Littérature scientifique sur le sujet « Protease encoding genes »
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Articles de revues sur le sujet "Protease encoding genes"
Xavier-Filho, J., et F. A. Paiva Campos. « Genes encoding protease inhibitors ». Plant Molecular Biology Reporter 12, no 2 (juin 1994) : S58—S59. http://dx.doi.org/10.1007/bf02671572.
Texte intégralReid, Vernita J., Louwrens W. Theron, Maret du Toit et Benoit Divol. « Identification and Partial Characterization of Extracellular Aspartic Protease Genes from Metschnikowia pulcherrima IWBT Y1123 and Candida apicola IWBT Y1384 ». Applied and Environmental Microbiology 78, no 19 (20 juillet 2012) : 6838–49. http://dx.doi.org/10.1128/aem.00505-12.
Texte intégralAkula, Srinivas, Zhirong Fu, Sara Wernersson et Lars Hellman. « The Evolutionary History of the Chymase Locus -a Locus Encoding Several of the Major Hematopoietic Serine Proteases ». International Journal of Molecular Sciences 22, no 20 (11 octobre 2021) : 10975. http://dx.doi.org/10.3390/ijms222010975.
Texte intégralLewis, Janina P., Divya Iyer et Cecilia Anaya-Bergman. « Adaptation of Porphyromonas gingivalis to microaerophilic conditions involves increased consumption of formate and reduced utilization of lactate ». Microbiology 155, no 11 (1 novembre 2009) : 3758–74. http://dx.doi.org/10.1099/mic.0.027953-0.
Texte intégralLundwall, Åke, et Adam Clauss. « Genes encoding WFDC- and Kunitz-type protease inhibitor domains : are they related ? » Biochemical Society Transactions 39, no 5 (21 septembre 2011) : 1398–402. http://dx.doi.org/10.1042/bst0391398.
Texte intégralBasta, David W., David Angeles-Albores, Melanie A. Spero, John A. Ciemniecki et Dianne K. Newman. « Heat-shock proteases promote survival of Pseudomonas aeruginosa during growth arrest ». Proceedings of the National Academy of Sciences 117, no 8 (6 février 2020) : 4358–67. http://dx.doi.org/10.1073/pnas.1912082117.
Texte intégralBidochka, Michael J., et Michael J. Melzer. « Genetic polymorphisms in three subtilisin-like protease isoforms (Pr1A, Pr1B, and Pr1C) from Metarhizium strains ». Canadian Journal of Microbiology 46, no 12 (1 décembre 2000) : 1138–44. http://dx.doi.org/10.1139/w00-112.
Texte intégralLewis, Janina P., et Francis L. Macrina. « IS195, an Insertion Sequence-Like Element Associated with Protease Genes in Porphyromonas gingivalis ». Infection and Immunity 66, no 7 (1 juillet 1998) : 3035–42. http://dx.doi.org/10.1128/iai.66.7.3035-3042.1998.
Texte intégralGARNIER, Gérard, Antonella CIRCOLO, Yuanyuan XU et John E. VOLANAKIS. « Complement C1r and C1s genes are duplicated in the mouse : differential expression generates alternative isomorphs in the liver and in the male reproductive system ». Biochemical Journal 371, no 2 (15 avril 2003) : 631–40. http://dx.doi.org/10.1042/bj20021555.
Texte intégralHeusel, JW, EM Scarpati, NA Jenkins, DJ Gilbert, NG Copeland, SD Shapiro et TJ Ley. « Molecular cloning, chromosomal location, and tissue-specific expression of the murine cathepsin G gene ». Blood 81, no 6 (15 mars 1993) : 1614–23. http://dx.doi.org/10.1182/blood.v81.6.1614.1614.
Texte intégralThèses sur le sujet "Protease encoding genes"
Camilleri, Raymond Stephen. « Molecular genetic and biochemical studies of the D1-processing protease of Arabidopsis Thaliana ». Thesis, Royal Holloway, University of London, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.322223.
