Literatura académica sobre el tema "ADN Ligase"
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Artículos de revistas sobre el tema "ADN Ligase"
Lee, Jaeseok, Youngjun Lee, Young Mee Jung, Ju Hyun Park, Hyuk Sang Yoo y Jongmin Park. "Discovery of E3 Ligase Ligands for Target Protein Degradation". Molecules 27, n.º 19 (2 de octubre de 2022): 6515. http://dx.doi.org/10.3390/molecules27196515.
Texto completoTomkinson, Alan E., Tasmin Naila y Seema Khattri Bhandari. "Altered DNA ligase activity in human disease". Mutagenesis 35, n.º 1 (20 de octubre de 2019): 51–60. http://dx.doi.org/10.1093/mutage/gez026.
Texto completoCao, Weiguo. "DNA ligases and ligase-based technologies". Clinical and Applied Immunology Reviews 2, n.º 1 (noviembre de 2001): 33–43. http://dx.doi.org/10.1016/s1529-1049(01)00039-3.
Texto completoFang, Deyu, An Chen y Sang-Myeong Lee. "Inhibition of activation-induced T cell death by AIP2-mediated ubiquitination of EGR2 (35.20)". Journal of Immunology 182, n.º 1_Supplement (1 de abril de 2009): 35.20. http://dx.doi.org/10.4049/jimmunol.182.supp.35.20.
Texto completoKennan, Alan J., V. Haridas, Kay Severin, David H. Lee y M. Reza Ghadiri. "Ade NovoDesigned Peptide Ligase: A Mechanistic Investigation". Journal of the American Chemical Society 123, n.º 9 (marzo de 2001): 1797–803. http://dx.doi.org/10.1021/ja991266c.
Texto completoFanucci, Francesco. "Quaternary shorelines and continental shelf of the Ligurian coast". Zeitschrift für Geomorphologie 31, n.º 4 (17 de diciembre de 1987): 463–72. http://dx.doi.org/10.1127/zfg/31/1987/463.
Texto completoGu, Jiafeng, Haihui Lu, Brigette Tippin, Noriko Shimazaki, Myron F. Goodman y Michael R. Lieber. "XRCC4:DNA ligase IV can ligate incompatible DNA ends and can ligate across gaps". EMBO Journal 26, n.º 14 (25 de julio de 2007): 3506–7. http://dx.doi.org/10.1038/sj.emboj.7601729.
Texto completoThayale Purayil, Fayas, Naganeeswaran Sudalaimuthuasari, Ling Li, Ruwan Aljneibi, Aysha Mohammed Khamis Al Shamsi, Nelson David, Martin Kottackal et al. "Transcriptome Profiling and Functional Validation of RING-Type E3 Ligases in Halophyte Sesuvium verrucosum under Salinity Stress". International Journal of Molecular Sciences 23, n.º 5 (4 de marzo de 2022): 2821. http://dx.doi.org/10.3390/ijms23052821.
Texto completoGong, Yao y Yue Chen. "UbE3-APA: a bioinformatic strategy to elucidate ubiquitin E3 ligase activities in quantitative proteomics study". Bioinformatics 38, n.º 8 (9 de febrero de 2022): 2211–18. http://dx.doi.org/10.1093/bioinformatics/btac069.
Texto completoAlomari, Arqam, Robert Gowland, Callum Southwood, Jak Barrow, Zoe Bentley, Jashel Calvin-Nelson, Alice Kaminski et al. "Identification of Novel Inhibitors of Escherichia coli DNA Ligase (LigA)". Molecules 26, n.º 9 (25 de abril de 2021): 2508. http://dx.doi.org/10.3390/molecules26092508.
Texto completoTesis sobre el tema "ADN Ligase"
Touzé, Elodie Giegé Richard. "Cristallogenèse et études structurales appliquées aux aminoacyl-ARNt synthétases". Strasbourg : Université Louis Pasteur, 2008. http://eprints-scd-ulp.u-strasbg.fr:8080/911/01/TOUZE_Elodie_2007.pdf.
