Relevant bibliographies by topics / Cytochrome c oxidase subunit 1

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers
  5. Reports

Academic literature on the topic 'Cytochrome c oxidase subunit 1'

Author: Grafiati
Published: 3 June 2025
Last updated: 31 July 2025

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Journal articles on the topic "Cytochrome c oxidase subunit 1"

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Kossekova, G., B. Atanasov, R. Bolli, and A. Azzi. "Ionic-strength-dependence of the oxidation of native and pyridoxal 5′-phosphate-modified cytochromes c by cytochrome c oxidase." Biochemical Journal 262, no. 2 (1989): 591–96. http://dx.doi.org/10.1042/bj2620591.

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The ionic-strength-dependences of the rate constants (log k plotted versus square root of 1) for oxidation of native and pyridoxal 5′-phosphate-modified cytochromes c by three different preparations of cytochrome c oxidase have complex non-linear character, which may be explained on the basis of present knowledge of the structure of the oxidase and the monomer-dimer equilibrium of the enzyme. The wave-type curve (with a minimum and a maximum) for oxidation of native cytochrome c by purified cytochrome c oxidase depleted of phospholipids may reflect consecutively inhibition of oxidase monomers
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Burke, P. V., and R. O. Poyton. "Structure/function of oxygen-regulated isoforms in cytochrome c oxidase." Journal of Experimental Biology 201, no. 8 (1998): 1163–75. http://dx.doi.org/10.1242/jeb.201.8.1163.

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Eukaryotic cytochrome c oxidases are complex oligomeric membrane proteins composed of subunit polypeptides encoded by both nuclear and mitochondrial genomes. While the mitochondrially encoded subunits are encoded by unique genes, some of the nuclear-encoded subunits are encoded by multigene families. The isoforms produced by these multigene families are tissue-specific and/or developmentally regulated in mammals and environmentally regulated in lower eukaryotes. Isoforms for one of the subunits, V, in the yeast Saccharomyces cerevisiae and one of the subunits, VII, in the slime mold Dictyostel
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Megehee, James A., Jonathan P. Hosler, and Michael D. Lundrigan. "Evidence for a cytochrome bcc–aa 3 interaction in the respiratory chain of Mycobacterium smegmatis." Microbiology 152, no. 3 (2006): 823–29. http://dx.doi.org/10.1099/mic.0.28723-0.

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Spectroscopic analysis of membranes isolated from Mycobacterium smegmatis, along with analysis of its genome, indicates that the cytochrome c branch of its respiratory pathway consists of a modified bc 1 complex that contains two cytochromes c in its c 1 subunit, similar to other acid-fast bacteria, and an aa 3-type cytochrome c oxidase. A functional association of the cytochrome bcc and aa 3 complexes was indicated by the findings that levels of detergent sufficient to completely disrupt isolated membranes failed to inhibit quinol-driven O2 reduction, but known inhibitors of the bc 1 complex
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Dhar, Shilpa S., Kaid Johar, and Margaret T. T. Wong-Riley. "Bigenomic transcriptional regulation of all thirteen cytochrome c oxidase subunit genes by specificity protein 1." Open Biology 3, no. 3 (2013): 120176. http://dx.doi.org/10.1098/rsob.120176.

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Cytochrome c oxidase (COX) is one of only four known bigenomic proteins, with three mitochondria-encoded subunits and 10 nucleus-encoded ones derived from nine different chromosomes. The mechanism of regulating this multi-subunit, bigenomic enzyme is not fully understood. We hypothesize that specificity protein 1 (Sp1) functionally regulates the 10 nucleus-encoded COX subunit genes directly and the three mitochondrial COX subunit genes indirectly by regulating mitochondrial transcription factors A and B ( TFAM , TFB1M and TFB2M ) in neurons. By means of in silico analysis, electrophoretic mobi
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Balodite, Elina, Inese Strazdina, Nina Galinina, et al. "Structure of the Zymomonas mobilis respiratory chain: oxygen affinity of electron transport and the role of cytochrome c peroxidase." Microbiology 160, no. 9 (2014): 2045–52. http://dx.doi.org/10.1099/mic.0.081612-0.

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The genome of the ethanol-producing bacterium Zymomonas mobilis encodes a bd-type terminal oxidase, cytochrome bc 1 complex and several c-type cytochromes, yet lacks sequences homologous to any of the known bacterial cytochrome c oxidase genes. Recently, it was suggested that a putative respiratory cytochrome c peroxidase, receiving electrons from the cytochrome bc 1 complex via cytochrome c 552, might function as a peroxidase and/or an alternative oxidase. The present study was designed to test this hypothesis, by construction of a cytochrome c peroxidase mutant (Zm6-perC), and comparison of
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Oliva, Claudia R., Md Yousuf Ali, Susanne Flor, and Corinne E. Griguer. "Effect of Expression of Nuclear-Encoded Cytochrome C Oxidase Subunit 4 Isoforms on Metabolic Profiles of Glioma Cells." Metabolites 12, no. 8 (2022): 748. http://dx.doi.org/10.3390/metabo12080748.

