Literatura académica sobre el tema "Extracellular Bacterial Protein (EBP)"
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Artículos de revistas sobre el tema "Extracellular Bacterial Protein (EBP)"
Haggar, Axana, Muzaffar Hussain, Helena Lönnies, Mathias Herrmann, Anna Norrby-Teglund y Jan-Ingmar Flock. "Extracellular Adherence Protein from Staphylococcus aureus Enhances Internalization into Eukaryotic Cells". Infection and Immunity 71, n.º 5 (mayo de 2003): 2310–17. http://dx.doi.org/10.1128/iai.71.5.2310-2317.2003.
Texto completoBui, Long M. G., Peter Hoffmann, John D. Turnidge, Peter S. Zilm y Stephen P. Kidd. "Prolonged Growth of a Clinical Staphylococcus aureus Strain Selects for a Stable Small-Colony-Variant Cell Type". Infection and Immunity 83, n.º 2 (10 de noviembre de 2014): 470–81. http://dx.doi.org/10.1128/iai.02702-14.
Texto completoPalma, Marco, Axana Haggar y Jan-Ingmar Flock. "Adherence of Staphylococcus aureus Is Enhanced by an Endogenous Secreted Protein with Broad Binding Activity". Journal of Bacteriology 181, n.º 9 (1 de mayo de 1999): 2840–45. http://dx.doi.org/10.1128/jb.181.9.2840-2845.1999.
Texto completoHussain, Muzaffar, Axana Haggar, Christine Heilmann, Georg Peters, Jan-Ingmar Flock y Mathias Herrmann. "Insertional Inactivation of eap in Staphylococcus aureus Strain Newman Confers Reduced Staphylococcal Binding to Fibroblasts". Infection and Immunity 70, n.º 6 (junio de 2002): 2933–40. http://dx.doi.org/10.1128/iai.70.6.2933-2940.2002.
Texto completoHinek, A. y M. Rabinovitch. "67-kD elastin-binding protein is a protective "companion" of extracellular insoluble elastin and intracellular tropoelastin." Journal of Cell Biology 126, n.º 2 (15 de julio de 1994): 563–74. http://dx.doi.org/10.1083/jcb.126.2.563.
Texto completoOtto, Ben R., Silvy J. M. van Dooren, Jan H. Nuijens, Joen Luirink y Bauke Oudega. "Characterization of a Hemoglobin Protease Secreted by the Pathogenic Escherichia coli Strain EB1". Journal of Experimental Medicine 188, n.º 6 (21 de septiembre de 1998): 1091–103. http://dx.doi.org/10.1084/jem.188.6.1091.
Texto completoLee, Y. M., L. H. Miau, C. J. Chang y S. C. Lee. "Transcriptional induction of the alpha-1 acid glycoprotein (AGP) gene by synergistic interaction of two alternative activator forms of AGP/enhancer-binding protein (C/EBP beta) and NF-kappaB or Nopp140." Molecular and Cellular Biology 16, n.º 8 (agosto de 1996): 4257–63. http://dx.doi.org/10.1128/mcb.16.8.4257.
Texto completoJiang, J. G. y R. Zarnegar. "A novel transcriptional regulatory region within the core promoter of the hepatocyte growth factor gene is responsible for its inducibility by cytokines via the C/EBP family of transcription factors." Molecular and Cellular Biology 17, n.º 10 (octubre de 1997): 5758–70. http://dx.doi.org/10.1128/mcb.17.10.5758.
Texto completoKida, Yutaka, Hiroyoshi Inoue, Takashi Shimizu y Koichi Kuwano. "Serratia marcescens Serralysin Induces Inflammatory Responses through Protease-Activated Receptor 2". Infection and Immunity 75, n.º 1 (16 de octubre de 2006): 164–74. http://dx.doi.org/10.1128/iai.01239-06.
Texto completoKwak, Dong Hoon, Ji-Hye Lee, Dong-Gun Kim, Taesoo Kim, Kwang Jin Lee y Jin Yeul Ma. "Inhibitory Effects of Hwangryunhaedok-Tang in 3T3-L1 Adipogenesis by Regulation of Raf/MEK1/ERK1/2 Pathway and PDK1/Akt Phosphorylation". Evidence-Based Complementary and Alternative Medicine 2013 (2013): 1–12. http://dx.doi.org/10.1155/2013/413906.
Texto completoTesis sobre el tema "Extracellular Bacterial Protein (EBP)"
Haggar, Axana. "Interaction between Extracellular adherence protein (Eap) from Staphylococcus aureus and the human host". Stockholm, 2005. http://diss.kib.ki.se/2005/91-7140-496-1/.
