, Theodore E. Simos i George Maroulis. "Towards Simulations of Outer Membrane Proteins in Lipopolysaccharide Membranes". W COMPUTATIONAL METHODS IN SCIENCE AND ENGINEERING: Theory and Computation: Old Problems and New Challenges. Lectures Presented at the International Conference on Computational Methods in Science and Engineering 2007 (ICCMSE 2007): VOLUME 1. AIP, 2007. http://dx.doi.org/10.1063/1.2836008.
Pełny tekst źródłaRaporty organizacyjne na temat "Outer membrane protein"
Walian, P. J. Electron crystallography of PhoE porin, an outer membrane, channel- forming protein from E. coli. Office of Scientific and Technical Information (OSTI), listopad 1989. http://dx.doi.org/10.2172/6365889.
Pełny tekst źródłaPalmer, Guy H., Eugene Pipano, Terry F. McElwain, Varda Shkap i Donald P. Knowles, Jr. Development of a Multivalent ISCOM Vaccine against Anaplasmosis. United States Department of Agriculture, lipiec 1993. http://dx.doi.org/10.32747/1993.7568763.bard.
Pełny tekst źródłaElbaum, Michael, i Peter J. Christie. Type IV Secretion System of Agrobacterium tumefaciens: Components and Structures. United States Department of Agriculture, marzec 2013. http://dx.doi.org/10.32747/2013.7699848.bard.
Pełny tekst źródłaDunn, Bruce E., Martin J. Blaser i Edward L. Snyder. Two-Dimensional Gel Electrophoresis and Immunoblotting of Campylobacter Outer Membrane Proteins. Fort Belvoir, VA: Defense Technical Information Center, kwiecień 1987. http://dx.doi.org/10.21236/ada265461.
Pełny tekst źródłaBlaser, Martin J. Studies of the Outer Membrane Proteins of Campylobacter Jejuni for Vaccine Development. Fort Belvoir, VA: Defense Technical Information Center, listopad 1991. http://dx.doi.org/10.21236/ada245442.
Pełny tekst źródłaBrayton, Kelly A., Varda Shkap, Guy H. Palmer, Wendy C. Brown i Thea Molad. Control of Bovine Anaplasmosis: Protective Capacity of the MSP2 Allelic Repertoire. United States Department of Agriculture, styczeń 2014. http://dx.doi.org/10.32747/2014.7699838.bard.
Pełny tekst źródłaSplitter, Gary, i Menachem Banai. Microarray Analysis of Brucella melitensis Pathogenesis. United States Department of Agriculture, 2006. http://dx.doi.org/10.32747/2006.7709884.bard.
Pełny tekst źródłaEldar, Avigdor, i Donald L. Evans. Streptococcus iniae Infections in Trout and Tilapia: Host-Pathogen Interactions, the Immune Response Toward the Pathogen and Vaccine Formulation. United States Department of Agriculture, grudzień 2000. http://dx.doi.org/10.32747/2000.7575286.bard.
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