Littérature scientifique sur le sujet « Proteinaceo »
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Articles de revues sur le sujet "Proteinaceo"
Oppert, B., K. Hartzer et M. Zuercher. « Digestive proteinases in Lasioderma serricorne (Coleoptera : Anobiidae) ». Bulletin of Entomological Research 92, no 4 (août 2002) : 331–36. http://dx.doi.org/10.1079/ber2002179.
Texte intégralJankangram, Wichuda, et Sunthorn Chooluck. « In silico Analysis and Characterization of a Putative Aspartic Proteinase Inhibitor, IA3 from Lachancea kluyveri ». Trends in Sciences 20, no 3 (19 janvier 2023) : 6377. http://dx.doi.org/10.48048/tis.2023.6377.
Texte intégralRosenthal, P. J., K. Kim, J. H. McKerrow et J. H. Leech. « Identification of three stage-specific proteinases of Plasmodium falciparum. » Journal of Experimental Medicine 166, no 3 (1 septembre 1987) : 816–21. http://dx.doi.org/10.1084/jem.166.3.816.
Texte intégralSever, Natasa, Metka Filipic, Joze Brzin et Tamara T. Lah. « Effect of Cysteine Proteinase Inhibitors on Murine B16 Melanoma Cell Invasion in vitro ». Biological Chemistry 383, no 5 (15 mai 2002) : 839–42. http://dx.doi.org/10.1515/bc.2002.088.
Texte intégralGarciacarreno, F. L., L. E. Dimes et N. F. Haard. « Substrate-Gel Electrophoresis for Composition and Molecular Weight of Proteinases or Proteinaceous Proteinase Inhibitors ». Analytical Biochemistry 214, no 1 (octobre 1993) : 65–69. http://dx.doi.org/10.1006/abio.1993.1457.
Texte intégralHiemstra, P. S. « Novel roles of protease inhibitors in infection and inflammation ». Biochemical Society Transactions 30, no 2 (1 avril 2002) : 116–20. http://dx.doi.org/10.1042/bst0300116.
Texte intégralIkeda, T. « Involvement of cysteine proteinases in excystment of Paragonimus ohirai metacercariae induced by sodium cholate and A23187 ». Journal of Helminthology 77, no 1 (mars 2003) : 21–26. http://dx.doi.org/10.1079/joh2002144.
Texte intégralBózner, P., et P. Demeš. « Proteinases inTrichomonas vaginalisandTritrichomonas mobilensisare not exclusively of cysteine type ». Parasitology 102, no 1 (février 1991) : 113–15. http://dx.doi.org/10.1017/s0031182000060418.
Texte intégralJakobs, K. H., et K. Aktories. « Stimulation of high-affinity GTPase by trypsin and trypsin-like proteinases in membranes of human platelets ». Biochemical Journal 249, no 3 (1 février 1988) : 639–43. http://dx.doi.org/10.1042/bj2490639.
Texte intégralDubin, A., J. Potempa et J. Travis. « Structural and functional characterization of elastases from horse neutrophils ». Biochemical Journal 300, no 2 (1 juin 1994) : 401–6. http://dx.doi.org/10.1042/bj3000401.
Texte intégralThèses sur le sujet "Proteinaceo"
ZEYNALI, AMIRBAHADOR. « Two-photon assisted direct laser writing of proteinaceous microarchitectures containing plasmonic nanoparticles ; characterization and optimization ». Doctoral thesis, Università degli Studi di Milano-Bicocca, 2021. http://hdl.handle.net/10281/304319.