Texto completoMenchon, Grégory. "Criblage virtuel et fonctionnel sur le complexe XRCC4/ADN ligase IV/Cer-XLF de ligature des cassures double-brin de l'ADN : application en radiosensibilisation tumorale". Thesis, Toulouse 3, 2015. http://www.theses.fr/2015TOU30395.
Texto completoRadiotherapy is a major weapon used against cancer. Radio-induced DNA double strand breaks (DSB) are the main lesions responsible for cell death. Non-homologous end-joining (NHEJ) is a predominant DSB repair mechanism which contributes to cancer cells resistance to radiotherapy. NHEJ is thus a good target for strategies which aim at increasing the radio-sensitivity of tumors. Through in silico screening and biophysical and biochemical assays, our objective was to find specific ligands for the XRCC4/Lig4 and XRCC4/Cer-XLF protein-protein interactions involved in NHEJ. Here, we isolated the first compounds able to prevent their interaction in vitro. These early stage inhibitors are promising tools for cancer therapy with the hope to develop more specific compounds for cellular assays through the 3D structure of the protein/inhibitor complexes
De, Melo Abinadabe Jackson. "Molecular basis for the structural role of human DNA ligase IV". Thesis, Aix-Marseille, 2016. http://www.theses.fr/2016AIXM4040.
Texto completoFailure to repair DNA double-strand breaks (DSBs) may have deleterious consequences inducing genomic instability and even cell death. In most mammalian cells, Non-Homologous End Joining (NHEJ) is a prominent DSB repair pathway. DNA ligase IV (LigIV) is unique in its ability to promote classical NHEJ. It associates with two structurally related proteins called XRCC4 and XLF (aka Cernunnos). LigIV directly interacts with XRCC4 forming a stable complex while the XLF interaction with this complex is mediated by XRCC4. XLF strongly stimulates the ligation activity of the LigIV/XRCC4 complex by an unknown mechanism. Recently, a structural noncatalytic role of LigIV has been uncovered (Cottarel et al., 2013). Here, we have reconstituted the end joining ligation step using recombinant proteins produced in bacteria to explore not only the molecular basis for the structural role of LigIV, but also to understand the mechanism by which XLF stimulates the ligation complex, and how these three proteins work together during NHEJ. Our biochemical analysis suggests that XLF, through interactions with LigIV/XRCC4 complex, could induce a conformational change in LigIV. Rearrangement of the LigIV would expose its DNA binding interface that is able to bridge two independent DNA molecules. This bridging ability is fully independent of LigIV’s catalytic activity. We have mutated this interface in order to attempt to disrupt the newly identified DNA bridging ability. In vitro analysis of this LigIV mutant will be presented as well as a preliminary in vivo analysis
Wu, Pei-Yu. "Le complexe de ligation dans la réaction de réparation des cassures de l'ADN par recombination non homologué". Toulouse 3, 2008. http://www.theses.fr/2008TOU30064.