Texte intégralMatsebula, Aaron Mfanuzile. « Cloning and expression of a chimeric protease inhibitor encoding gene in Escherichia coli and Pichia pastoris ». Master's thesis, University of Cape Town, 1996. http://hdl.handle.net/11427/9649.
Texte intégralSquash family protease inhibitors are small peptides of 27-32 residues, hence they are ideal subjects for structure-function studies. Their small size is within the reach of peptide chemical synthesis, which enables one to produce enough peptide material for experimental purposes within a reasonable time frame.
Rawat, Reetika. « Characterization of the promoter of SmCP, the gene encoding Solanum melongena cysteine proteinase ». Thesis, Click to view the E-thesis via HKUTO, 2004. http://sunzi.lib.hku.hk/hkuto/record/B34740156.
Texte intégralLugli, Elena. « Analysis of a multi-gene family, PRT1. encoding subtilism-like serine proteases in Pneumocystis carinii ». Thesis, University of Oxford, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.302531.
Texte intégralMa, Pei-yin. « Chemical synthesis, cloning and expression of a gene encoding systemin, a proteinase inhibitor-inducing factor ». Master's thesis, University of Cape Town, 1996. http://hdl.handle.net/11427/9241.
Texte intégralWound-inducible proteinase inhibitors in plants elicit a defence mechanism by inactivating the proteinases of insects. This triggers a feedback mechanism causing overproduction of digestive enzymes together with a decrease in appetite, leading to starvation. System in, a polypeptide proteinase inhibitor-inducing factor, when applied to cut stems of young tomato plants induces the accumulation of inhibitors in a manner similar to the normal wounding response. We designed and synthesised the minus strand oligonucleotide template complementary to the system in DNA sequence using Escherichia coli codon preferences. The double stranded fragment encoding the 18 amino acid residue systemin was cloned into pUCJ 8 for amplification and subcloning into pMAL-pk for expression as a maltose binding-fusion protein. The recombinant systemin was released by enterokinase and isolated by HPLC. After further purification, the physical characteristics including amino acid composition, peptide sequence and molecular weight of r-systemin were determined. When the recombinant peptide was applied to young tomato plants, it induced the accumulation of proteinase inhibitor I messenger RNA.
BARANIYA, DIVYASHRI. « Microbial protease encoding genes in soil : diversity, abundance and enzymatic activity ». Doctoral thesis, 2016. http://hdl.handle.net/2158/1040253.
Texte intégralSu, Xun Zheng, et 蘇訓正. « Cloning and sequence analysis of the gene encoding the protease of vibrio parahaemolyticus ». Thesis, 1994. http://ndltd.ncl.edu.tw/handle/85027532088389443602.
Texte intégralYu, Mei Xuan, et 余美萱. « Expression and characterization of the gene encoding the extracellular protease of vibrio parahemolyticus ». Thesis, 1995. http://ndltd.ncl.edu.tw/handle/41066787887294982987.
Texte intégralLin, Tzu-Jay, et 林子傑. « Characterization and sequences analysis on the gene prtS1 encoding serine protease of Aeromonas hydrophila ». Thesis, 2000. http://ndltd.ncl.edu.tw/handle/78571215317033041633.