Texte intégralMetallic nanoparticles, due to their fascinating optical and electrochemical properties, attract the attention of different science and engineering research disciplines. Among these properties, the plasmonic photothermal effect is a notable and exclusive feature of noble-metal nanoparticles that, by today, are exploited through lots of research activities for various purposes, especially for biomedical applications. This optically-tunable phenomenon uniquely increases the flexibility of the optical response of host matrices, by allowing to induce highly localized temperature increases that can be triggered via simple external stimulation device like a light source. Such matrices can be valuable tools in the field of cell treatments and, in general, tissue engineering. In the present study, the two-photon-assisted direct laser writing (DLW) technique was employed to fabricate microarchitectures with the different elastic modulus (80kPa to 800kPa) from a proteinaceous ink composed of bovine serum albumin (BSA), rose Bengal (RB), or methylene blue (MB), and non-spherical symmetric gold nanoparticles (GNPs), with the ability to generate local temperature increase by stimulation in the near-infrared spectral region. The recorded photothermal efficiency measured using focused continuous wave (CW) laser irradiation at 800nm on microstructures loaded with GNPs at low gold atom concentration (1%w/w) reached 12.2 pm 0.4 C/W, that is a record photothermal effect induced from a printed proteinaceous feature. This photo-thermal functionality arising from the GNPs embedded within the fabricated proteinaceous microstructures can then be applied for studying responses of living systems like cells and bacteria cultures under an externally triggered highly localized heat release.
Turk, Boris. « Papain-like cysteine proteinases : regulation by proteinase inhibitors and pH / ». Uppsala : Swedish Univ. of Agricultural Sciences (Sveriges lantbruksuniv.), 1996. http://epsilon.slu.se/avh/1996/91-576-5227-9.gif.
Texte intégralZhang, Xiaorong. « The roles of proteinases and proteinase inhibitors in plant-nematode interactions ». Diss., Virginia Tech, 1994. http://hdl.handle.net/10919/37260.
Texte intégralBridges, Sylvia Shadinger. « Design, synthesis, and evaluation of cysteine protease inhibitors ». Diss., Georgia Institute of Technology, 2008. http://hdl.handle.net/1853/29738.
Texte intégralSouza, Thais Paula de. « Efeito dos inibidores de proteinase de soja no padrão de expressão de proteinases de Spodoptera frugiperda ». Universidade de São Paulo, 2013. http://www.teses.usp.br/teses/disponiveis/11/11137/tde-05112013-150120/.
Texte intégralAmong the chemicals secreted by plants against insect herbivores, peptidase inhibitors (PIs) are of great interest. The attention given to PIs is due to the fact that they are a good alternative to control insect pests since they do not cause damage to human health and the environment. However, many species of insects are able to escape the negative effects of PIs plants via different adaptive mechanisms. Because of this, it is important to understand the mechanisms developed by insects to circumvent the effects of PIs plants. Against this background, this research aimed to study the adaptive mechanism of serine endopeptidases Spodoptera frugiperda to soybean endopeptidase inhibitors. For this purpose, larvae of S. frugiperda were reared on artificial diet and control artificial diet plus 0.5% of endopeptidase inhibitors of soybean. We conducted a transcriptome midgut of worms maintained in chronic ingestion of the inhibitor. The relative expression of the genes, trypsin and chymotrypsin, was also compared the midgut of sixth instar larvae kept in these diets. In another experiment, the larvae were conducted to moth, then the treatments were mated forming a second generation. Relative expression data were obtained for individuals of the first and second generation, and then compared. Identified 14 genes with potential of chymotrypsin and 9 trypsin like genes. The trypsin gene were divided into two groups for both their sensitivity to PI soybean endopeptidase, and for their relative expression pattern. There was a differentiated response on the genes activation of S. frugiperda serina endopeptidases. The genes were clustered in 2 groups, the responsive ones and the non responsive to the inhibitor. The acute exposition to the inhibitor activated a small group of genes and the chronic exposition affected several genes, indicating the existence of temporal regulated mechanism. Besides, there is a possible occurance of an epigenetic mechanism, which is related to the digestive serina endopeptidases inhibitors of soybean.
