Gotowa bibliografia na temat „Phosphoesterase”
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Artykuły w czasopismach na temat "Phosphoesterase"
Ogden, Kristen M., Liya Hu, Babal K. Jha, Banumathi Sankaran, Susan R. Weiss, Robert H. Silverman, John T. Patton i B. V. Venkataram Prasad. "Structural Basis for 2′-5′-Oligoadenylate Binding and Enzyme Activity of a Viral RNase L Antagonist". Journal of Virology 89, nr 13 (15.04.2015): 6633–45. http://dx.doi.org/10.1128/jvi.00701-15.
Pełny tekst źródłaYin, Yue, David Frank, Weijie Zhou, Neena Kaur, Jarrod B. French i Nick Carpino. "An unexpected 2-histidine phosphoesterase activity of suppressor of T-cell receptor signaling protein 1 contributes to the suppression of cell signaling". Journal of Biological Chemistry 295, nr 25 (5.05.2020): 8514–23. http://dx.doi.org/10.1074/jbc.ra120.013482.
Pełny tekst źródłaKatz, Michael J., Su-Young Moon, Joseph E. Mondloch, M. Hassan Beyzavi, Casey J. Stephenson, Joseph T. Hupp i Omar K. Farha. "Exploiting parameter space in MOFs: a 20-fold enhancement of phosphate-ester hydrolysis with UiO-66-NH2". Chemical Science 6, nr 4 (2015): 2286–91. http://dx.doi.org/10.1039/c4sc03613a.
Pełny tekst źródłaHan, Gye Won, Jaeju Ko, Carol L. Farr, Marc C. Deller, Qingping Xu, Hsiu-Ju Chiu, Mitchell D. Miller i in. "Crystal structure of a metal-dependent phosphoesterase (YP_910028.1) from Bifidobacterium adolescentis: Computational prediction and experimental validation of phosphoesterase activity". Proteins: Structure, Function, and Bioinformatics 79, nr 7 (2.05.2011): 2146–60. http://dx.doi.org/10.1002/prot.23035.
Pełny tekst źródłaLi, Xiao-Yu. "Clinical application of phosphoesterase complex in liver diseases". World Chinese Journal of Digestology 22, nr 29 (2014): 4424. http://dx.doi.org/10.11569/wcjd.v22.i29.4424.
Pełny tekst źródłaGold, Matthew G., F. Donelson Smith, John D. Scott i David Barford. "AKAP18 Contains a Phosphoesterase Domain that Binds AMP". Journal of Molecular Biology 375, nr 5 (luty 2008): 1329–43. http://dx.doi.org/10.1016/j.jmb.2007.11.037.
Pełny tekst źródłaBressan, Debra A., Heidi A. Olivares, Benjamin E. Nelms i John H. J. Petrini. "Alteration of N-Terminal Phosphoesterase Signature Motifs Inactivates Saccharomyces cerevisiae Mre11". Genetics 150, nr 2 (1.10.1998): 591–600. http://dx.doi.org/10.1093/genetics/150.2.591.
Pełny tekst źródłaAravind, L., i E. V. Koonin. "Phosphoesterase domains associated with DNA polymerases of diverse origins". Nucleic Acids Research 26, nr 16 (1.08.1998): 3746–52. http://dx.doi.org/10.1093/nar/26.16.3746.
Pełny tekst źródłaQuist, Eugene. "Ca2+-stimulated phospholipid phosphoesterase activities in rabbit erythrocyte membranes". Archives of Biochemistry and Biophysics 236, nr 1 (styczeń 1985): 140–49. http://dx.doi.org/10.1016/0003-9861(85)90613-7.
Pełny tekst źródłaBreaker, Ronald R., i Gerald F. Joyce. "A DNA enzyme with Mg2+-dependent RNA phosphoesterase activity". Chemistry & Biology 2, nr 10 (październik 1995): 655–60. http://dx.doi.org/10.1016/1074-5521(95)90028-4.
Pełny tekst źródłaRozprawy doktorskie na temat "Phosphoesterase"
Daver, Henrik. "Quantum Chemical Modeling of Phosphoesterase Mimics and Chemistry in Confined Spaces". Doctoral thesis, Stockholms universitet, Institutionen för organisk kemi, 2017. http://urn.kb.se/resolve?urn=urn:nbn:se:su:diva-148259.
Pełny tekst źródłaAt the time of the doctoral defense, the following paper was unpublished and had a status as follows: Paper 5: Manuscript.
McMillen, Lyle, i l. mcmillen@sct gu edu au. "Isolation and Characterisation of the 5'-Nucleotidase from Escherichia coli". Griffith University. School of Biomolecular and Biomedical Science, 2001. http://www4.gu.edu.au:8080/adt-root/public/adt-QGU20030226.153545.