Texto completoDNA double-strand breaks (DSBs) are the most lethal threats among all the DNA damages in cells. They can arise not only endogenously from normal physiological processes such as V(D)J recombination or toxic lesions like DNA replication forks collapses, but also exogenously from DNA damaging agents like ionizing radiation (IR) or radiomimetic compounds. In mammals, DSBs are mainly repaired by homologous recombination (HR) during S and G2 phases of the cell cycle when sister chromatids are available, and, more predominantly, in all the phases of cell cycle by the non-homologous end-joining (NHEJ) pathway without any requirement for homology guidance. The NHEJ machinery is also involved in V(D)J recombination to rearrange B-cell immunoglobulin and T-cell receptor genes. Deficiency in NHEJ consequently results in hypersensitivity to IR, immunodeficiency, as well as chromosomal instability. After DSBs induction, Ku70/Ku80 heterodimer binds to free DNA ends, allowing the subsequent recruitment and activation of the DNA-dependent protein kinase catalytic subunit (DNA-PKcs). The resulting DNA-PK holoenzyme (i. E. Ku/DNA-PKcs or Complex-1) tethers two DNA termini and form the synaptic complex that may further activates DNA-PKcs by several (auto)phosphorylation events. Upon activation, Complex-1 undergoes conformational changes to accommodate the ligation complex (Complex-2) and accessory factors that make DNA ends compatible with ligation, when necessary. Complex-2 comprises XRCC4, DNA LigIV (LigIV) and the more recently identified factor Cernunnos-XLF (Cer-XLF). The three partners interact with each other and Complex-2 also binds Complex-1 and accessory factors, thus accounting for its highly efficient end-joining activity. In this work we aimed at characterizing the intimate interaction network between Complex-2 factors. .
Nassar, Joelle. "Caractérisation de la fonction de OBI1, une E3 ubiquitine ligase, dans la réplication de l'ADN". Thesis, Montpellier, 2019. http://www.theses.fr/2019MONTT039.
Texto completoCell division is one of the most complex processes a cell undergoes. For this to happen properly, the genetic material stored in a cell must be faithfully copied or replicated. During this process, DNA replication is initiated at pre-defined sites in the genome, called "origins of replication". The activation of these origins is highly regulated, as a dysfunction in origin activity is linked to several human pathologies. Several proteins have been found at replication origins, but none of them explain how to be activated origins are recognized and selected. Our research group aims to understand how DNA replication origins are regulated in metazoan cells, to this aim, a proteomic approach was performed to define the interactome of human replication origins. Our goal was to identify new factors that could be involved in replication origin regulation. Using this methodology, a novel E3 ubiquitin ligase, named OBI1 (for ORC-ubiquitin-ligase-1), was identified prior to my arrival in the laboratory. OBI1 binds the origin recognition complex (ORC complex) and my project aimed at further characterizing the role of this new protein in DNA replication. Our experimental strategy used two different model systems: an in-vivo model based on human cells in culture, and an in-vitro DNA replication system derived from Xenopus eggs.Our analyses in human cells revealed that OBI1 was a crucial gene involved in cellular proliferation, this observation was later attributed to OBI1’s role in DNA replication and more specifically, to replication origin activation. Indeed, OBI1 knockdown resulted in a deficient origin firing and a decrease in the chromatin recruitment of factors involved in origin firing. A further functional analysis showed that OBI1 multiubiquitylates two subunits of the ORC complex, ORC3 and ORC5. This ubiquitylation was directly linked to OBI1’s role in origin firing, after the over-expression of non-ubiquitylable ORC3/5 mutants yielded similar results to OBI1’s knock down. Altogether, our results demonstrated that OBI1 encoded for a protein essential for origin activation, and allowed us to propose its main role: by multiubiquitylating a subset of the ORC complex, OBI1 could select the replication origins to be activated amongst all the potential replication origins set in G1 phase of the cell cycle. After this set of experiments, now published, we wanted to address the mechanistic impact of the multiubiquitylation of ORC on origin activation. Our preliminary experiments suggest a role of the histone acetyl-transferase (HAT) GCN5/KAT2A in the “OBI1 pathway”In the second part of my project, we used the in vitro DNA replication system, based on Xenopus laevis egg extracts, to study the role of OBI1 and ubiquitylation in origin activation. Our in-vitro analyses confirmed the conservation of OBI1 in Xenopus Laevis and its recruitment to the chromatin during DNA replication. We showed that de novo ubiquitylation takes place on chromatin during origin activation. Moreover, using E1 inhibitors, we found that active ubiquitylation is important for efficient origin firing. Interestingly, our loss of function experiments suggested that OBI1’s impact on origin activation could defer in early development when compared to somatic-like conditions.Taken together, the discovery of this new replication initiation factor provided key information on the role of ubiquitylation in general and OBI1 in particular on origin activation and selection. Such selection could participate as well in the regulation of the timing of DNA replication
Amram, Jérémy. "Etude structurale et fonctionnelle des complexes multi-protéiques de la voie de réparation NHEJ chez l’homme". Thesis, Paris 11, 2015. http://www.theses.fr/2015PA114822/document.