Nadalini, Larissa Cristina Deppmann. « Caracterização do mecanismo adaptativo de Spodoptera frugiperda aos inibidores de proteinase de plantas ». Universidade de São Paulo, 2007. http://www.teses.usp.br/teses/disponiveis/11/11137/tde-07022008-151221/.
Texte intégralThe existence of a diverse serine proteinase gene family in lepidopteran insects has suggested its significant role in the insect adaptation to plant proteinase inhibitors. These enzymes have been shown to be involved in the proteolytic digestion process of insect larvae. Spodoptera frugiperda larvae were fed on a diet supplemented with soybean proteinase inhibitor (SPI) and the gene expression of intestinal proteinases was evaluated by real time PCR. Previous transcription analyses found two groups of intestinal serine proteinases: one group of genes constitutively expressed in the control larvae that is induced by the SPI-containing diet during the experiment, and a second group that is absent in the control but also induced by the SPI rich diet. Herein was observed a third group of proteinases that are neither induced nor repressed by the presence of SPI in the diet. This observation suggests that adaptation of S. frugiperda to SPI involves de novo synthesis, up regulation of existing enzymes and that there is a third group insensitive to the presence of the inhibitors. Proteinases from intestines of larvae reared on a diet with SPI showed insensitivity to the inhibitor. The proteinases were also insensitive when the activity was checked with a broad-spectrum potato proteinase inhibitor. The results here presented propose that adaptation of S. frugiperda to SPI follows a \"shotgun\" approach, based on a general up regulation of a large set of endoproteinases.
Estrada, Sergio. « Cystatin A, a mammalian cysteine proteinase inhibitor : mechanism of inhibition of target proteinases by recombinant cystatin A variants / ». Uppsala : Swedish Univ. of Agricultural Sciences (Sveriges lantbruksuniv.), 1998. http://epsilon.slu.se/avh/1998/91-576-5448-4.gif.
Texte intégralSouza, Diego Pereira de. « ProteÃnas inibidoras de fitopatÃgenos em fluidos laticÃferos : atividade e mecanismo de aÃÃo ». Universidade Federal do CearÃ, 2010. http://www.teses.ufc.br/tde_busca/arquivo.php?codArquivo=7887.
Texte intégralUm relevante nÃmero de espÃcies vegetais à descrito como plantas produtoras de um fluido leitoso comumente denominado de lÃtex. Nestas espÃcies, o lÃtex à sintetizado e armazenado sob pressÃo em um sistema de canais formados por cÃlulas altamente especializadas denominadas de laticÃferas, em cujos citoplasmas estÃo presentes todas as estruturas eucariontes em meio à Ãgua, borracha e inÃmeras molÃculas, muitas das quais especÃficas deste conteÃdo. Muitos estudos tÃm sugerido que molÃculas produzidas nestes fluidos participam da defesa vegetal. Neste trabalho, o lÃtex de 5 espÃcies foi coletado e processado em laboratÃrio para obtenÃÃo de suas fraÃÃes protÃicas e estas foram avaliadas quanto a atividade sobre fungos fitopatogÃnicos atravÃs de ensaios de inibiÃÃo da germinaÃÃo de esporos e crescimento de hifas. ProteÃnas do lÃtex de C. procera (PLCp), Cryptostegia grandiflora (PLCg) e Carica candamarcensis (P1 G10) apresentaram atividade antifÃngica enquanto que Plumeria rubra (PLPr) e Euphorbia tirucalli (PLEt) nÃo apresentaram atividade sobre qualquer dos fungos avaliados (Colletotrichum gloeosporioides, Fusarium oxysporum, Fusarium solani, Rhizoctonia solani, Neurospora sp. e Aspergillus niger). A atividade inibitÃria das fraÃÃes protÃicas se correlacionou diretamente com a presenÃa de atividade proteolÃtica do tipo cisteÃnica presente nas amostras de PLCp, PLCg e P1G10. A atividade antifÃngica foi aumentada na presenÃa de DTT, um ativador destas proteases e foi diminuÃda ou eliminada quanto Ãs amostras foram prÃ-tratadas com iodoacetamida (IAA), um inibidor especÃfico de proteases cisteÃnicas. AlÃm disso, a atividade antifÃngica foi observada quando papaÃna, uma protease cisteÃnica purificada do lÃtex de Carica papaya foi avaliada, mas tripsina e quimotripsina, duas proteases serÃnicas nÃo apresentaram atividade. AtravÃs de cromatografia em coluna de Mono-S Sepharose acoplada ao sistema de FPLC, uma protease cisteÃnica foi isolada de PLCg. A proteÃna purificada (Cg24-I) apresentou massa molecular de 24,118 KDa. A Cg24-I apresentou atividade proteolÃtica mÃxima em pH 8,0 e foi inibida por IAA e E-64, utilizando azocaseÃna e BANA como substratos, respectivamente. Cg24-I inibiu a germinaÃÃo de F. solani e foi capaz de alterar a permeabilidade das membranas dos esporos na concentraÃÃo de 90 ng/ml. Esse conjunto de resultados sugere que proteinases cisteÃnicas de fluidos laticÃferos participam da defesa das plantas contra fungos fitopatogÃnicos e que o provÃvel mecanismo de aÃÃo destas proteÃnas seja a alteraÃÃo da permeabilidade da membrana plasmÃtica destes microrganismos. A descriÃÃo de atividade antifÃngica de proteases cisteÃnicas oriundas de fluidos laticÃferos nÃo à ainda descrita em detalhes na literatura, sendo este um trabalho com carÃter original.
Canal systems containing secretions, such as latex, are widely disseminated in the plant kingdom. These fluids are chemically complex and exhibit intense metabolism. Despite their origin, latex is the cytoplasm of specialized cells growing intrusively into organized tissues and organs, forming an interconnected network allowing latex exudation immediately after tissue damage. Insecticidal effects of latex proteins have been described, however minor studies were devoted to investigate antifungal activities in latex. In this study proteins extracted from latex of Calotropis procera (Ait.) R.Br (PLCp), Plumeria rubra L.(PLPr), Carica candamarcensis Hook F.(P1 G10), Cryptostegia grandiflora (PLCg), and Euphorbia tirucalli L. (PLEt) were tested for antifungal activity against six phytopathogens (Fusarium solani, F. oxysporium, Aspergilus niger, Rhizoctonia solani, Neurospora sp. and Colletrotricum gloerosporioides). PLCp, PLCg and P1G10 exhibited antifungal activity and PLPr and PLEt were not efetive. Inhibitory activity of the protein fractions correlated with the cysteine-type proteolytic activity found in these fractions. The endogenous proteolytic activity and inhibitory activity on fungal growth were both increased when samples were first activated with DTT, a cysteine proteinase activator. Conversely, pre-treatment of samples with iodoacetamide, an inhibitor of these proteases rendered all samples deficient of both, proteolytic and antifungal activities. Antifungal of activity of cysteine proteinases of latex origin was also confirmed when papain, obtained from latex of Caryca papaya was tested while purified trypsin and chemotrysin, two serine-type proteases were not antifungal. A cysteine proteinase was thus, purified form PLCg by ion exchange chromatography on a Mono-S Sepharose matrix monitored by a FPLC system. The protein, named Cg24-I exhibited molecular mass of 26.118 KDa determined by MALDI spectrometry; maximum of proteolysis at pH 8.0 and inhibited by iodoacetamide and E-64 when assayed with azocazein or BANA as substrates. Cg24-I inhibited germination of F. solani and altered membrane permeability of spores at a minimum concentration of 90 ng/ml. Results present here suggest that cysteine proteinases of laticifer fluids are proteins with antifungal activity capable of damaging spore structure and inhibiting hyphae growth. Reports of antifungal activity of latex proteases are still scarce in literature and this work appears as an important contribution to this field. Furthermore, this work gives important evidence for the multiple defensive role of latex in plants.
