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Relevant bibliographies by topics / Mitochondrial porin

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Academic literature on the topic 'Mitochondrial porin'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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Journal articles on the topic "Mitochondrial porin"

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Bay, Denice C., Joe D. O’Neil, and Deborah A. Court. "The influence of sterols on the conformation of recombinant mitochondrial porin in detergent." Biochemistry and Cell Biology 86, no. 6 (2008): 539–45. http://dx.doi.org/10.1139/o08-132.

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Mitochondrial porins (voltage-dependent anion-selective channels, VDAC) are key contributors to cellular metabolism. When isolated from mitochondria porins copurify with sterols, and some isolated forms of the protein require sterol for insertion into artificial membranes. Nonetheless, the contributions of sterols to the folded state of mitochondrial porin are not understood. Recently, with the goal of high-resolution structural studies, several laboratories have developed methods for folding recombinant porins at high concentration in detergent. In the present study, recombinant Neurospora cr

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Singha, Ujjal K., Shvetank Sharma, and Minu Chaudhuri. "Downregulation of Mitochondrial Porin Inhibits Cell Growth and Alters Respiratory Phenotype in Trypanosoma brucei." Eukaryotic Cell 8, no. 9 (2009): 1418–28. http://dx.doi.org/10.1128/ec.00132-09.

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ABSTRACT Porin is the most abundant outer membrane (OM) protein of mitochondria. It forms the aqueous channel on the mitochondrial OM and mediates major metabolite flux between mitochondria and cytosol. Mitochondrial porin in Trypanosoma brucei, a unicellular parasitic protozoan and the causative agent of African trypanosomiasis, possesses a β-barrel structure similar to the bacterial OM porin OmpA. T. brucei porin (TbPorin) is present as a monomer as well as an oligomer on the mitochondrial OM, and its expression is developmentally regulated. In spite of its distinct structure, the TbPorin fu

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Endo, Toshiya, and Haruka Sakaue. "Multifaceted roles of porin in mitochondrial protein and lipid transport." Biochemical Society Transactions 47, no. 5 (2019): 1269–77. http://dx.doi.org/10.1042/bst20190153.

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Abstract Mitochondria are essential eukaryotic organelles responsible for primary cellular energy production. Biogenesis, maintenance, and functions of mitochondria require correct assembly of resident proteins and lipids, which require their transport into and within mitochondria. Mitochondrial normal functions also require an exchange of small metabolites between the cytosol and mitochondria, which is primarily mediated by a metabolite channel of the outer membrane (OM) called porin or voltage-dependent anion channel. Here, we describe recently revealed novel roles of porin in the mitochondr

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Krimmer, Thomas, Doron Rapaport, Michael T. Ryan, et al. "Biogenesis of Porin of the Outer Mitochondrial Membrane Involves an Import Pathway via Receptors and the General Import Pore of the Tom Complex." Journal of Cell Biology 152, no. 2 (2001): 289–300. http://dx.doi.org/10.1083/jcb.152.2.289.

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Porin, also termed the voltage-dependent anion channel, is the most abundant protein of the mitochondrial outer membrane. The process of import and assembly of the protein is known to be dependent on the surface receptor Tom20, but the requirement for other mitochondrial proteins remains controversial. We have used mitochondria from Neurospora crassa and Saccharomyces cerevisiae to analyze the import pathway of porin. Import of porin into isolated mitochondria in which the outer membrane has been opened is inhibited despite similar levels of Tom20 as in intact mitochondria. A matrix-destined p

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Grevel, Alexander, and Thomas Becker. "Porins as helpers in mitochondrial protein translocation." Biological Chemistry 401, no. 6-7 (2020): 699–708. http://dx.doi.org/10.1515/hsz-2019-0438.

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AbstractMitochondria import the vast majority of their proteins via dedicated protein machineries. The translocase of the outer membrane (TOM complex) forms the main entry site for precursor proteins that are produced on cytosolic ribosomes. Subsequently, different protein sorting machineries transfer the incoming preproteins to the mitochondrial outer and inner membranes, the intermembrane space, and the matrix. In this review, we highlight the recently discovered role of porin, also termed voltage-dependent anion channel (VDAC), in mitochondrial protein biogenesis. Porin forms the major chan

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Wideman, Jeremy G., Nancy E. Go, Astrid Klein, et al. "Roles of the Mdm10, Tom7, Mdm12, and Mmm1 Proteins in the Assembly of Mitochondrial Outer Membrane Proteins in Neurospora crassa." Molecular Biology of the Cell 21, no. 10 (2010): 1725–36. http://dx.doi.org/10.1091/mbc.e09-10-0844.

