Academic literature on the topic 'Co-translational assembly'

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Journal articles on the topic "Co-translational assembly"

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Wells, Jonathan N., L. Therese Bergendahl, and Joseph A. Marsh. "Co-translational assembly of protein complexes." Biochemical Society Transactions 43, no. 6 (2015): 1221–26. http://dx.doi.org/10.1042/bst20150159.

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The interaction of biological macromolecules is a fundamental attribute of cellular life. Proteins, in particular, often form stable complexes with one another. Although the importance of protein complexes is widely recognized, we still have only a very limited understanding of the mechanisms underlying their assembly within cells. In this article, we review the available evidence for one such mechanism, namely the coupling of protein complex assembly to translation at the polysome. We discuss research showing that co-translational assembly can occur in both prokaryotic and eukaryotic organism
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Williams, Neal K., and Bernhard Dichtl. "Co-translational control of protein complex formation: a fundamental pathway of cellular organization?" Biochemical Society Transactions 46, no. 1 (2018): 197–206. http://dx.doi.org/10.1042/bst20170451.

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Analyses of proteomes from a large number of organisms throughout the domains of life highlight the key role played by multiprotein complexes for the implementation of cellular function. While the occurrence of multiprotein assemblies is ubiquitous, the understanding of pathways that dictate the formation of quaternary structure remains enigmatic. Interestingly, there are now well-established examples of protein complexes that are assembled co-translationally in both prokaryotes and eukaryotes, and indications are that the phenomenon is widespread in cells. Here, we review complex assembly wit
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Zhang, Lixin, Virpi Paakkarinen, Klaas Jan van Wijk, and Eva-Mari Aro. "Co-translational Assembly of the D1 Protein into Photosystem II." Journal of Biological Chemistry 274, no. 23 (1999): 16062–67. http://dx.doi.org/10.1074/jbc.274.23.16062.

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Panasenko, Olesya O., Syam Prakash Somasekharan, Zoltan Villanyi, et al. "Co-translational assembly of proteasome subunits in NOT1-containing assemblysomes." Nature Structural & Molecular Biology 26, no. 2 (2019): 110–20. http://dx.doi.org/10.1038/s41594-018-0179-5.

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Tang, Jia Xin, Kyle Thompson, Robert W. Taylor, and Monika Oláhová. "Mitochondrial OXPHOS Biogenesis: Co-Regulation of Protein Synthesis, Import, and Assembly Pathways." International Journal of Molecular Sciences 21, no. 11 (2020): 3820. http://dx.doi.org/10.3390/ijms21113820.

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The assembly of mitochondrial oxidative phosphorylation (OXPHOS) complexes is an intricate process, which—given their dual-genetic control—requires tight co-regulation of two evolutionarily distinct gene expression machineries. Moreover, fine-tuning protein synthesis to the nascent assembly of OXPHOS complexes requires regulatory mechanisms such as translational plasticity and translational activators that can coordinate mitochondrial translation with the import of nuclear-encoded mitochondrial proteins. The intricacy of OXPHOS complex biogenesis is further evidenced by the requirement of many
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Rutledge, Angela C., Qiaozhu Su, and Khosrow Adeli. "Apolipoprotein B100 biogenesis: a complex array of intracellular mechanisms regulating folding, stability, and lipoprotein assemblyThis paper is one of a selection of papers published in this special issue entitled “Canadian Society of Biochemistry, Molecular & Cellular Biology 52nd Annual Meeting — Protein Folding: Principles and Diseases” and has undergone the Journal's usual peer review process." Biochemistry and Cell Biology 88, no. 2 (2010): 251–67. http://dx.doi.org/10.1139/o09-168.

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Apolipoprotein B100 (apoB) is a large amphipathic lipid-binding protein that is synthesized by hepatocytes and used to assemble and stabilize very low density lipoproteins (VLDL). It may have been derived through evolution from other lipid-associating proteins such as microsomal triglyceride transfer protein or vitellogenin. The correct folding of apoB requires assistance from chaperone proteins in co-translational lipidation, disulfide bond formation, and glycosylation. Any impairment in these processes results in co-translational targeting of the misfolded apoB molecule for proteasomal degra
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Lautier, Ophélie, Arianna Penzo, Jérôme O. Rouvière, et al. "Co-translational assembly and localized translation of nucleoporins in nuclear pore complex biogenesis." Molecular Cell 81, no. 11 (2021): 2417–27. http://dx.doi.org/10.1016/j.molcel.2021.03.030.