Texte intégral國立臺灣大學
農業化學研究所
88
Aeromonas hydrophila and related aeromonads are gram negative, facultatively anaerobic fresh water bacteria, many strains of which are pathogens of humans and animals. The pathogenicity may involve with several extracellular enzymes including haemolysins, lipase, and protease. It has been suggested that proteolytic enzymes produced by A. hydrophila may play an important role in invasiveness and in establishment of infection by such as overcoming initial host defense and providing nutrients for cell proliferation. During further study, we have cloned and sequenced a proteolytic gene prtS1 from clinical strain A. hydrophila CKH29. In this study we characterized the gene product of prtS1. prtS1 can be translated into a 453 a.a. protein which displays high homology with E. coli HtrA/DegQ/DegS family. PrtS1 was overexpressed in E.coli with a multicopy plasmid pUC18, after expression, it can be translocated into periplasma by postulated recognition of E. coli leader peptidase, but most gene product remained in cytosol after translation. Purification of PrtS1 was proceeded by ammonium sulfate precipitation, following of ion-exchge and gel filtration fractionation. The molecular weight of PrtS1 was estimated as 45 kD and 41 kD by SDS PAGE and 378 kD by CL-6B elution analysis, according to these results, it is predicted that PrtS1 can form an octomer by oligomerization after protein synthesized and achieved most proteolytic activity. The PrtS1 protein was shown to be a specific endopeptidase could be inhibited by PMSF, it showed high temperature stability, suggesting that PrtS1 is a thermostable serine protease. The optimal reaction pH and temperature with casein as substrate was pH 8.0 and 45℃. Inorganic ion Zn2+ showed inhibition to proteolytic activity of PrtS1, in contrast, the activity of PrtS1 was increased by Mg2+and Ca2+. Towards the N-termial near middle of PrtS1 amino sequences shows serine protease catalytic triad and GNSGGAL motif, PrtS1 may involve putative PDZ domains behind the catalytic domain, which may in response to its multi-function.
Chapitres de livres sur le sujet "Protease encoding genes"
Mulks, M. H., D. A. Simpson et R. J. Shoberg. « Restriction site polymorphism in genes encoding type 2 but not type 1 gonococcal IgAl proteases ». Dans Gonococci and Meningococci, 419–26. Dordrecht : Springer Netherlands, 1988. http://dx.doi.org/10.1007/978-94-009-1383-7_67.
Texte intégralHershberger, R. J., C. Mueller, H. K. Gershenfeld et I. L. Weissman. « A Serine Protease-Encoding Gene That Marks Activated Cytotoxic T Cells In Vivo and In Vitro ». Dans Current Topics in Microbiology and Immunology, 81–92. Berlin, Heidelberg : Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-73911-8_7.
Texte intégralSama, Babru, Tom Boone, Barbara Karan, Kenneth Chen, Raj Sachdev et Tsutomo Arakawa. « Cloning and Expression of the Gene Encoding a Novel Proteinase from TritiraChium Album Limber ». Dans Advances in Experimental Medicine and Biology, 95–104. Boston, MA : Springer US, 1996. http://dx.doi.org/10.1007/978-1-4613-0319-0_10.
Texte intégralTakeuchi, M., K. Ogura, T. Hamamoto et Y. Kobayashi. « Molecular Cloning and Sequence Analysis of a Gene Encoding an Aspartic Proteinase from Aspergillus Oryzae ». Dans Aspartic Proteinases, 577–80. Boston, MA : Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1871-6_77.
Texte intégralJayagoudar, Santoshkumar, Ch Ramesh, Pradeep Kumar, Aditya Banyal, Bhagwan Rekadwad, Ramchander Merugu, Tiina Nõges et Rahul Kumar. « Thermophilic Fungi and their Applications in Biotechnology ». Dans Mycology : Current and Future Developments, 359–83. BENTHAM SCIENCE PUBLISHERS, 2022. http://dx.doi.org/10.2174/9789815040340122040023.
Texte intégralA. Elkonin, Lev, Valery M. Panin, Odissey A. Kenzhegulov et Saule Kh. Sarsenova. « RNAi-Mutants of Sorghum bicolor (L.) Moench with Improved Digestibility of Seed Storage Proteins ». Dans Grain and Seed Proteins Functionality [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.96204.
Texte intégralGrant, Seth G. N. « Synaptic Disease in Psychiatry ». Dans Neurobiology of Mental Illness, sous la direction de Pamela Sklar, 311–21. Oxford University Press, 2013. http://dx.doi.org/10.1093/med/9780199934959.003.0024.
Texte intégralPrimrose, Sandy B. « Tracking Horizontal Gene Transfer : Staphylococcus aureus ». Dans Microbiology of Infectious Disease, 124–32. Oxford University Press, 2022. http://dx.doi.org/10.1093/oso/9780192863843.003.0016.