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The Mdm10, Mdm12, and Mmm1 proteins have been implicated in several mitochondrial functions including mitochondrial distribution and morphology, assembly of β-barrel proteins such as Tom40 and porin, association of mitochondria and endoplasmic reticulum, and maintaining lipid composition of mitochondrial membranes. Here we show that loss of any of these three proteins in Neurospora crassa results in the formation of large mitochondrial tubules and reduces the assembly of porin and Tom40 into the outer membrane. We have also investigated the relationship of Mdm10 and Tom7 in the biogenesis of β

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Bay, Denice C., and Deborah A. Court. "Origami in the outer membrane: the transmembrane arrangement of mitochondrial porins." Biochemistry and Cell Biology 80, no. 5 (2002): 551–62. http://dx.doi.org/10.1139/o02-149.

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Voltage-dependent anion-selective channels (VDAC), also known as mitochondrial porins, are key regulators of metabolite flow across the mitochondrial outer membrane. Porins from a wide variety of organisms share remarkably similar electrophysiological properties, in spite of considerable sequence dissimilarity, indicating that they share a common structure. Based on primary sequence considerations, analogy with bacterial porins, and circular dichroism analysis, it is agreed that VDAC spans the outer membrane as a β-barrel. However, the residues that form the antiparallel β-strands comprising t

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Bay, Denice C., and Deborah A. Court. "Effects of ergosterol on the structure and activity of Neurospora mitochondrial porin in liposomes." Canadian Journal of Microbiology 55, no. 11 (2009): 1275–83. http://dx.doi.org/10.1139/w09-088.

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Mitochondrial porins (also known as voltage-dependent anion-selective channels (VDACs)) regulate and contribute to cellular metabolism. These proteins copurify with sterols, and some purified forms of the protein require sterol for insertion into planar artificial membranes. Recently, interactions between detergent-solubilized mitochondrial porins and sterols have been detected by NMR and spectroscopic methods, but the effects of sterols on pore function remained to be assessed. Therefore, in this work, a freeze–thaw technique was used to introduce recombinant Neurospora porin into liposomes c

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Ferens, Fraser G., Victor Spicer, Oleg V. Krokhin, Anna Motnenko, William A. T. Summers, and Deborah A. Court. "A deletion variant partially complements a porin-less strain of Neurospora crassa." Biochemistry and Cell Biology 95, no. 2 (2017): 318–27. http://dx.doi.org/10.1139/bcb-2016-0166.

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Mitochondrial porin, the voltage-dependent anion channel, plays an important role in metabolism and other cellular functions within eukaryotic cells. To further the understanding of porin structure and function, Neurospora crassa wild-type porin was replaced with a deletion variant lacking residues 238–242 (238porin). 238porin was assembled in the mitochondrial outer membrane, but the steady state levels were only about 3% of those of the wild-type protein. The strain harbouring 238porin displayed cytochrome deficiencies and expressed alternative oxidase. Nonetheless, it exhibited an almost no

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Ha, H., P. Hajek, D. M. Bedwell, and P. D. Burrows. "A mitochondrial porin cDNA predicts the existence of multiple human porins." Journal of Biological Chemistry 268, no. 16 (1993): 12143–49. http://dx.doi.org/10.1016/s0021-9258(19)50319-2.

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Dissertations / Theses on the topic "Mitochondrial porin"

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Runke, Gregory S. "Functional and structural studies of mitochondrial porin." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2000. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape2/PQDD_0012/MQ53217.pdf.

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Smeyers, Mathias. "Structure et fonction du VDAC: aspects phylogénétiques et biochimiques." Doctoral thesis, Universite Libre de Bruxelles, 2005. http://hdl.handle.net/2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/210913.