Macgregor, James Mylne. « Alimentary tract proteinases of the Southern corn rootworm (Diabrotica undecimpunctata howardi) and the potential of potato Kunitz proteinase inhibitors for larval control ». Thesis, Durham University, 2001. http://etheses.dur.ac.uk/3808/.
Texte intégralMistry, Rohit. « Development of a sheep model to investigate the role of neutrophil proteinases and their endogenous inhibitors in acute lung injury : a novel proteinase inhibitor ». Thesis, Imperial College London, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.308934.
Texte intégralLivres sur le sujet "Proteinaceo"
Fusek, Martin. Aspartic proteinases : Physiology and pathology. Boca Raton, Fla : CRC Press, 1995.
Trouver le texte intégralTurk, Boris. Papain-like cysteine proteinases : Regulation by proteinase inhibitors and pH. Uppsala : SverigesLantbruksuniversitet, 1996.
Trouver le texte intégralEstrada, Sergio. Cystatin A, a mammalian cysteine proteinase inhibitor : Mechanism of inhibition of target proteinases by recombinant cystatin A variants. Uppsala : Sveriges Lantbruksuniversitet, 1998.
Trouver le texte intégralKirschke, Heidrun. Proteinases 1 : lysosomal cysteine proteinases. London : Academic Press, 1995.
Trouver le texte intégralCaspases, paracaspases, and metacaspases : Methods and protocols. New York : Humana, 2014.
Trouver le texte intégralG, James Michael N., et International Conference on Aspartic Proteinases (7th : 1996 : Banff, Alta.), dir. Aspartic proteinases : Retroviral and cellular enzymes. New York : Plenum Press, 1998.
Trouver le texte intégralTakahashi, Kenji, dir. Aspartic Proteinases. Boston, MA : Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1871-6.
Texte intégralJames, Michael N. G., dir. Aspartic Proteinases. Boston, MA : Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-5373-1.
Texte intégralJ, Barrett Alan, et Salvesen G, dir. Proteinase inhibitors. Amsterdam : Elsevier, 1986.
Trouver le texte intégralPhilippe, Taupin, dir. The cystatin superfamily of proteinase inhibitors. New York : Nova Science Publishers, 2007.
Trouver le texte intégralChapitres de livres sur le sujet "Proteinaceo"
diZerega, Gere S., et Kathleen E. Rodgers. « Proteinases and Proteinase Inhibitors ». Dans The Peritoneum, 231–73. New York, NY : Springer New York, 1992. http://dx.doi.org/10.1007/978-1-4613-9235-4_8.
Texte intégralBode, Wolfram, et Robert Huber. « Natural protein proteinase inhibitors and their interaction with proteinases ». Dans EJB Reviews, 43–61. Berlin, Heidelberg : Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-78046-2_5.
Texte intégralOwen, Caroline A., et Edward J. Campbell. « Proteinases ». Dans ARDS Acute Respiratory Distress in Adults, 139–65. Boston, MA : Springer US, 1996. http://dx.doi.org/10.1007/978-1-4899-3430-7_10.
Texte intégralJochum, M., W. Machleidt, H. Neuhof et H. Fritz. « Proteinases ». Dans Pathophysiology of Shock, Sepsis, and Organ Failure, 46–60. Berlin, Heidelberg : Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-76736-4_5.
Texte intégralStockley, R. A., et D. Burnett. « Proteinases and Proteinase Inhibitors in the Pathogenesis of Pulmonary Emphysema in Humans ». Dans Biochemistry of Pulmonary Emphysema, 47–69. London : Springer London, 1992. http://dx.doi.org/10.1007/978-1-4471-3771-9_5.
Texte intégralDunn, Ben M., Paula E. Scarborough, W. Todd Lowther et Chetana Rao-Naik. « Comparison of the Active Site Specificity of the Aspartic Proteinases Based on a Systematic Series of Peptide Substrates ». Dans Aspartic Proteinases, 1–9. Boston, MA : Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1871-6_1.