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Although often effective at treating newly diagnosed glioblastoma (GBM), increasing evidence suggests that chemo- and radiotherapy-induced alterations in tumor metabolism promote GBM recurrence and aggressiveness, as well as treatment resistance. Recent studies have demonstrated that alterations in glioma cell metabolism, induced by a switch in the isoform expression of cytochrome c oxidase subunit 4 (COX4), a key regulatory subunit of mammalian cytochrome c oxidase, could promote these effects. To understand how the two COX4 isoforms (COX4-1 and COX4-2) differentially affect glioma metabolism
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Nunoura, Takuro, Yoshihiko Sako, Takayoshi Wakagi, and Aritsune Uchida. "Cytochrome aa3 in facultatively aerobic and hyperthermophilic archaeon Pyrobaculum oguniense." Canadian Journal of Microbiology 51, no. 8 (2005): 621–27. http://dx.doi.org/10.1139/w05-040.

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We partially purified and characterized the cytochrome aa3 from the facultatively aerobic and hyperthermophilic archaeon Pyrobaculum oguniense. This cytochrome aa3 showed oxygen consumption activity with N, N, N′, N′-tetramethyl-1,4-phenylenediamine and ascorbate as substrates, and also displayed bovine cytochrome c oxidase activity. These enzymatic activities of cytochrome aa3 were inhibited by cyanide and azide. This cytochrome contained heme As, but not typical heme A. An analysis of trypsin-digested fragments indicated that 1 subunit of this cytochrome was identical to the gene product of
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Seo, Yong Bae, Sung Chul Kang, Seong Seok Choi, et al. "Phylogenetic Study of Genus Haliotis in Korea by Cytochrome c Oxidase Subunit 1 and RAPD Analysis." Journal of Life Science 26, no. 4 (2016): 406–13. http://dx.doi.org/10.5352/jls.2016.26.4.406.

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Hernandez-Zimbron, Luis Fernando, Jose Luna-Muñoz, Raul Mena та ін. "Amyloid-β Peptide Binds to Cytochrome C Oxidase Subunit 1". PLoS ONE 7, № 8 (2012): e42344. http://dx.doi.org/10.1371/journal.pone.0042344.

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MALATESTA, Francesco, Giovanni ANTONINI, Flavia NICOLETTI, et al. "Probing the high-affinity site of beef heart cytochrome c oxidase by cross-linking." Biochemical Journal 315, no. 3 (1996): 909–16. http://dx.doi.org/10.1042/bj3150909.

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A covalent complex between cytochrome c oxidase and Saccharomyces cerevisiae iso-1-cytochrome c (called caa3) has been prepared at low ionic strength. Subunit III Cys-115 of beef heart cytochrome c oxidase cross-links by disulphide bond formation to thionitrobenzoate-modified yeast cytochrome c, a derivative shown to bind into the high-affinity site for substrate [Fuller, Darley-Usmar and Capaldi (1981) Biochemistry 20, 7046–7053]. Stopped-flow experiments show that (1) covalently bound yeast cytochrome c cannot donate electrons to cytochrome oxidase, whereas oxidation of exogenously added cyt
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Dissertations / Theses on the topic "Cytochrome c oxidase subunit 1"

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Lydon, Anniken. "Identification of Saccharina groenlandica (Phaeophyceae) around the Svalbard Archipelago: DNA barcoding using cytochrome c oxidase subunit 1 (COI)." DigitalCommons@CalPoly, 2015. https://digitalcommons.calpoly.edu/theses/1368.

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In the Arctic, brown algae (kelps) and seaweeds are ecologically important: providing habitat, protection, and nutrients for invertebrate and vertebrate species living in nearshore environments. Migrations of biota between the North Pacific and North Atlantic Oceans have occurred periodically during Earth’s history leading to colonization of the Arctic Ocean. Around 3.5 Mya the “Great Trans-Arctic Biotic Interchange” occurred and the Laminariales order of kelp, thought to be of North Pacific origin, underwent a massive radiation and speciation event around the Arctic Ocean. Phylogenetic analys
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Johnston, Anne. "Evolutionary Relationships Among Duiker Antelope (Bovidae: Cephalophinae)." ScholarWorks@UNO, 2011. http://scholarworks.uno.edu/td/1401.

