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Journal articles on the topic 'Mitochondrial porin'

Author: Grafiati

Published: 4 June 2021

Last updated: 1 February 2022

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1

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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Lindén, M., B. D. Nelson, and J. F. Leterrier. "The specific binding of the microtubule-associated protein 2 (MAP2) to the outer membrane of rat brain mitochondria." Biochemical Journal 261, no. 1 (1989): 167–73. http://dx.doi.org/10.1042/bj2610167.

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Purified mitochondria from rat brain contain microtubule-associated proteins (MAPs) bound to the outer membrane. Studies of binding in vitro performed with microtubules and with purified microtubule proteins showed that mitochondria preferentially interact with the high-molecular-mass MAPs (and not with Tau protein). Incubation of intact mitochondria with Taxol-stabilized microtubules resulted in the selective trapping of both MAPs 1 and 2 on mitochondria, indicating that an interaction between the two organelles occurred through a site on the arm-like projection of MAPs. Two MAP-binding sites

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12

Park, Jeehye, Yongsung Kim, Sekyu Choi, et al. "Drosophila Porin/VDAC Affects Mitochondrial Morphology." PLoS ONE 5, no. 10 (2010): e13151. http://dx.doi.org/10.1371/journal.pone.0013151.

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13

Summers, William A. T., and Deborah A. Court. "Origami in outer membrane mimetics: correlating the first detailed images of refolded VDAC with over 20 years of biochemical data." Biochemistry and Cell Biology 88, no. 3 (2010): 425–38. http://dx.doi.org/10.1139/o09-115.

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Mitochondrial porin forms an aqueous pore in the outer membrane, through which selective passage of small metabolites and ions occurs, thereby regulating both mitochondrial function and cellular respiration. Investigations of the structure and function of porin have been performed with whole mitochondria, membrane vesicles, artificial membranes, and in detergent solutions, resulting in numerous models of porin structure. The mechanisms by which this protein functions are undoubtedly linked to its structure, which remained elusive until 2008, with reports of 3 high-resolution structures of this

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14

VYSSOKIKH, Mikhail Yu, Annette KATZ, Alexander RUECK, et al. "Adenine nucleotide translocator isoforms 1 and 2 are differently distributed in the mitochondrial inner membrane and have distinct affinities to cyclophilin D." Biochemical Journal 358, no. 2 (2001): 349–58. http://dx.doi.org/10.1042/bj3580349.

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Different isoforms of the adenine nucleotide translocase (ANT) are expressed in a tissue-specific manner. It was assumed that ANT-1 and ANT-2 co-exist in every single mitochondrion and might be differently distributed within the membrane structures that constitute the peripheral inner membrane or the crista membrane. To discriminate between ANT originating from peripheral or from cristal inner membranes we made use of the fact that complexes between porin, the outer-membrane pore protein, and the ANT can be generated. Such complexes between porin and the ANT in the peripheral inner membrane we

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15

Zeth, Kornelius, and Marcus Thein. "Porins in prokaryotes and eukaryotes: common themes and variations." Biochemical Journal 431, no. 1 (2010): 13–22. http://dx.doi.org/10.1042/bj20100371.

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Gram-negative bacteria and mitochondria are both covered by two distinct biological membranes. These membrane systems have been maintained during the course of evolution from an early evolutionary precursor. Both outer membranes accommodate channels of the porin family, which are designed for the uptake and exchange of metabolites, including ions and small molecules, such as nucleosides or sugars. In bacteria, the structure of the outer membrane porin protein family of β-barrels is generally characterized by an even number of β-strands; usually 14, 16 or 18 strands are observed forming the bac

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16

Mannella, C. A. "Nature of In-Plane Phase Transitions in 2D Crystals of the Mitochondrial Porin, VDAC." Microscopy and Microanalysis 3, S2 (1997): 1065–66. http://dx.doi.org/10.1017/s1431927600012216.

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VDAC is a voltage-gated ion and metabolite channel that occurs at high density in the mitochondrial outer membrane. Although VDAC is probably related structurally to bacterial porins, small transmembrane voltages cause it to undergo reversible, partial closures that are not seen with the prokaryotic pores. The “closed” states, which are impermeable to ATP, can be induced by effectors, including a synthetic polyanion. There is evidence that closure involves major rearrangements of the pore structure that are difficult to explain in terms of porin-like β-barrels.The main source of information ab

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17

jamal, J. A. Al. "Characterization of Different Reactive Lysines in Bovine Heart Mitochondrial Porin." Biological Chemistry 383, no. 12 (2002): 1967–70. http://dx.doi.org/10.1515/bc.2002.222.