Texte intégralRao, Chetana, et Ben M. Dunn. « Evidence for Electrostatic Interactions in the S2 Subsite of Porcine Pepsin ». Dans Aspartic Proteinases, 91–94. Boston, MA : Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1871-6_10.
Texte intégralDhanaraj, Raj R. V., Jim E. Pitts, Phil Nugent, Poonsook Orprayoon, Jon B. Cooper, Tom L. Blundell, Janna Uusitalo et Merja Penttilä. « Protein Engineering of Surface Loops : Preliminary X-Ray Analysis of the Chy155–165rhi Mutant ». Dans Aspartic Proteinases, 95–99. Boston, MA : Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1871-6_11.
Texte intégralSzecsi, Pal Bela, et Hans Lilja. « Seminal Progastricsin ». Dans Aspartic Proteinases, 101–5. Boston, MA : Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1871-6_12.
Texte intégralIchinose, Masao, Shinko Tsukada, Kazumasa Miki, Nobuyuki Kakei, Masashi Matsushima, Naohisa Yahagi, Satoshi Ishihama et al. « Effects of Hydrocortisone on the Pepsinogen-Producing Cells in Rat Stomach Mucosa ». Dans Aspartic Proteinases, 107–13. Boston, MA : Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-1871-6_13.
Texte intégralActes de conférences sur le sujet "Proteinaceo"
Jackson, Craig M. « A DEFINITION OF HEPARIN ANTICOAGULANT POTENCY APPLICABLE TO ALL HEPARINS AND HEPARIN-LIKE SUBSTANCES AND ITS PRACTICAL APPLICATION IN ASSAYING HEPARIN ». Dans XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642928.
Texte intégralLarsson, L. J., E. P. Frisch et I. Bjoörk. « PROPERTIES OF THE COMPLEX BETWEEN ou-MACROGLOBULIN AND THE PROTEINASE BRINASE FROM ASPERGILLUS ORYZAE ». Dans XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643039.
Texte intégralGibson, Stacy G., Koichiro Mihara, Andries Zijlstra, Matthew E. Hyndman et Morley D. Hollenberg. « Abstract 2014 : Genitourinary cancer-derived cells produce microenvironment proteinases that regulate proteinase activated receptors (PARs) to drive oncogenic signaling ». Dans Proceedings : AACR Annual Meeting 2017 ; April 1-5, 2017 ; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-2014.
Texte intégralBasañez, Gorka, Ana J. García Sáez, Oihana Terrones Uria, Juan Garcia Valero, Miguel Garcia Porras, Itsasne Bustillo Zabalbeitia, Hector Flores Romero, Ane Landajuela Larma et Olatz Landeta Diaz. « BAK proteinaren mekanismo proapoptotikoa aztertzen ». Dans I. Ikergazte. Nazioarteko ikerketa euskaraz. Bilbao : UEU arg, 2015. http://dx.doi.org/10.26876/ikergazte.i.47.
Texte intégralDeSha, Michael S. « Biological Aerosol Sensor Breadboard ». Dans The European Conference on Lasers and Electro-Optics. Washington, D.C. : Optica Publishing Group, 1998. http://dx.doi.org/10.1364/cleo_europe.1998.cfj7.
Texte intégralJung, Jung-Yeul, Ki-Taek Byun, Jae-Ho Hong et Ho-Young Kwak. « Proteinaceous Bubbles and Nano Particle Flows in Microchannel ». Dans ASME 2004 2nd International Conference on Microchannels and Minichannels. ASMEDC, 2004. http://dx.doi.org/10.1115/icmm2004-2437.
Texte intégralCrisford, H. A., E. Sapey et R. A. Stockley. « Validation of an In Vitro Model of the Proteinase/Anti-Proteinase Imbalance Observed in Alpha-1 Antitrypsin Deficiency ». Dans American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a4080.