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Duikers are a species rich subfamily of threatened African antelope whose recent origin poses a challenge to the molecular identification of taxa and estimation of their phylogeny. I test the ability of DNA barcodes to identify all taxa within this group. I then use mitochondrial and nuclear genes to estimate a multi-locus species tree and to date divergence times. DNA barcodes are unable to distinguish many sister taxa, calling into question the utility of barcodes for the regulation of duiker trade or in identification of field-collected feces. The multi-locus phylogeny provides support for
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Brett, Christy Donna. "Testing the effectiveness of the mt DNA Cytochrome c oxidase subunit 1 (COI) gene locus for identifying species of Polychaete worm (Polychaeta: Annelida) in New Zealand." The University of Waikato, 2006. http://hdl.handle.net/10289/2425.

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The ability to accurately identify species is fundamental to ecological research and environmental monitoring. Current taxonomic identifications often rely on differentiation of morphologically ambiguous characters, and a process of categorization which is tedious and often leads to misidentifications. This is compounded by the presence of cryptic taxa, which may be prevalent among Polychaete worms (Polychaeta: Annelida). With increased access to genetic techniques, Cytochrome c oxidase subunit I has been suggested as a possible aid to assist in the discrimination of species resources. In this
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Stanley, Brian Allan. "Characterization of cytochrome c oxidase subunit II from Bacillus subtilis." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2001. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp05/MQ63372.pdf.

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Hartlen, Rebecca. "Expression of cytochrome c oxidase subunit II from a nuclear transgene." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape10/PQDD_0024/MQ50783.pdf.

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Geyer, R. Ryan. "Investigating the Role of Subunit III in the Structure and Function of Rhodobacter Sphaeroides Cytochrome C Oxidase." Wright State University / OhioLINK, 2007. http://rave.ohiolink.edu/etdc/view?acc_num=wright1183979032.

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Omolewu, Rachel. "Characterization of Three Mutations in Conserved Domain of Subunit III of Cytochrome c Oxidase from Rhodobacter sphaeroides." Wright State University / OhioLINK, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=wright1292612174.

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Fisher, Kelli Nicole. "Investigating the Undefined Role of Subunit IIIin Cytochrome c Oxidase Functioning Using Dicyclohexylcarbodiimide Chemical Modification; Insight Into Enzyme Structure and Molecular Mechanism." Wright State University / OhioLINK, 2014. http://rave.ohiolink.edu/etdc/view?acc_num=wright1405294648.

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Cvetkov, Teresa L. "Cytochrome c Oxidase from Rhodobacter sphaeroides: Oligomeric Structure in the Phospholipid Bilayer and the Structural and Functional Effects of a C-Terminal Truncation in Subunit III." Wright State University / OhioLINK, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=wright1279028849.

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Beauchemin, Annie. "Cytochrome c oxidase subunit Vb interacts with human androgen receptor : a potential mechanism for neuronotoxicity in spinobulbar muscular atrophy." Thesis, McGill University, 2000. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=33377.

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Spinobulbar muscular atrophy (SBMA) is a neurodegenerative disease caused by the expansion of a polyglutamine (polyGln) tract in the human androgen receptor (hAR). One mechanism by which polyGln-expanded proteins are believed to cause neuronotoxicity is through aberrant interaction(s) with, and possible sequestration of, critical cellular protein(s).<br>Our goal was to confirm and further characterize the interaction between hAR and cytochrome c oxidase subunit Vb (COXVb), a nuclear-encoded mitochondrial protein. We had previously isolated COXVb as an AR-interacting protein in a yeast two-hybr
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Book chapters on the topic "Cytochrome c oxidase subunit 1"

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Suske, Guntram, Christel Enders, Thomas Mengel, and Bernhard Kadenbach. "The cDna and a Structural Gene for Rat Liver Cytochrome C Oxidase Subunit VIc." In Cytochrome Systems. Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1941-2_7.

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Patterson, Thomas E., Cynthia E. Trueblood, Richard M. Wright, and Robert O. Poyton. "Polypeptide Subunits Encoded by Nuclear Genes are Essential Components of Eukaryotic Cytochrome C Oxidase." In Cytochrome Systems. Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1941-2_34.

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Bisson, Roberto, and Barbara Bacci. "Evidence for a Functional Role of Nuclear Encoded Subunits in Mitochondrial Cytochrome c Oxidase." In Cytochrome Systems. Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1941-2_37.

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Luntz, Thomas L., and E. Margoliash. "An Amino Acid Sequence Region of Subunit II of Cytochrome Oxidase which may be Responsible for Evolutionary Changes in Reactivity with Different Cytochromes c." In Cytochrome Systems. Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1941-2_36.

