Littérature scientifique sur le sujet « Heme-binding protein 2 »
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Articles de revues sur le sujet "Heme-binding protein 2"
Liu, Liu, Arti B. Dumbrepatil, Angela S. Fleischhacker, E. Neil G. Marsh et Stephen W. Ragsdale. « Heme oxygenase-2 is post-translationally regulated by heme occupancy in the catalytic site ». Journal of Biological Chemistry 295, no 50 (13 octobre 2020) : 17227–40. http://dx.doi.org/10.1074/jbc.ra120.014919.
Texte intégralNakamura, Nozomi, Yoichi Naoe, Akihiro Doi, Yoshitsugu Shiro et Hiroshi Sugimoto. « Conformational change of periplasmic heme-binding protein in ABC transporter ». Acta Crystallographica Section A Foundations and Advances 70, a1 (5 août 2014) : C1496. http://dx.doi.org/10.1107/s2053273314085039.
Texte intégralNath, Karl A., Joseph P. Grande, John D. Belcher, Vesna D. Garovic, Anthony J. Croatt, Matthew L. Hillestad, Michael A. Barry, Meryl C. Nath, Raymond F. Regan et Gregory M. Vercellotti. « Antithrombotic effects of heme-degrading and heme-binding proteins ». American Journal of Physiology-Heart and Circulatory Physiology 318, no 3 (1 mars 2020) : H671—H681. http://dx.doi.org/10.1152/ajpheart.00280.2019.
Texte intégralEl-Mashtoly, Samir F., et Teizo Kitagawa. « Structural chemistry involved in information detection and transmission by gas sensor heme proteins : Resonance Raman investigation ». Pure and Applied Chemistry 80, no 12 (1 janvier 2008) : 2667–78. http://dx.doi.org/10.1351/pac200880122667.
Texte intégralTiedemann, Michael T., Naomi Muryoi, David E. Heinrichs et Martin J. Stillman. « Characterization of IsdH (NEAT domain 3) and IsdB (NEAT domain 2) in Staphylococcus aureus by magnetic circular dichroism spectroscopy and electrospray ionization mass spectrometry ». Journal of Porphyrins and Phthalocyanines 13, no 10 (octobre 2009) : 1006–16. http://dx.doi.org/10.1142/s1088424609001352.
Texte intégralFreeman, Samuel L., Hanna Kwon, Nicola Portolano, Gary Parkin, Umakhanth Venkatraman Girija, Jaswir Basran, Alistair J. Fielding et al. « Heme binding to human CLOCK affects interactions with the E-box ». Proceedings of the National Academy of Sciences 116, no 40 (16 septembre 2019) : 19911–16. http://dx.doi.org/10.1073/pnas.1905216116.
Texte intégralFleischhacker, Angela S., Amanda L. Gunawan, Brent A. Kochert, Liu Liu, Thomas E. Wales, Maelyn C. Borowy, John R. Engen et Stephen W. Ragsdale. « The heme-regulatory motifs of heme oxygenase-2 contribute to the transfer of heme to the catalytic site for degradation ». Journal of Biological Chemistry 295, no 16 (9 mars 2020) : 5177–91. http://dx.doi.org/10.1074/jbc.ra120.012803.
Texte intégralLechuga, Guilherme C., Franklin Souza-Silva, Carolina Q. Sacramento, Monique R. O. Trugilho, Richard H. Valente, Paloma Napoleão-Pêgo, Suelen S. G. Dias et al. « SARS-CoV-2 Proteins Bind to Hemoglobin and Its Metabolites ». International Journal of Molecular Sciences 22, no 16 (21 août 2021) : 9035. http://dx.doi.org/10.3390/ijms22169035.
Texte intégralJeong, Jinsook, Tracey A. Rouault et Rodney L. Levine. « Identification of a Heme-sensing Domain in Iron Regulatory Protein 2 ». Journal of Biological Chemistry 279, no 44 (16 août 2004) : 45450–54. http://dx.doi.org/10.1074/jbc.m407562200.
Texte intégralYang, Jianhua, Kevin D. Kim, Andrew Lucas, Karen E. Drahos, Carlo S. Santos, Sean P. Mury, Daniel G. S. Capelluto et Carla V. Finkielstein. « A Novel Heme-Regulatory Motif Mediates Heme-Dependent Degradation of the Circadian Factor Period 2 ». Molecular and Cellular Biology 28, no 15 (27 mai 2008) : 4697–711. http://dx.doi.org/10.1128/mcb.00236-08.