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Wagner, Susan, Anna Herrmannová, Vladislava Hronová, et al. "Selective Translation Complex Profiling Reveals Staged Initiation and Co-translational Assembly of Initiation Factor Complexes." Molecular Cell 79, no. 4 (2020): 546–60. http://dx.doi.org/10.1016/j.molcel.2020.06.004.

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Kassem, Sari, Zoltan Villanyi, and Martine A. Collart. "Not5-dependent co-translational assembly of Ada2 and Spt20 is essential for functional integrity of SAGA." Nucleic Acids Research 45, no. 3 (2016): 1186–99. http://dx.doi.org/10.1093/nar/gkw1059.

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Kassem, Sari, Zoltan Villanyi, and Martine A. Collart. "Not5-dependent co-translational assembly of Ada2 and Spt20 is essential for functional integrity of SAGA." Nucleic Acids Research 45, no. 12 (2017): 7539. http://dx.doi.org/10.1093/nar/gkx447.

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Dissertations / Theses on the topic "Co-translational assembly"

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Mukherjee, Pooja. "Study of the co-translational assembly mechanism of transcription complexes in mammalian cells." Thesis, Strasbourg, 2019. http://www.theses.fr/2019STRAJ051.

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La majorité des processus biologiques sont réalisés par des complexes protéiques multisubunités dans les cellules et une quantité importante d'énergie est requise par les cellules pour construire ces énormes complexes. Contrairement aux bactéries, les gènes codant pour les protéines sont dispersés dans le génome des eucaryotes, ce qui complique la compréhension de l'assemblage des complexes protéiques. En utilisant l'immunoprécipitation d'ARN suivie par la détection des ARNm à l'échelle du génome par analyse par micropuce, ARN molécule unique, FISH, immunofluorescence, cellules souches embryon
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Sono-Koree, Nana. "Role of Members of the Phosducin Gene Family in Protein Translation and Folding." BYU ScholarsArchive, 2010. https://scholarsarchive.byu.edu/etd/2438.

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G proteins regulate various physiological processes by way of transducing a wide variety of signals ranging from hormonal to sensory stimuli. Malfunctions in G protein signaling lead to numerous diseases. G protein signaling begins with binding of a ligand to a G protein-coupled receptor resulting in a conformational change that leads to the exchange of a GDP for a GTP on G α. The GTP bound α subunit dissociates for its stable Gβγ dimer partner. G α-GTP and Gβγ control the activity of effector enzymes and ion channels that ultimately orchestrate the cellular response to stimulus. Current repor
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Bertolini, Matilde [Verfasser], and Bernd [Akademischer Betreuer] Bukau. "Profiling interactions of proximal nascent chains reveals a general co-translational mechanism of protein complex assembly / Matilde Bertolini ; Betreuer: Bernd Bukau." Heidelberg : Universitätsbibliothek Heidelberg, 2021. http://d-nb.info/1229628967/34.

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Book chapters on the topic "Co-translational assembly"

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Zhang, Xin. "A Multistep Mechanism for Assembly of the SRP–SR Complex." In Multistate GTPase Control Co-translational Protein Targeting. Springer US, 2011. http://dx.doi.org/10.1007/978-1-4419-7808-0_2.

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Zhang, Xin. "Direct Visualization Reveals Dynamics of a Transient Intermediate During Protein Assembly." In Multistate GTPase Control Co-translational Protein Targeting. Springer US, 2011. http://dx.doi.org/10.1007/978-1-4419-7808-0_3.

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Zhang, Lixin, Virpi Paakkarinen, Klaas Jan van Wijk, and Eva-Mari Aro. "Co-translational Assembly of the D1 Protein into Photosystem II Complexes." In Photosynthesis: Mechanisms and Effects. Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-3953-3_731.

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