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Müller, Michele, and Angelo Azzi. "Subunit I is the Catalytic Center of P. Denitrificans Cytochrome C Oxidase." In Bioenergetics. Springer US, 1990. http://dx.doi.org/10.1007/978-1-4684-5835-0_13.

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Asahi, Tadashi, Masayodhi Maeshima, Tsuyoshi Nakagawa, Kazuto Kobayashi, Yukimoto Iwasaki, and Kenzo Nakamura. "Synthesis of the Nuclear DNA-Encoded Subunits of Higher Plant Cytochrome C Oxidase and F1ATPase." In Plant Mitochondria. Springer US, 1987. http://dx.doi.org/10.1007/978-1-4899-3517-5_45.

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Freedman, Jo A., Samuel H. P. Chan, and P. Nicholls. "Topographical Changes in Cytochrome C Oxidase in the Soluble and Membrane-Bound Enzyme as Probed by Antibodies to Subunit V and the Whole Enzyme." In Integration of Mitochondrial Function. Springer US, 1988. http://dx.doi.org/10.1007/978-1-4899-2551-0_7.

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Yoshikawa, Shinya. "Cytochrome-c Oxidase." In Handbook of Copper Pharmacology and Toxicology. Humana Press, 2002. https://doi.org/10.1007/978-1-59259-288-3_7.

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Vondráčková, Alžběta, Kateřina Veselá, Jiří Zeman, and Markéta Tesařová. "High-Resolution Melting Analysis for Identifying Sequence Variations in Nuclear Genes for Assembly Factors and Structural Subunits of Cytochrome C Oxidase." In Methods in Molecular Biology. Springer New York, 2015. http://dx.doi.org/10.1007/978-1-4939-2257-4_31.

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Bisson, Roberto. "Cytochrome c Oxidase: Structure." In Bioelectrochemistry III. Springer US, 1990. http://dx.doi.org/10.1007/978-1-4757-9459-5_7.

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Conference papers on the topic "Cytochrome c oxidase subunit 1"

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Xạ, Trương Văn, and Trần Kim Thoa. "The Use of Mitochondrial Cytochrome C Oxidase Subunit I Gene in Identifying Pila Species in The Mekong Delta." In 2024 9th International Conference on Applying New Technology in Green Buildings (ATiGB). IEEE, 2024. http://dx.doi.org/10.1109/atigb63471.2024.10717675.

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Schonfeld, Justin, and Dan Ashlock. "Classifying Cytochrome c Oxidase subunit 1 by translation initiation mechanism using side effect machines." In 2010 IEEE Symposium on Computational Intelligence in Bioinformatics and Computational Biology (CIBCB). IEEE, 2010. http://dx.doi.org/10.1109/cibcb.2010.5510703.

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Kwak, Mi-Kyoung, Kyeong-Ah Jung, Donghyeok Kim, and Sujin Lee. "Abstract 1502: The link between NRF2 and mitochondria through the regulation of miR-181c/mitochondria-encoded cytochrome c oxidase subunit-1." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-1502.

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Ramzan, R., P. Cybulski, V. Ruppert, et al. "Does MRNA Upregulation of Cytochrome C Oxidase Subunit 4 Isoform 2 Sustain Atrial Fibrillation?" In 50th Annual Meeting of the German Society for Thoracic and Cardiovascular Surgery (DGTHG). Georg Thieme Verlag KG, 2021. http://dx.doi.org/10.1055/s-0041-1725838.

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Niode, Nurdjannah Jane, Aryani Adji, Jimmy Rimbing, et al. "Genetic diversity analysis of Apis dorsata (hymenoptera: apidae) based on cytochrome C oxidase subunit I gene sequences." In 2ND INTERNATIONAL CONFERENCE ON ADVANCED INFORMATION SCIENTIFIC DEVELOPMENT (ICAISD) 2021: Innovating Scientific Learning for Deep Communication. AIP Publishing, 2023. http://dx.doi.org/10.1063/5.0103887.

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Pratama, Risky, Mochamad Syaifudin, and Marini Wijayanti. "DNA Barcoding of Clown Loach Chromobotia macracanthus from Ogan and Musi River Based on Cytochrome C Oxidase Subunit I (COI) Gene." In Proceedings of the 3rd Sriwijaya International Conference on Environmental Issues, SRICOENV 2022, October 5th, 2022, Palembang, South Sumatera, Indonesia. EAI, 2023. http://dx.doi.org/10.4108/eai.5-10-2022.2328352.