Texto completoShannon, Oonagh. "Biological effects of extracellular fibrinogen binding protein (Efb) in Staphylococcus aureus infection /". Stockholm, 2005. http://diss.kib.ki.se/2005/91-7140-275-6/.
Texto completoTiouajni, Mounira. "Caractérisation structurale et fonctionnelle du réseau d'interaction du Gelatin Binding Domain de la fibronectine humaine". Thesis, Paris 11, 2013. http://www.theses.fr/2013PA114820.
Texto completoThe extracellular matrix (ECM) is involved in a number of biological pathways associated with the cell migration, differentiation, adhesion and is also implicated in several pathological events. The cohesion of the ECM is accomplished by a highly organized protein complex network on the cell surface. The Gelatin Binding Domain (GBD) (⁶FI¹²FII ⁷⁸⁹FI) of the N-terminal region of fibronectin is found to interact with the transglutaminase 2 (TG2), collagen type I and the bacterial adhesion protein FNE. In this study, we conducted the structural and functional characterization of the protein complexes involved in the cohesion of ECM. The interactions between either TG2 or FNE and GBD have been characterized and the regions responsible for the interactions have also been mapped. Furthermore, we studied TG2/GBD and FNE/GBD complex by SAXS and built two models underscoring the interactions between (1), the GBD and the Nterminus of TG2 and (2), FNE and the sub-fragment ⁷⁸⁹FI of GBD providing insights on mechanistically elucidating the protein interactions during the cohehsion of ECM. The X-ray structure of the protein FNE of Streptococcus equi has been determined at 1.8 Å, by using an original tool that facilitates obtaining crystals
WU, ZHONGQIN. "Bacterial low temperature survival, ice nucleation proteins and ice-associating polymers". Thesis, 2010. http://hdl.handle.net/1974/5411.
Texto completoThesis (Ph.D, Biology) -- Queen's University, 2010-01-27 11:47:02.385
Zulfakar, SS. "Quantitative measurements of factors influencing bacterial attachment to meat surfaces". Thesis, 2013. https://eprints.utas.edu.au/17095/3/whole-thesis-Zulfakar.pdf.
Texto completoChitayat, Seth. "NMR and Biophysical Studies of Modular Protein Structure and Function". Thesis, 2007. http://hdl.handle.net/1974/727.
Texto completoThesis (Ph.D, Biochemistry) -- Queen's University, 2007-09-27 11:46:38.753
Chu, Mien-Sheng y 朱勉生. "Role of cyclic AMP-dependent Kinase (PKA), Extracellular Signal-regulated Kinase (ERK) and p38 Mitogen-activated Protein Kinase (p38 MAPK) Pathways in Bacterial Endotoxin-induced Expression of Nitric Oxide Synthase II and Production of Nitric Oxide: Requi". Thesis, 2001. http://ndltd.ncl.edu.tw/handle/85530499126278854895.
Texto completo國立陽明大學
解剖暨細胞生物學研究所
89
Upon inflammatory insults, microglia, the principal inflammatory cells in the brain, are capable of generating large amounts of regulatory factors, such as cytokines and nitric oxides (NO), that may play important roles in the pathogenesis of neurological diseases. In microglia, NO is produced by the inducible type of NO synthase (iNOS or NOS2) that was reported to be both neurodestructive and neuroprotective. Despite the numerous studies that have been conducted, the mechanisms for the regulation of NO biosynthesis remain to be elucidated. Expression of NOS2 in various phagocytic inflammatory cells can be strongly induced by the bacterial endotoxin, lipopolysaccharide (LPS). The bioactivity of LPS is mediated through a pertussis toxin-sensitive, Gi-protein-coupled receptor that, upon activation, results in down-regulation of adenylyl cyclase (AC), cyclic AMP (cAMP) levels, and the cAMP-dependent kinase (PKA) pathway. On the other hand, LPS has been shown to activate mitogen-activated protein kinases (MAPKs; including extracellular signal-regulated kinase, ERK, p38 MAPK, and c-Jun N-terminal kinase, JNK). The roles of the Gi-protein/AC/cAMP/PKA and Ras/Raf/MEK/MAPK pathways in the activation of various cell types have been well documented; however, the interaction between PKA and MAPKs, particularly in microglia, has rarely discussed. Because many neuroendocrine factors can activate the PKA pathway, the interactions between PKA and MAPK and their effect on NOS2 expression warrants further investigation. The purpose of this study is, therefore, to elucidate the effect of intracellular cAMP modulation on LPS-induced NOS2 expression and NO production in microglia cells. Using an immortalized murine