Texto completoHuman DNA repair pathway NHEJ (Non-Homologous End-Joining) is a major pathway of double-strand breaks repair. The proteins involved in this pathway interact and form dynamic complexes whose molecular mechanisms are largely unknown. Firstly, we established protocols to be able to purify milligrams of those NHEJ pathway core proteins using MultiBac insect cells system. We then purified Ku70/Ku80 and Ligase4/XRCC4 complexes, Artemis and Cernunnos to homogeneity. Crystallogenesis assays, SAXS experiments and Transmission Electronic Microscopy experiments have been performed on several complexes formed by these core NHEJ proteins. We also characterized the interactions between these proteins by Size Exclusion Chromatography and Isothermal Calorimetry. These experiments have led to biochemical results sufficient to establish a solid basis to initiate the structural and functional study of the Human NHEJ Pathway
Aoufouchi, Said. "Adn ligases chez les eucaryotes superieurs". Rennes 1, 1992. http://www.theses.fr/1992REN10016.
Texto completoCastagné, Claire. "Analyse par résonance magnétique nucléaire des interactions ADN-protéine : étude des facteurs de transcription Rev-erb [bêta] et SRY ; détermination de la structure secondaire du domaine C-terminal de la tyrosyl'RNA synthétase". Université Joseph Fourier (Grenoble), 1999. http://www.theses.fr/1999GRE10039.
Texto completoTouzé, Elodie. "Cristallogenèse et études structurales appliquées aux aminoacyl-ARNt synthétases". Phd thesis, Université Louis Pasteur - Strasbourg I, 2007. http://tel.archives-ouvertes.fr/tel-00206952.
Texto completoDorison, Hugo. "Sumo-Directed Control of the Resolvase Yen1 in Mitotic Cells Slx5-Slx8 Ubiquitin Ligase Targets Active Pools of the Yen1 Nuclease To Limit Crossover Formation SUMO-Mediated Recruitment Allows Timely Function of the Yen1 Nuclease". Thesis, université Paris-Saclay, 2021. http://www.theses.fr/2021UPASL003.
Texto completoThe repair of double-stranded DNA breaks (DSBs) by homologous recombination involves the formation of branched intermediates that can lead to crossovers following nucleolytic resolution. Ubiquitin and SUMO modification is commonplace amongst the DNA damage repair proteins. What is more, a number of DSB repair factors interact with each other when sumoylated, making use of SUMO interaction motifs (SIMs). The nuclease Yen1 is tightly controlled during the cell cycle to limit the extent of crossover formation and preserve genome integrity. In this manuscript we describe further regulation of Yen1 by ubiquitination, sumoylation and non-covalent interaction with SUMO through its newly characterized SIMs. Yen1 is sumoylated by Siz1 and Siz2 SUMO ligases, especially in conditions of DNA damage. Furthermore, Yen1 is a substrate of the Slx5-Slx8 ubiquitin ligase. Loss of Slx5-Slx8 stabilizes the sumoylated fraction of Yen1, and results in persistent localization of Yen1 in nuclear foci. Slx5-Slx8-dependent ubiquitination of Yen1 occurs mainly at K714 and mutation of this lysine increases crossover formation during DSB repair and suppresses chromosome segregation defects when other nucleases are unavailable. In addition, proper and timely nucleolytic processing from Yen1 is dependent on interactions mediated by non-covalent binding to sumoylated partners. Mutations in the motifs that allow SUMO-mediated recruitment of Yen1 leads to its mis-localization, decreasing Yen1’s ability to resolve DNA joint-molecule intermediates and resulting in increased genome instability and chromosome mis-segregation
Libros sobre el tema "ADN Ligase"
Gómez, Ramón Terol. Las ligas profesionales. [Spain]: Fundación del Fútbol Profesional, 1998.