Texte intégralThèses sur le sujet "Heme-binding protein 2"
AMBROSI, Emanuele. « Expression, purification and structural characterization of three human proteins : apolipoprotein M, heme-binding protein 2 and folate receptor α ». Doctoral thesis, 2008. http://hdl.handle.net/11562/337640.
Texte intégralThis thesis work was aimed at the expression, purification and crystallization of three human proteins (apolipoprotein M, folate receptor α and SOUL protein) in order to determine their three-dimensional structure by means of X-ray protein crystallography. Human apolipoprotein M was expressed using the methylotrophic yeast P. pastoris. The recombinant protein was purified by ion-exchange chromatography, preparative isoelectric focusing, gel filtration, and Lipidex-1000 chromatography. In order to obtain a more homogeneous protein, the non-glycosylated mutant (Asn135Gln) was also expressed and purified. The crystallization trials gave some positive results with mutated apoM, although the crystals are still not suitable for X-ray diffraction experiments. The heterologous expression of the human FR-a was troublesome, and although different expression systems (P. pastoris, baculovirus, and N. benthamiana) were tested, only a low amount of recombinant protein was obtained (from P. pastoris) and purified (by ion-exchange chromatography and gel filtration). However non of the crystallization conditions tested was successful, probably due to the low protein concentration. Human SOUL (heme-binding protein 2) was expressed in E. coli and purified by immobilized metal ion affinity chromatography, using the hexa-histidine tag added to the C-terminus of the protein. The recombinant SOUL was crystallized both as apoprotein and as a complex in the presence of hemin. The preliminary X-ray diffraction analysis shows the presence of six molecules in the unit cell, and no significant differences between the apoand the holoprotein were found. Further studies suggest that hemin is not bound to the protein, since the Fe peak could not be found in the X-ray fluorescence spectrum of the crystals. Attempts to solve the three-dimensional structure by means of multiple isomorphous replacement, multiwavelength anomalous diffraction and molecular replacement are still in progress.
Chapitres de livres sur le sujet "Heme-binding protein 2"
Morishima, Isao. « Pressure Effects on the Ligand-Binding Kinetics for Hemoproteins and Their Site-Directed Mutants ». Dans High Pressure Effects in Molecular Biophysics and Enzymology. Oxford University Press, 1996. http://dx.doi.org/10.1093/oso/9780195097221.003.0016.
Texte intégralSaito, Jennifer A., Tracey Allen K. Freitas et Maqsudul Alam. « Cloning, Expression, and Purification of the N-terminal Heme-Binding Domain of Globin-Coupled Sensors ». Dans Globins and Other Nitric Oxide-Reactive Proteins, Part B, 163–72. Elsevier, 2008. http://dx.doi.org/10.1016/s0076-6879(07)37009-2.
Texte intégralActes de conférences sur le sujet "Heme-binding protein 2"
Dyer, R. Brian, et Timothy P. Causgrove. « Ultrafast Protein Relaxation : Time-Resolved Infrared Studies of Protein Dynamics Triggered by CO Photodissociation from CO Myoglobin ». Dans International Conference on Ultrafast Phenomena. Washington, D.C. : Optica Publishing Group, 1994. http://dx.doi.org/10.1364/up.1994.tub.4.
Texte intégralHill, Jeffrey R., Matthew J. Cote, Dana D. Dlott, John F. Kauffman, J. Douglas McDonald, Peter J. Steinbach, Joel R. Berendzen et Hans Frauenfelder. « Chemical Reaction in a Glassy Matrix : Dynamics of Ligand Binding to Protoheme in Glycerol : Water ». Dans International Conference on Ultrafast Phenomena. Washington, D.C. : Optica Publishing Group, 1986. http://dx.doi.org/10.1364/up.1986.wf8.
Texte intégralGenberg, L., L. Richard, S. Gracewski, G. McLendon et R. J. D. Miller. « Picosecond Transient Phase Grating Studies of the Energetics and Structure Dynamics of Heme Proteins ». Dans International Conference on Ultrafast Phenomena. Washington, D.C. : Optica Publishing Group, 1990. http://dx.doi.org/10.1364/up.1990.mb3.
Texte intégralRapports d'organisations sur le sujet "Heme-binding protein 2"
Ohad, 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.
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