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Abstract Incubation of mitochondrial outer membrane porin with citraconic anhydride prior to treatment with fluorescein isothiocyanate (FITC) resulted in the labeling of a set of lysines located at a boundary between the water phase and lipid phase. The elution pattern of porin from the cation exchanger has been considered as indicative for the location of lysines. Electrical measurements after reconstitution of the modified protein in lipid bilayer membranes revealed that certain specific lysine residues are more susceptible to alterations. The innermost positive residues were only slightly i

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18

Konduri, Girija G., Adeleye J. Afolayan, Annie Eis, Kirkwood A. Pritchard, and Ru-Jeng Teng. "Interaction of endothelial nitric oxide synthase with mitochondria regulates oxidative stress and function in fetal pulmonary artery endothelial cells." American Journal of Physiology-Lung Cellular and Molecular Physiology 309, no. 9 (2015): L1009—L1017. http://dx.doi.org/10.1152/ajplung.00386.2014.

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An increase in oxygen tension at birth is one of the key signals that initiate pulmonary vasodilation in the fetal lung. We investigated the hypothesis that targeting endothelial nitric oxide synthase (eNOS) to the mitochondrial outer membrane regulates reactive oxygen species (ROS) formation in the fetal pulmonary artery endothelial cells (PAEC) during this transition. We isolated PAEC and pulmonary arteries from 137-day gestation fetal lambs (term = 144 days). We exposed PAEC to a simulated transition from fetal to (3% O2) to normoxic (21%) or hyperoxic (95% O2) postnatal Po2 or to the nitri

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19

Benz, Roland. "Porin from Bacterial and Mitochondrial Outer Membrane." Critical Reviews in Biochemistry 19, no. 2 (1985): 145–90. http://dx.doi.org/10.3109/10409238509082542.

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20

Doan, Kim Nguyen, Lars Ellenrieder, and Thomas Becker. "Mitochondrial porin links protein biogenesis to metabolism." Current Genetics 65, no. 4 (2019): 899–903. http://dx.doi.org/10.1007/s00294-019-00965-z.

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21

Pfaller, R., R. Kleene, and W. Neupert. "Biogenesis of mitochondrial porin: The import pathway." Experientia 46, no. 2 (1990): 153–61. http://dx.doi.org/10.1007/bf02027311.

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22

Brdiczka, D. "Interaction of mitochondrial porin with cytosolic proteins." Experientia 46, no. 2 (1990): 161–66. http://dx.doi.org/10.1007/bf02027312.

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23

Strogolova, Vera, Marianna Orlova, Aishwarya Shevade, and Sergei Kuchin. "Mitochondrial Porin Por1 and Its Homolog Por2 Contribute to the Positive Control of Snf1 Protein Kinase in Saccharomyces cerevisiae." Eukaryotic Cell 11, no. 12 (2012): 1568–72. http://dx.doi.org/10.1128/ec.00127-12.

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ABSTRACTSaccharomyces cerevisiaeSnf1 is a member of the conserved Snf1/AMP-activated protein kinase (Snf1/AMPK) family involved in regulating responses to energy limitation, which is detected by mechanisms that include sensing adenine nucleotides. Mitochondrial voltage-dependent anion channel (VDAC) proteins, also known as mitochondrial porins, are conserved in eukaryotes from yeast to humans and play key roles in mediating mitochondrial outer membrane permeability to small metabolites, including ATP, ADP, and AMP. We previously recovered the yeast mitochondrial porin Por1 (yVDAC1) from a two-

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24

Shuvo, Sabbir R., Uliana Kovaltchouk, Abdullah Zubaer, et al. "Functional characterization of an N-terminally-truncated mitochondrial porin expressed in Neurospora crassa." Canadian Journal of Microbiology 63, no. 8 (2017): 730–38. http://dx.doi.org/10.1139/cjm-2016-0764.

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Mitochondrial porin, which forms voltage-dependent anion-selective channels (VDAC) in the outer membrane, can be folded into a 19-β-stranded barrel. The N terminus of the protein is external to the barrel and contains α-helical structure. Targeted modifications of the N-terminal region have been assessed in artificial membranes, leading to different models for gating in vitro. However, the in vivo requirements for gating and the N-terminal segment of porin are less well-understood. Using Neurospora crassa porin as a model, the effects of a partial deletion of the N-terminal segment were invest

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25

Perez Velazquez, J. L., M. V. Frantseva, D. V. Huzar, and P. L. Carlen. "Mitochondrial porin required for ischemia-induced mitochondrial dysfunction and neuronal damage." Neuroscience 97, no. 2 (2000): 363–69. http://dx.doi.org/10.1016/s0306-4522(99)00569-2.