Buscar texto completoLigabue, Antonio. Ligabue. Cavallermaggiore [Italy]: Gribaudo, 1995.
Buscar texto completoCatran, Ken. Bloody Liggie. St. Lucia: University of Queensland Press, 2003.
Buscar texto completoBoulaga, F. Eboussi. Lignes de résistance. Yaoundé: Editions CLE, 1999.
Buscar texto completoMorais, Clodomir. História das Ligas Camponesas do Brasil. Brasília, DF: Edições Instituto de Apoio Técnico aos Países de Terceiro Mundo, 1997.
Buscar texto completoCaffier, Michel. Nancy entre les lignes. Nancy: Presses universitaires de Nancy, 1993.
Buscar texto completoY cómo eran las ligas de Madame Bovary? Barcelona: Ediciones Destino, 2003.
Buscar texto completoRazauskas, Romualdas. Juoko piliulės: Anekdotai apie ligas, ligonius ir gydytojus. Vilnius: UAB Mileta, 2002.
Buscar texto completoFabio, Francione, ed. Il cinema di Luciano Ligabue. Alessandria: Falsopiano, 2004.
Buscar texto completoAlechinsky, Pierre. Alechinsky: Entre les lignes. Paris: Y. Rivière, 1996.
Buscar texto completoCapítulos de libros sobre el tema "ADN Ligase"
Chistiakov, Dimitry A. "Ligase IV Syndrome". En Advances in Experimental Medicine and Biology, 175–85. New York, NY: Springer New York, 2010. http://dx.doi.org/10.1007/978-1-4419-6448-9_16.
Texto completoSchomburg, Dietmar y Ida Schomburg. "Mn2+-dependent ADP-ribose/CDP-alcohol diphosphatase 3.6.1.53". En Class 3.4–6 Hydrolases, Lyases, Isomerases, Ligases, 303–8. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-36260-6_22.
Texto completoSchwehr, Bradley J., David Hartnell, Massimiliano Massi y Mark J. Hackett. "Luminescent metal complexes as emerging tools for lipid imaging". En Metal Ligand Chromophores for Bioassays, 75–114. Cham: Springer International Publishing, 2022. http://dx.doi.org/10.1007/978-3-031-19863-2_3.
Texto completoProske, Uwe, David L. Morgan, Tamara Hew-Butler, Kevin G. Keenan, Roger M. Enoka, Sebastian Sixt, Josef Niebauer et al. "E3 Ubiquitin Ligases". En Encyclopedia of Exercise Medicine in Health and Disease, 269. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-540-29807-6_2315.
Texto completoYu, Tao, Yinfeng Zhang y Pei-feng Li. "Mitochondrial Ubiquitin Ligase in Cardiovascular Disorders". En Advances in Experimental Medicine and Biology, 327–33. Cham: Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-55330-6_17.
Texto completoTauler Riera, Pedro, Maurizio Volterrani, Ferdinando Iellamo, Francesco Fallo, Andrea Ermolao, William J. Kraemer, Nicholas A. Ratamess, Avery Faigenbaum, Andrew Philp y Keith Baar. "RANK Ligand". En Encyclopedia of Exercise Medicine in Health and Disease, 749. Berlin, Heidelberg: Springer Berlin Heidelberg, 2012. http://dx.doi.org/10.1007/978-3-540-29807-6_2939.
Texto completoIshino, Sonoko y Yoshizumi Ishino. "DNA Polymerases and DNA Ligases". En Thermophilic Microbes in Environmental and Industrial Biotechnology, 429–57. Dordrecht: Springer Netherlands, 2013. http://dx.doi.org/10.1007/978-94-007-5899-5_17.