Texte intégralI. Kane, Emma, et Donald E. Spratt. « New Discoveries on the Roles of “Other” HECT E3 Ubiquitin Ligases in Disease Development ». Dans Ubiquitin - Proteasome Pathway. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.91770.
Texte intégralRavichandiran, Nerethika, Muneesh Kumar Barman, Sai Tejaswi Lavuri, Manjita Srivastava, Shalini Sakthivel, Meenakshi Singh, Kailash Chand, Subash C. Sonkar et Prudhvilal Bhukya. « Precision Medicine in Cancer ». Dans Handbook of Research on Advancements in Cancer Therapeutics, 433–66. IGI Global, 2021. http://dx.doi.org/10.4018/978-1-7998-6530-8.ch015.
Texte intégralActes de conférences sur le sujet "Protease encoding genes"
Pannekoek, H., M. Linders, J. Keijer, H. Veerman, H. Van Heerikhuizen et D. J. Loskutoff. « THE STRUCTURE OF THE HUMAN ENDOTHELIAL PLASMINOGEN ACTIVATOR INHIBITOR (PAI-1) GENE : NON-RANDOM POSITIONING OF INTRONS ». Dans XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644767.
Texte intégralO'hara, Patrick J., Frank A. Grant, A. Betty, J. Haldmen et Mark J. Murray. « Structure of the Human Factor VII Gene ». Dans XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643786.
Texte intégralPannekok, H., A. J. Van Zonneveid, C. J. M. de vries, M. E. MacDonald, H. Veerman et F. Blasi. « FUNCTIONAL PROPERTIES OF DELETION-MUTANTS OF TISSUE-TYPE PLASMINOGEN ACTIVATOR ». Dans XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643724.
Texte intégralde Vries, C. J. M., N. K. Veerman et H. Pannekoek. « ARTIFICIAL EXON SHUFFLING : CONSTRUCTION OF HYBRID cDNAS CONTAINING DOMAINS OF TISSUE-TYPE PLASMINOGEN ACTIVATOR (T-PA) AND UROKINASE (u-PA) ». Dans XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643940.
Texte intégralGeddes, V. A., G. V. Louie, G. D. Brayer et R. T. A. MacGillivray. « MOLECULAR BASIS OF HEMOPHILIA B : IDENTIFICATION OF THE DEFECT IN FACTOR IX VANCOUVER ». Dans XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643872.
Texte intégralRapports d'organisations sur le sujet "Protease encoding genes"
Barkan, Alice, et Zach Adam. The Role of Proteases in Regulating Gene Expression and Assembly Processes in the Chloroplast. United States Department of Agriculture, janvier 2003. http://dx.doi.org/10.32747/2003.7695852.bard.
Texte intégralOhad, Itzhak, et Himadri Pakrasi. Role of Cytochrome B559 in Photoinhibition. United States Department of Agriculture, décembre 1995. http://dx.doi.org/10.32747/1995.7613031.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 intégralManulis-Sasson, Shulamit, Christine D. Smart, Isaac Barash, Laura Chalupowicz, Guido Sessa et Thomas J. Burr. Clavibacter michiganensis subsp. michiganensis-tomato interactions : expression and function of virulence factors, plant defense responses and pathogen movement. United States Department of Agriculture, février 2015. http://dx.doi.org/10.32747/2015.7594405.bard.
Texte intégralLers, Amnon, E. Lomaniec, S. Burd, A. Khalchitski, L. Canetti et Pamela J. Green. Analysis of Senescence Inducible Ribonuclease in Tomato : Gene Regulation and Function. United States Department of Agriculture, février 2000. http://dx.doi.org/10.32747/2000.7570563.bard.
Texte intégralLers, Amnon, et Pamela J. Green. LX Senescence-Induced Ribonuclease in Tomato : Function and Regulation. United States Department of Agriculture, septembre 2003. http://dx.doi.org/10.32747/2003.7586455.bard.
Texte intégralHarman, Gary E., et Ilan Chet. Enhancement of plant disease resistance and productivity through use of root symbiotic fungi. United States Department of Agriculture, juillet 2008. http://dx.doi.org/10.32747/2008.7695588.bard.
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