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Le VDAC (Voltage-Dependent Anion-selective Channel) est un canal ionique de la membrane externe de la mitochondrie. Il est caractérisé par une haute conductance (4nS dans du KCl 1M) à des faibles différences de potentiel et des fermetures vers des niveaux de conductance inférieurs suite à l’application de voltages élevés. La selectivité de l’état de haute conductance est anionique alors que celle du principal état de faible conductance est fortement cationique. La structure secondaire et la fonction est bien conservée chez les animaux, les plantes et les champignons alors que les séquences son

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Martins, Trindade Dario. "Contribution of the adenine nucleotide carrier, porin, and sphingolipid metabolism to mitochondria membrane permeabilization in Saccharomyces cerevisiae." Thesis, Bordeaux 2, 2013. http://www.theses.fr/2013BOR22133/document.

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La perméabilisation de la membrane mitochondriale externe (MOMP) est un évènement décisif lors de la balance entre la vie et la mort de la cellule. Les évènements biochimiques responsables de la MOMP ne sont pas encore complètement définis. Deux mécanismes majeurs et distincts ont été impliqués dans le contrôle de la MOMP: i) l'action des protéines de la famille de Bcl-2, qui peuvent directement s'insérer dans la membrane mitochondriale externe (OMM) et induire l'ouverture de pores; et ii) le pore de transition de perméabilité (PTP), un canal non sélectif de la membrane mitochondriale interne,

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Buckler, Carlyn Suzanne Keith. "Miniature plant phenotype and mitochondrial porins in maize /." free to MU campus, to others for purchase, 1999. http://wwwlib.umi.com/cr/mo/fullcit?p9946248.

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Spira, Afchain Agathe. "Étude des relations structure-fonction du transporteur mitochondrial d’ADP/ATP et de ses interactions avec d’autres protéines membranaires mitochondriales." Grenoble 1, 2007. http://www.theses.fr/2007GRE10107.

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La mitochondrie, organite présent chez toutes les cellules eucaryotes aérobies, est délimitée par deux membranes qui compartimentent des fonctions physiologiques essentielles. La membrane interne est une barrière que les métabolites ne peuvent franchir que grâce à des protéines spécifiques, dont le transporteur mitochondrial d’ADP/ATP. Un premier volet de cette thèse s’attache à la purification du transporteur bovin en complexe avec l’acide bongkrékique. Il s’inscrit dans le cadre des approches précédemment engagées au laboratoire, qui visent à résoudre la structure tridimensionnelle du transp

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Guo, Xiaojun. "Isolement et caractérisation du gène de la porine mitochondriale de Saccharomyces cerevisiae étude de l'expression du gène et construction de mutants déficients en porine /." Grenoble 2 : ANRT, 1988. http://catalogue.bnf.fr/ark:/12148/cb37614154r.

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Guo, Xiaojun. "Isolement et caractérisation du gène de la porine mitochondriale de Saccharomyces cerevisiae : étude de l'expression du gène et construction de mutants déficients en porine." Aix-Marseille 2, 1988. http://www.theses.fr/1988AIX22023.

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La prine de saccharomyces cerevisiae, proteine intrinseque majeure de la membrane externe mitochondriale, permet le passage de petites molecules dont la taille est inferieure a 8000 daltons. Le gene codant pour la prine a ete isole, localise (chromosome 14) et sequence. Le rna messager du gene por ne subit pas d'epissage et sa transcription est sensible a la repression catabolique. Des mutants deficients en porine ont ete construits a la suite par la deletion totale de l'element tyl-p

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Weichbrodt, Conrad. "Elektrophysiologische Charakterisierung des mitochondrialen Porins VDAC1 und des antimikrobiellen Peptids Dermcidin in lösungsmittelfreien Modellmembranen." Doctoral thesis, Niedersächsische Staats- und Universitätsbibliothek Göttingen, 2013. http://hdl.handle.net/11858/00-1735-0000-0001-BAA4-C.

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9

Clemençon, Benjamin. "Etude conformationnelle de protéines membranaires mitochondriales modèles chez Saccharomyces cerevisiae : Analyses des relations structure/fonction du transporteur d'ADP/ATP et de l'accessibilité au solvant de la porine VDAC." Phd thesis, Université de Grenoble, 2010. http://tel.archives-ouvertes.fr/tel-00577042.