Texto completoFu, Lin, Chun-Ping Cui y Lingqiang Zhang. "Regulation of Stem Cells by Cullin-RING Ligase". En Advances in Experimental Medicine and Biology, 79–98. Singapore: Springer Singapore, 2020. http://dx.doi.org/10.1007/978-981-15-1025-0_6.
Texto completoKershaw, Christopher J. y Raymond T. O’Keefe. "Splint Ligation of RNA with T4 DNA Ligase". En Recombinant and In Vitro RNA Synthesis, 257–69. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-62703-113-4_19.
Texto completoChang, Hsuan-Ping y Dhaval K. Shah. "Determination of ADC Concentration by Ligand-Binding Assays". En Methods in Molecular Biology, 361–69. New York, NY: Springer US, 2019. http://dx.doi.org/10.1007/978-1-4939-9929-3_26.
Texto completoActas de conferencias sobre el tema "ADN Ligase"
Chandra, S. y V. Kumar. "Thermodynamic Properties of LiGaS2 and LiGaSe2 using First-Principle Calculations". En 2018 5th IEEE Uttar Pradesh Section International Conference on Electrical, Electronics and Computer Engineering (UPCON). IEEE, 2018. http://dx.doi.org/10.1109/upcon.2018.8596990.
Texto completoChandra, Satish, V. Kumar y Yadvendra Singh. "First-principle calculations of Debye temperature of optoelectronic LiGaS2 and LiGaSe2 semiconductors under different pressures". En Optical Components and Materials XVI, editado por Michel J. Digonnet y Shibin Jiang. SPIE, 2019. http://dx.doi.org/10.1117/12.2506878.
Texto completoBarrett, Dwhyte O., Amit Maha, Yun Wang, Steven A. Soper, Dimitris E. Nikitopoulos y Michael C. Murphy. "Design of a Microfabricated Device for the Ligase Detection Reaction (LDR)". En ASME 2004 International Mechanical Engineering Congress and Exposition. ASMEDC, 2004. http://dx.doi.org/10.1115/imece2004-62111.
Texto completoLee, Tae Yoon, Dimistris E. Nikitopoulos, Daniel S. Park, Steven A. Soper y Michael C. Murphy. "Design and Fabrication of a Ligase Detection Reaction (LDR) Microchip With an Integrated Passive Micromixer". En ASME 2007 International Mechanical Engineering Congress and Exposition. ASMEDC, 2007. http://dx.doi.org/10.1115/imece2007-42216.
Texto completoLim, Manko, Timothy A. Jackson y Philip A. Anfinrud. "Ultrafast Near-IR Spectroscopy of Carbonmonoxymyoglobin: the Dynamics of Protein Relaxation". En International Conference on Ultrafast Phenomena. Washington, D.C.: Optica Publishing Group, 1992. http://dx.doi.org/10.1364/up.1992.thb3.
Texto completoSteimle, Timothy C., Boa-Zhong Li y Kook Young Jung. "Molecular Beam Optical Stark and PPMODR Spectroscopy of Pt Containing Molecules". En Modern Spectroscopy of Solids, Liquids, and Gases. Washington, D.C.: Optica Publishing Group, 1995. http://dx.doi.org/10.1364/msslg.1995.ssaa4.
Texto completoKawaguchi, Kazutomo, Hiroyuki Takagi, Masako Takasu, Hiroaki Saito y Hidemi Nagao. "Molecular dynamics studies of Hsp90 with ADP: Protein-ligand binding dynamics". En 4TH INTERNATIONAL SYMPOSIUM ON SLOW DYNAMICS IN COMPLEX SYSTEMS: Keep Going Tohoku. American Institute of Physics, 2013. http://dx.doi.org/10.1063/1.4794650.
