Academic literature on the topic 'Ubiquitin-conjugates'

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Journal articles on the topic "Ubiquitin-conjugates"

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Jabben, M., J. Shanklin, and R. D. Vierstra. "Ubiquitin-Phytochrome Conjugates." Journal of Biological Chemistry 264, no. 9 (1989): 4998–5005. http://dx.doi.org/10.1016/s0021-9258(18)83690-0.

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Carlson, N., and M. Rechsteiner. "Microinjection of ubiquitin: intracellular distribution and metabolism in HeLa cells maintained under normal physiological conditions." Journal of Cell Biology 104, no. 3 (1987): 537–46. http://dx.doi.org/10.1083/jcb.104.3.537.

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Radioiodinated ubiquitin was introduced into HeLa cells by erythrocyte-mediated microinjection. Subsequent electrophoretic analyses revealed that the injected ubiquitin molecules were rapidly conjugated to HeLa proteins. At equilibrium, 10% of the injected ubiquitin was conjugated to histones and 40% was distributed among conjugates of higher molecular weight. Although the remaining ubiquitin molecules appeared to be unconjugated, the free pool of ubiquitin decreased by one-third and additional conjugates were present when electrophoresis was performed at low temperature under nonreducing cond
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Jahngen-Hodge, Jessica, Deanna Cyr, Eric Laxman, and Allen Taylor. "Ubiquitin and ubiquitin conjugates in human lens." Experimental Eye Research 55, no. 6 (1992): 897–902. http://dx.doi.org/10.1016/0014-4835(92)90016-l.

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Carlson, N., S. Rogers, and M. Rechsteiner. "Microinjection of ubiquitin: changes in protein degradation in HeLa cells subjected to heat-shock." Journal of Cell Biology 104, no. 3 (1987): 547–55. http://dx.doi.org/10.1083/jcb.104.3.547.

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Ubiquitin was radiolabeled by reaction with 125I-Bolton-Hunter reagent and introduced into HeLa cells using erythrocyte-mediated microinjection. The injected cells were then incubated at 45 degrees C for 5 min (reversible heat-shock) or for 30 min (lethal heat-shock). After either treatment, there were dramatic changes in the levels of ubiquitin conjugates. Under normal culture conditions, approximately 10% of the injected ubiquitin is linked to histones, 40% is found in conjugates with molecular weights greater than 25,000, and the rest is unconjugated. After heat-shock, the free ubiquitin po
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Hartmann-Petersen, Rasmus, Klavs B. Hendil, and Colin Gordon. "Ubiquitin binding proteins protect ubiquitin conjugates from disassembly." FEBS Letters 535, no. 1-3 (2002): 77–81. http://dx.doi.org/10.1016/s0014-5793(02)03874-7.

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Ghaboosi, Nazli, and Raymond J. Deshaies. "A Conditional Yeast E1 Mutant Blocks the Ubiquitin–Proteasome Pathway and Reveals a Role for Ubiquitin Conjugates in Targeting Rad23 to the Proteasome." Molecular Biology of the Cell 18, no. 5 (2007): 1953–63. http://dx.doi.org/10.1091/mbc.e06-10-0965.

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E1 ubiquitin activating enzyme catalyzes the initial step in all ubiquitin-dependent processes. We report the isolation of uba1-204, a temperature-sensitive allele of the essential Saccharomyces cerevisiae E1 gene, UBA1. Uba1-204 cells exhibit dramatic inhibition of the ubiquitin–proteasome system, resulting in rapid depletion of cellular ubiquitin conjugates and stabilization of multiple substrates. We have employed the tight phenotype of this mutant to investigate the role ubiquitin conjugates play in the dynamic interaction of the UbL/UBA adaptor proteins Rad23 and Dsk2 with the proteasome.
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Gracy, Robert W. "Oxidized proteins & ubiquitin conjugates." Neurobiology of Aging 23, no. 4 (2002): 515–16. http://dx.doi.org/10.1016/s0197-4580(01)00347-5.

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Agell, N., and C. Mezquita. "Cellular content of ubiquitin and formation of ubiquitin conjugates during chicken spermatogenesis." Biochemical Journal 250, no. 3 (1988): 883–89. http://dx.doi.org/10.1042/bj2500883.

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Ubiquitin was purified from chicken testis and its content, biosynthesis and formation of conjugates was determined in germinal cells at successive stages of spermatogenesis. Free ubiquitin increased markedly during spermatogenesis, reaching its maximum level in early spermatids. High levels of ubiquitin were still present in late spermatids but were not detectable in mature spermatozoa. Biosynthesis of ubiquitin occurred in vitro in a fraction containing meiotic and pre-meiotic cells, and during spermiogenesis, in early and late spermatids. The cellular content of free ubiquitin increased aft
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Doherty, F. J., N. U. Osborn, J. A. Wassell, P. E. Heggie, L. Laszlo, and R. J. Mayer. "Ubiquitin-protein conjugates accumulate in the lysosomal system of fibroblasts treated with cysteine proteinase inhibitors." Biochemical Journal 263, no. 1 (1989): 47–55. http://dx.doi.org/10.1042/bj2630047.