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Balasubramanian Lakshmi, V. S., T. Berger, C. F. Garcia Castro, et al. "Mitochondrial Cytochrome C Oxidase Subunit 4 Isoform 2 Regulates T-cell Activation and Hyperinflammation During Virus-induced Exacerbation Following Smoke Exposure." In American Thoracic Society 2024 International Conference, May 17-22, 2024 - San Diego, CA. American Thoracic Society, 2024. http://dx.doi.org/10.1164/ajrccm-conference.2024.209.1_meetingabstracts.a2785.

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Garcia, C., V. S. Balasubramanian Lakshmi, O. Pak, et al. "Mitochondrial Cytochrome C Oxidase Subunit 4 Isoform 2 Promotes Murine Smoke-induced Pulmonary Inflammation and Emphysema - Therapeutic Potential of ROS Inhibition." In American Thoracic Society 2024 International Conference, May 17-22, 2024 - San Diego, CA. American Thoracic Society, 2024. http://dx.doi.org/10.1164/ajrccm-conference.2024.209.1_meetingabstracts.a2954.

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Daskalakis, Vangelis, Stavros C. Farantos, Constantinos Varotsis, Theodore E. Simos, and George Maroulis. "Protein Dynamics and Spectroscopy for Ferryl Intermediate of Cytochrome c Oxidase: A Molecular Dynamics Approach." In COMPUTATIONAL METHODS IN SCIENCE AND ENGINEERING: Theory and Computation: Old Problems and New Challenges. Lectures Presented at the International Conference on Computational Methods in Science and Engineering 2007 (ICCMSE 2007): VOLUME 1. AIP, 2007. http://dx.doi.org/10.1063/1.2836073.

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Yoshioka, Yasunori, George Maroulis, and Theodore E. Simos. "Applications of B3LYP Method for Enzyme Reactions: O[sub 2] Reduction by Cytochrome c Oxidase and Ubiquinol Oxidation by Cytochrome bc[sub 1] Complex." In Computational Methods in Science and Engineering. AIP, 2007. http://dx.doi.org/10.1063/1.2827025.

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Reports on the topic "Cytochrome c oxidase subunit 1"

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Ohad, Itzhak, and Himadri Pakrasi. Role of Cytochrome B559 in Photoinhibition. United States Department of Agriculture, 1995. http://dx.doi.org/10.32747/1995.7613031.bard.

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The aim of this research project was to obtain information on the role of the cytochrome b559 in the function of Photosystem-II (PSII) with special emphasis on the light induced photo inactivation of PSII and turnover of the photochemical reaction center II protein subunit RCII-D1. The major goals of this project were: 1) Isolation and sequencing of the Chlamydomonas chloroplast psbE and psbF genes encoding the cytochrome b559 a and b subunits respectively; 2) Generation of site directed mutants and testing the effect of such mutation on the function of PSII under various light conditions; 3)
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งามประเสริฐวงศ์, ธงชัย, อาจอง ประทัตสุนทรสาร та พชรพล จุ่มศรี. สถานภาพและการใช้ทรัพยากรของค้างคาวคุณกิตติ Craseonycteris thonglongyai : รายงานผลการดำเนินงาน. ภาควิชาชีววิทยา คณะวิทยาศาสตร์ จุฬาลงกรณ์มหาวิทยาลัย, 2019. https://doi.org/10.58837/chula.res.2019.28.

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ค้างคาวกินแมลงมีบทบาทสำคัญต่อระบบนิเวศในการควบคุมประชากรแมลงในธรรมชาติ ในงานวิจัยนี้ได้ทำการศึกษาองค์ประกอบอาหารของค้างคาวคุณกิตติจากมูลค้างคาวที่เก็บจากถ้ำพระ ในพื้นที่โครงการอนุรักษ์พันธุกรรมพืชอันเนื่องมาจากพระราชดำริฯ อำเภอไทรโยค จังหวัดกาญจนบุรี โดยใช้ดีเอ็นเอบาร์โค้ดในการระบุชนิดของแมลง และใช้ไพร์เมอร์ที่มีความจำเพาะต่อแมลง (ZBJ-ArtF1c และ ZBJ-ArtR2c) ในปฏิกิริยาลูกโซ่โพลีเมอเรส (PCR) เพื่อเพิ่มจำนวนดีเอ็นเอของยีน cytochrome c oxidase subunit I (COI) ผลจากการวิเคราะห์ลำดับดีเอ็นเอด้วยเทคนิค next-generation sequencing (NGS) พบว่า อาหารของค้างคาวคุณกิตติส่วนใหญ่เป็นแมลงในอันดับผีเสื้อ (Lep
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