Texto completoM. H. Obaid, Shatha, Taghreed H. Al-Noor y Noor A. Hussien. "Preparation, Spectra and Biological Properties of Transition Metals ((III) and (II) Mixed - Ligand Complexes with 5-Chlorosalicylic Acid and L-Valine". En المؤتمر العلمي الدولي العاشر. شبكة المؤتمرات العربية, 2019. http://dx.doi.org/10.24897/acn.64.68.466.
Texto completoJelínek, Michal, Vaclav Kubecek, Miroslav Cech, Sergei Smetanin, Aleksey Kurus, Sergei Lobanov, Vitaliy Vedenyapin y Lyudmila Isaenko. "Narrowband difference-frequency generation at 4.6, 5.4, 7.5, 9.2, and 10.8 μm in LiGaS2 and LiGaSe2 pumped by 20-ps Nd:YAG laser and Raman laser seeding". En Solid State Lasers XXX: Technology and Devices, editado por W. Andrew Clarkson y Ramesh K. Shori. SPIE, 2021. http://dx.doi.org/10.1117/12.2579178.
Texto completoBarrett, Dwhyte O., Amit Maha, Yun Wang, Steven A. Soper, Dimitris E. Nikitopoulos y Michael C. Murphy. "Design of a microfabricated device for ligase detection reaction (LDR)". En Micromachining and Microfabrication, editado por Peter Woias y Ian Papautsky. SPIE, 2004. http://dx.doi.org/10.1117/12.524681.
Texto completoInformes sobre el tema "ADN Ligase"
Royer, Lacey. Cul3 Ubiquitin Ligase and Ctb73 Protein Interactions. Portland State University Library, enero de 2014. http://dx.doi.org/10.15760/honors.48.
Texto completoDavidge, Brittney. The Cul3 Ubiquitin Ligase: An Essential Regulator of Diverse Cellular Processes. Portland State University Library, enero de 2000. http://dx.doi.org/10.15760/etd.5666.
Texto completoMitchell, Jennifer. Characterization of Functional Domains of Cul3, an E3 Ubiquitin Ligase, Using Chimeric Analysis. Portland State University Library, enero de 2000. http://dx.doi.org/10.15760/etd.1969.
Texto completoRaj, Ganesh V. Targeting Ligand Dependent and Ligand Independent Androgen Receptor Signaling in Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, octubre de 2014. http://dx.doi.org/10.21236/ada613818.
Texto completoRaj, Ganesh V. Targeting Ligand-Dependent and Ligand-Independent Androgen Receptor Signaling in Prostate Cancer. Fort Belvoir, VA: Defense Technical Information Center, octubre de 2013. http://dx.doi.org/10.21236/ada604653.
Texto completoSLACK, JEFFREY, M. IDENTIFICATION, PRODUCTION AND CHARACTERIZATION OF NOVEL LIGNASE PROTEINS FROM TERMITES FOR DEPOLYMERIZATION OF LIGNOCELLULOSE. Office of Scientific and Technical Information (OSTI), diciembre de 2012. http://dx.doi.org/10.2172/1056676.
Texto completoSzigethy, Geza. Rational Ligand Design for U(VI) and Pu(IV). Office of Scientific and Technical Information (OSTI), agosto de 2009. http://dx.doi.org/10.2172/972716.
Texto completoKelley, DAVID. Ligand-Controlled Energetics and Charge Transfer in Pure and Doped Nanocrystals. Office of Scientific and Technical Information (OSTI), febrero de 2021. http://dx.doi.org/10.2172/1766125.
Texto completoHovey, Megan. Ligand strategies for green chemistry. Catalysts for amide reduction and hydroamination. Office of Scientific and Technical Information (OSTI), enero de 2014. http://dx.doi.org/10.2172/1226561.
Texto completoMa, Buyong y Ruth Nussinov. Computational Study of Cytolytic Peptides: Monomeric-Oligomeric Structures and Ligand Interactions. Fort Belvoir, VA: Defense Technical Information Center, noviembre de 2005. http://dx.doi.org/10.21236/ada444931.
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