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Mouse fibroblasts (3T3-L1 cells) accumulate detergent- and salt-insoluble aggregates of proteins conjugated to ubiquitin when incubated in the presence of inhibitors of lysosomal cysteine cathepsins, including E-64. These ubiquitin-protein conjugates co-fractionate with lysosomes on density gradients and are found in multivesicular dense bodies which by electron microscopy appear to be engaged in microautophagy. Both E-64 and ammonium chloride increase the intracellular concentration of free ubiquitin, but only E-64 leads to the formation of insoluble lysosomal ubiquitin-protein conjugates. Th
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Shang, F., and A. Taylor. "Oxidative stress and recovery from oxidative stress are associated with altered ubiquitin conjugating and proteolytic activities in bovine lens epithelial cells." Biochemical Journal 307, no. 1 (1995): 297–303. http://dx.doi.org/10.1042/bj3070297.

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Roles for ubiquitin (an 8.5 kDa polypeptide) involve its conjugation to proteins as a signal to initiate degradation and as a stress protein. We investigated ubiquitin conjugation and ubiquitin-dependent proteolytic activities in cultured bovine lens epithelial cells (BLECs) upon oxidative challenge. A 44% decrease in intracellular glutathione confirmed oxidative stress upon incubation with 1 mM H2O2. After 30 min incubation, endogenous high-molecular-mass ubiquitin conjugates decreased 73%, and intracellular proteolysis decreased about 50%. In the supernatants of the oxidatively treated BLECs
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Dissertations / Theses on the topic "Ubiquitin-conjugates"

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Jung, Ji Eun [Verfasser]. "Synthesis and mass spectrometric structural chracterization of ubiquitin conjugates / Ji Eun Jung." Konstanz : Bibliothek der Universität Konstanz, 2011. http://d-nb.info/1017236062/34.

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Keusekotten, Kirstin [Verfasser]. "Targeting SUMO conjugates for degradation : the human RING finger RNF4 as a specialized ubiquitin ligase / Kirstin Keusekotten." Köln : Universitäts- und Stadtbibliothek Köln, 2010. http://d-nb.info/1013740351/34.

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Wiemhoefer, Anne. "Identification and characterization of interferon-gamma induced ubiquitinated newly synthesized proteins." Doctoral thesis, Humboldt-Universität zu Berlin, Mathematisch-Naturwissenschaftliche Fakultät I, 2011. http://dx.doi.org/10.18452/16358.

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Ein Schlüsselprozess in der Immunantwort ist die durch das proinflammatorische Zytokin Interferon-gamma (IFNg) induzierte transiente Akkumulation von neu synthetisierten defekten Proteinen, die durch Anknüpfen von Polymeren des Proteins Ubiquitin (Ub) post-translational modifiziert werden. Die Ubiquitinierung ist das Schlüsselsignal für den Abbau dieser Proteine. Die Abbauprodukte dienen unter anderem als Quelle für die Prozessierung von Antigenen. Um die frühe Immunantwort besser zu verstehen, wurden im Rahmen dieser Arbeit die Identität und Charakteristika dieser neu synthetisierten Proteine
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Uzunova, Kristina Marinova. "Proteolytic control of SUMO conjugates /." 2006. http://bvbr.bib-bvb.de:8991/F?func=service&doc_library=BVB01&doc_number=017062212&line_number=0001&func_code=DB_RECORDS&service_type=MEDIA.

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Books on the topic "Ubiquitin-conjugates"

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Woods, Raymond Alwin. Studies on the radioimmunoassay of ubiquitin and its conjugates. 1986.

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Book chapters on the topic "Ubiquitin-conjugates"

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Shang, Fu, and Allen Taylor. "Ubiquitin Conjugates: A Sensitive Marker of Oxidative Stress." In Biomarkers for Antioxidant Defense and Oxidative Damage: Principles and Practical Applications. Wiley-Blackwell, 2010. http://dx.doi.org/10.1002/9780813814438.ch13.

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Schnellhardt, Marion, Kristina Uzunova, Veronika N. Bade, et al. "Analysis of Cellular SUMO and SUMO–Ubiquitin Hybrid Conjugates." In Methods in Molecular Biology. Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-474-2_4.

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Elsasser, Suzanne, Yuan Shi, and Daniel Finley. "Binding of Ubiquitin Conjugates to Proteasomes as Visualized with Native Gels." In Methods in Molecular Biology. Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-474-2_28.

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Kim, Hyoung Tae, and Alfred L. Goldberg. "Formation of Nondegradable Forked Ubiquitin Conjugates by Ring-Finger Ligases and Its Prevention by S5a." In Methods in Molecular Biology. Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-474-2_45.

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Peng, Junmin, and Dongmei Cheng. "Proteomic Analysis of Ubiquitin Conjugates in Yeast." In Methods in Enzymology. Elsevier, 2005. http://dx.doi.org/10.1016/s0076-6879(05)99025-3.

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Middleton, Adam J., Rhesa Budhidarmo, and Catherine L. Day. "Use of E2~Ubiquitin Conjugates for the Characterization of Ubiquitin Transfer by RING E3 Ligases Such as the Inhibitor of Apoptosis Proteins." In Regulated Cell Death Part B - Necroptotic, Autophagic and other Non-apoptotic Mechanisms. Elsevier, 2014. http://dx.doi.org/10.1016/b978-0-12-801430-1.00010-x.

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