Texte intégralDooley, Kevin, et Scott Banta. « Engineering of functional proteinaceous hydrogels for biotechnology applications ». Dans 2014 40th Annual Northeast Bioengineering Conference (NEBEC). IEEE, 2014. http://dx.doi.org/10.1109/nebec.2014.6972777.
Texte intégralSarioglu, Nurhan, Fuat Erel, Adnan Adil Hişmiogullari et Celalettin Cevik. « Association between ADAMTs proteinases and Obstructive Sleep Apnea ». Dans ERS International Congress 2017 abstracts. European Respiratory Society, 2017. http://dx.doi.org/10.1183/1393003.congress-2017.oa1759.
Texte intégralErdozain Fernandez, Amaia Maite, Koldo Callado Hernando, Vincent Vialou, Sylvie Dumas et Amaia Nuñez del Moral. « Zelulaz kanpoko matrizeko hevin proteinaren ikerketa giza garunean ». Dans III. Ikergazte. Nazioarteko ikerketa euskaraz. Bilbao : UEU arg, 2019. http://dx.doi.org/10.26876/ikergazte.iii.04.01.
Texte intégralRapports d'organisations sur le sujet "Proteinaceo"
Radisky, Evette. Identification of Serine Proteinases Involved in Breast Cancer Progression. Fort Belvoir, VA : Defense Technical Information Center, septembre 2007. http://dx.doi.org/10.21236/ada475734.
Texte intégralTweten, Rodney K. Development of a Novel, Proteinase-Activated Toxin Targeting Tumor Neovascularization. Fort Belvoir, VA : Defense Technical Information Center, octobre 1999. http://dx.doi.org/10.21236/ada391517.
Texte intégralTweten, Rodney K. Development of a Novel, Proteinase-Activated Toxin Targeting Tumor Neovascularization. Fort Belvoir, VA : Defense Technical Information Center, octobre 1998. http://dx.doi.org/10.21236/adb249654.
Texte intégralSieber, Fritz. Proteinated Subnano Particles of Elemental Selenium for the Treatment of Breast Cancer. Fort Belvoir, VA : Defense Technical Information Center, septembre 2005. http://dx.doi.org/10.21236/ada443081.
Texte intégralDolja, Valerian V., Amit Gal-On et Victor Gaba. Suppression of Potyvirus Infection by a Closterovirus Protein. United States Department of Agriculture, mars 2002. http://dx.doi.org/10.32747/2002.7580682.bard.
Texte intégralAntonaci, Francesca C. Control of Transformation and Invasiveness of Breast Cancer Cells by Estrogen Regulation of Proteinase Inhibitor 9. Fort Belvoir, VA : Defense Technical Information Center, avril 2005. http://dx.doi.org/10.21236/ada471083.
Texte intégralDougherty, W. Understanding and targeting a novel plant viral proteinase/substrate interaction. Final report, July 1, 1989--June 30, 1995. Office of Scientific and Technical Information (OSTI), octobre 1995. http://dx.doi.org/10.2172/108096.
Texte intégralGrubman, Marvin J., Yehuda Stram, Peter W. Mason et Hagai Yadin. Development of an Empty Viral Capsid Vaccine against Foot and Mouth Disease. United States Department of Agriculture, août 1995. http://dx.doi.org/10.32747/1995.7570568.bard.
Texte intégralGrafi, Gideon, et Brian Larkins. Endoreduplication in Maize Endosperm : An Approach for Increasing Crop Productivity. United States Department of Agriculture, septembre 2000. http://dx.doi.org/10.32747/2000.7575285.bard.
Texte intégralSela, Shlomo, et Michael McClelland. Investigation of a new mechanism of desiccation-stress tolerance in Salmonella. United States Department of Agriculture, janvier 2013. http://dx.doi.org/10.32747/2013.7598155.bard.
Texte intégral