Pełny tekst źródłaMcMillen, Lyle. "Isolation and Characterisation of the 5'-Nucleotidase from Escherichia coli". Thesis, Griffith University, 2001. http://hdl.handle.net/10072/366487.
Pełny tekst źródłaThesis (PhD Doctorate)
Doctor of Philosophy (PhD)
School of Biomolecular and Biomedical Sciences
Science, Environment, Engineering and Technology
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Gusho, Elona. "AKAP7 Degrades 2-5A Mediators of the Interferon Antiviral Response". Cleveland State University / OhioLINK, 2015. http://rave.ohiolink.edu/etdc/view?acc_num=csu1449496406.
Pełny tekst źródłaAwal, Sushil. "Targeting ubiquitin receptor protein UBASH3B for future cancer therapies". Thesis, Strasbourg, 2019. http://www.theses.fr/2019STRAJ094.
Pełny tekst źródłaDefects in proper segregation of chromosomes during mitosis result in aneuploidy or polyploidy. UBASH3B protein, a ubiquitin-binding protein, plays a crucial role in driving Aurora B to microtubules before anaphase onset for proper chromosome segregation. We here performed a high-throughput screening to screen out a novel small-molecule UBASH3B inhibitor, FD-E09 using recombinant UBASH3 protein. Treatment with UBASH3B inhibitor led to the spreading of Aurora B to chromosomal arms during prometaphase, thus affecting the timing and fidelity of mitosis. It also affects the UBASH3B-Aurora B-MKlp2 complex. My data also unfold the 2 Histidine phosphoesterase domain in UBASH3B between UBA and SH3 domain that plays a role in proper localization of Aurora B, mitotic progression, as well as interaction with Aurora B and MKlp2. We also screened out the cancer cell lines that are responsive to the UBASH3B inhibition. Hence, our findings uncover the small-molecule UBASH3B inhibitor that could target UBASH3B to treat specific cancer cells and also uncover newly identified 2H phosphoesterase domain in UBASH3B that regulates Aurora B localization in mitosis
Duboc-Toia, Carole. "Réactivité chimique des complexes dinucléaires de fer (III) à pont oxo : applications en catalyse d'oxydation énantiosélective et en hydrolyse de phosphoesters". Université Joseph Fourier (Grenoble), 1998. http://www.theses.fr/1998GRE10092.
Pełny tekst źródłaCzęści książek na temat "Phosphoesterase"
Daumann, Lena Josefine. "Structural and Mechanistic Studies of Zn(II) Complexes as Phosphoesterase Models". W Spectroscopic and Mechanistic Studies of Dinuclear Metallohydrolases and Their Biomimetic Complexes, 89–117. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-06629-5_4.
Pełny tekst źródłaDaumann, Lena Josefine. "Mechanistic Studies of Cd(II) Complexes as Phosphoesterase and Metallo-β-lactamase Models". W Spectroscopic and Mechanistic Studies of Dinuclear Metallohydrolases and Their Biomimetic Complexes, 119–43. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-06629-5_5.
Pełny tekst źródłaDaumann, Lena Josefine. "Spectroscopic and Mechanistic Studies of Co(II) Phosphoesterase and Metallo-β-lactamase Biomimetics". W Spectroscopic and Mechanistic Studies of Dinuclear Metallohydrolases and Their Biomimetic Complexes, 145–88. Cham: Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-06629-5_6.
Pełny tekst źródłaTole, Philip, i Carmay Lim. "Do Stereoelectronic Effects Control the Structure and Reactivity of Trigonal-Bipyramidal Phosphoesters?" W ACS Symposium Series, 240–55. Washington, DC: American Chemical Society, 1993. http://dx.doi.org/10.1021/bk-1993-0539.ch013.
Pełny tekst źródłaKrämer, Roland, i Tamás Gajda. "Functional model complexes for dinuclear phosphoesterase enzymes". W Perspectives on Bioinorganic Chemistry, 209–40. Elsevier, 1999. http://dx.doi.org/10.1016/s1062-239x(99)80032-7.
Pełny tekst źródłaRaporty organizacyjne na temat "Phosphoesterase"
Chin, Jik. Artificial Metallo-Phosphoesterase. Fort Belvoir, VA: Defense Technical Information Center, maj 2001. http://dx.doi.org/10.21236/ada394524.
Pełny tekst źródłaChin, Jik. Artificial Phosphoesterase: Metal Activation by Strain. Fort Belvoir, VA: Defense Technical Information Center, czerwiec 1993. http://dx.doi.org/10.21236/ada271367.
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