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Les transporteurs d'ADP/ATP (Ancp) et de phosphate inorganique (PiC) ainsi que la porine VDAC représentent les principaux maillons d'une machinerie de transport d'ADP, d'ATP et de phosphate inorganique à travers la double membrane mitochondrial. Actuellement, les connaissances relatives aux mécanismes moléculaires mis en jeu dans cette machinerie accusent un retard. L'objectif de ce projet de Thèse a été d'amener de nouveaux éléments sur l'état conformationnel de ces protéines étudiées dans la levure Saccharomyces cerevisiae, modèle biologique où la génétique est facilitée. La majeure partie d

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Weichbrodt, Conrad [Verfasser], Claudia [Akademischer Betreuer] Steinem, Jörg [Akademischer Betreuer] Schroeder, et al. "Elektrophysiologische Charakterisierung des mitochondrialen Porins VDAC1 und des antimikrobiellen Peptids Dermcidin in lösungsmittelfreien Modellmembranen / Conrad Weichbrodt. Gutachter: Claudia Steinem ; Jörg Schroeder ; Ulf Diederichsen ; Ralf Ficner ; Kai Tittmann ; Michael Meinecke. Betreuer: Claudia Steinem." Göttingen : Niedersächsische Staats- und Universitätsbibliothek Göttingen, 2013. http://d-nb.info/1044415088/34.

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Book chapters on the topic "Mitochondrial porin"

1

Adams, V., and E. R. B. McCabe. "Role of Porin-Kinase Interactions in Disease." In Molecular Biology of Mitochondrial Transport Systems. Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78936-6_25.

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Michejda, J., X. J. Guo, and G. J. M. Lauquin. "Bioenergetic Consequences of the Lack of Mitochondrial Porin: Identification of a Putative New Pore." In Anion Carriers of Mitochondrial Membranes. Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-74539-3_18.

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De Pinto, Vito, Ruggiero Caizzi, Jalal Ahmad Aljamal, Corrado Caggese, and Ferdinando Palmieri. "Experimental Supports to a Sixteen-Strands Model of Transmembrane Arrangement of Mitochondrial Porin and Preliminary Results Concerning a Multigene Family in Drosophila melanogaster Related to Human Mitochondrial Porin." In Molecular Biology of Mitochondrial Transport Systems. Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78936-6_19.

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Michejda, J., H. Kmita, O. Stobienia, M. Budzińska, and G. J. M. Lauquin. "Restrictions of Metabolite Permeation Through the Outer Mitochondrial Membrane of Porin-Deficient Yeast Mutant." In Molecular Biology of Mitochondrial Transport Systems. Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78936-6_24.

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Gellerich, F. N., M. Kapischke, M. Wagner, and D. Brdiczka. "Influence of Macromolecules on the Permeability of Porin Pores and Dynamic Compartmentation of Adenine Nucleotides in the Mitochondrial Intermembrane Space." In Molecular Biology of Mitochondrial Transport Systems. Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78936-6_23.

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Thinnes, F. P., D. Babel, M. Heiden, et al. "“Porin 31HL” in the Plasmalemma of Human Cells: A VDAC Discussed as Part of a Chloride Channel Complex in Normal and Cystic Fibrosis B-Lymphocyte Cell Lines." In Molecular Biology of Mitochondrial Transport Systems. Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78936-6_27.

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de Pinto, Vito, Laura Gaballo, Roland Benz, and Ferdinando Palmieri. "Purification of Mammalian Porins." In Anion Carriers of Mitochondrial Membranes. Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-74539-3_19.

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Benz, Roland. "Porins from Mitochondrial and Bacterial Outer Membranes: Structural and Functional Aspects." In Anion Carriers of Mitochondrial Membranes. Springer Berlin Heidelberg, 1989. http://dx.doi.org/10.1007/978-3-642-74539-3_16.

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Benz, Roland. "Structure and Function of Mitochondrial (Eukaryotic) Porins." In Bacterial and Eukaryotic Porins. Wiley-VCH Verlag GmbH & Co. KGaA, 2005. http://dx.doi.org/10.1002/3527603875.ch13.

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Anflous, Keltoum, and William J. Craigen. "Mitochondrial Porins in Mammals: Insights into Functional Roles from Mutant Mice and Cells." In Bacterial and Eukaryotic Porins. Wiley-VCH Verlag GmbH & Co. KGaA, 2005. http://dx.doi.org/10.1002/3527603875.ch14.

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