microglia cell line, BV-2, stimulated with LPS, we measured NOS2 expression and NO production by immunoblotting assays and the Griess method, respectively, in the presence of various cAMP/PKA modulating agents. BV-2 cells, upon exposure to LPS, displayed detectable amounts of NOS2 in 3 hr. At 6 hr after LPS stimulation, accumulation of NO in the culture medium was detectable and reached maximum in 18 hr. The addition of a membrane-permeable cAMP (dibutyryl-cAMP; db-cAMP) or an AC-activating agent (forskolin) inhibited NO production relative to the concentration of cAMP added. On the other hand, additional of melatonin, a neurohormone with Gi-protein-coupled receptors also dose-dependently inhibited NO production, suggesting a lack of synergism by simultaneous down-regulation of PKA. Further examination of the effect of cAMP modulators on MAPK activation indicated that both ERK and p38 MAPK were essential for LPS-induced NOS2 expression; however, p38 appeared to play more important roles because a relatively low concentration of p38 inhibitor (SB203580) markedly suppressed NO production. CAMP and melatnonin alone caused activation of p38 MAPK and ERK, respectively. Pretreatment of BV-2 cells with cAMP or melatonin, however, inhibited the activation of p38 but had less effects on ERK. Our data provide a novel model for the interaction between PKA and MAPK. We propose that homeostasis of cAMP levels is crucial to MAPK-mediated signal for NOS2 expression. These results may prove to be insightful in the treatment of microglia-associated chronic inflammatory diseases of the brain.
Capítulos de libros sobre el tema "Extracellular Bacterial Protein (EBP)"
Garcia, Roberto Alvarez-Fernandez, Guillermo Aragoneses-Cazorla, Laura Lerma, Rafael C. Prados-Rosales y Jose L. Luque-Garcia. "Isolation of Bacterial Extracellular Vesicles and Identification of Their Protein Cargo". En Methods in Molecular Biology, 285–92. New York, NY: Springer US, 2023. http://dx.doi.org/10.1007/978-1-0716-3147-8_17.
Texto completoEvans, John Spencer y Sunney I. Chan. "The N-terminal fragment of bovine phosphophoryn, an extracellular mineral matrix protein, shares sequence homology with viral, bacterial and eukaryotic transcriptional and post-translational regulatory proteins". En Proteins, 251–59. Dordrecht: Springer Netherlands, 1991. http://dx.doi.org/10.1007/978-94-010-9063-6_35.
Texto completoBoggs, Amy Fujishige y David A. Agard. "Bacterial extracellular secretion". En Membrane Protein Transport, 165–79. Elsevier, 1996. http://dx.doi.org/10.1016/s1874-592x(96)80007-2.
Texto completoLeBar, Kristen y Zhijie Wang. "Extracellular Matrix in Cardiac Tissue Mechanics and Physiology: Role of Collagen Accumulation". En Extracellular Matrix - Developments and Therapeutics [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.96585.
Texto completoPatel, Hershna y David B. Whitehouse. "Microbial Proteomics". En Genomics and Clinical Diagnostics, 103–38. The Royal Society of Chemistry, 2019. http://dx.doi.org/10.1039/9781782628217-00103.
Texto completoSelwal, Krishan K., Garima Deswal, Harsha Nirvan y Manjit K. Selwal. "Green Synthesis of Nanoparticles using Fungal Extracts". En Mycology: Current and Future Developments, 103–28. BENTHAM SCIENCE PUBLISHERS, 2022. http://dx.doi.org/10.2174/9789815051360122030008.
Texto completoBorkow, Gadi y Eyal Melamed. "Copper, an Abandoned Player Returning to the Wound Healing Battle". En Wound Healing [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.96952.
Texto completoActas de conferencias sobre el tema "Extracellular Bacterial Protein (EBP)"
Zhang, D., Y. Zhu y X. Wang. "Extracellular Vesicle-Containing Clara Cell Protein 16 (CC16) Regulates Bacterial-Induced Macrophage Activation". En 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.a2291.
Texto completoInformes sobre el tema "Extracellular Bacterial Protein (EBP)"
Barash, Itamar, J. Mina Bissell, Alexander Faerman y Moshe Shani. Modification of Milk Composition via Transgenesis: The Role of the Extracellular Matrix in Regulating Transgene Expression. United States Department of Agriculture, julio de 1995. http://dx.doi.org/10.32747/1995.7570558.bard.
Texto completoShani, Moshe y C. P. Emerson. Genetic Manipulation of the Adipose Tissue via Transgenesis. United States Department of Agriculture, abril de 1995. http://dx.doi.org/10.32747/1995.7604929.bard.
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