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26

Fritzen, Andreas, Frank Thøgersen, Kasper Thybo, et al. "Adaptations in Mitochondrial Enzymatic Activity Occurs Independent of Genomic Dosage in Response to Aerobic Exercise Training and Deconditioning in Human Skeletal Muscle." Cells 8, no. 3 (2019): 237. http://dx.doi.org/10.3390/cells8030237.

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Mitochondrial DNA (mtDNA) replication is thought to be an integral part of exercise-training-induced mitochondrial adaptations. Thus, mtDNA level is often used as an index of mitochondrial adaptations in training studies. We investigated the hypothesis that endurance exercise training-induced mitochondrial enzymatic changes are independent of genomic dosage by studying mtDNA content in skeletal muscle in response to six weeks of knee-extensor exercise training followed by four weeks of deconditioning in one leg, comparing results to the contralateral untrained leg, in 10 healthy, untrained mal

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27

Lima, Wanessa C. "The AK421 antibody recognizes the Dictyostelium mitochondrial porin by immunofluorescence." Antibody Reports 2, no. 3 (2019): e56. http://dx.doi.org/10.24450/journals/abrep.2019.e56.

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28

Bose, Mahuya, Randy M. Whittal, C. Gary Gairola, and Himangshu S. Bose. "Cigarette smoke decreases mitochondrial porin expression and steroidogenesis." Toxicology and Applied Pharmacology 227, no. 2 (2008): 284–90. http://dx.doi.org/10.1016/j.taap.2007.10.021.

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29

Báthori, György, Ildikó Szabó, Ibolya Schmehl, Francesco Tombola, Vito De Pinto, and Mario Zoratti. "Novel Aspects of the Electrophysiology of Mitochondrial Porin." Biochemical and Biophysical Research Communications 243, no. 1 (1998): 258–63. http://dx.doi.org/10.1006/bbrc.1997.7926.

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30

Báthori, György, Ildikö Szabö, Ibolya Schmehl, Francesco Tombola, Vito De Pinto, and Mario Zoratti. "Novel Aspects of the Electrophysiology of Mitochondrial Porin." Biochemical and Biophysical Research Communications 246, no. 1 (1998): 299. http://dx.doi.org/10.1006/bbrc.1998.8478.

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31

De Pinto, Vito, Roland Benz, Corrado Caggese, and Ferdinando Palmieri. "Characterization of the mitochondrial porin from Drosophila melanogaster." Biochimica et Biophysica Acta (BBA) - Biomembranes 987, no. 1 (1989): 1–7. http://dx.doi.org/10.1016/0005-2736(89)90447-1.

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32

Flinner, Nadine, Enrico Schleiff, and Oliver Mirus. "Identification of two voltage-dependent anion channel-like protein sequences conserved in Kinetoplastida." Biology Letters 8, no. 3 (2012): 446–49. http://dx.doi.org/10.1098/rsbl.2011.1121.

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The eukaryotic porin superfamily consists of two families, voltage-dependent anion channel (VDAC) and Tom40, which are both located in the mitochondrial outer membrane. In Trypanosoma brucei , only a single member of the VDAC family has been described. We report the detection of two additional eukaryotic porin-like sequences in T. brucei . By bioinformatic means, we classify both as putative VDAC isoforms.

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33

Lima, Wanessa C. "The AK421 antibody recognizes the Dictyostelium mitochondrial porin by Western blot." Antibody Reports 2, no. 3 (2019): e57. http://dx.doi.org/10.24450/journals/abrep.2019.e57.

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34

Summers, William A. T., John A. Wilkins, Ravi C. Dwivedi, Peyman Ezzati, and Deborah A. Court. "Mitochondrial dysfunction resulting from the absence of mitochondrial porin in Neurospora crassa." Mitochondrion 12, no. 2 (2012): 220–29. http://dx.doi.org/10.1016/j.mito.2011.09.002.

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35

Sakaguchi, Masao, Naomi Hachiya, Katsuyoshi Mihara, and Tsuneo Omura. "Mitochondrial Porin Can Be Translocated across Both Endoplasmic Reticulum and Mitochondrial Membranes1." Journal of Biochemistry 112, no. 2 (1992): 243–48. http://dx.doi.org/10.1093/oxfordjournals.jbchem.a123884.

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36

Smith, M., S. Hicks, K. Baker, and R. McCauley. "Rupture of the mitochondrial outer membrane impairs porin assembly." Journal of Biological Chemistry 269, no. 45 (1994): 28460–64. http://dx.doi.org/10.1016/s0021-9258(18)46949-9.

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37

Bay, Denice C., Joe D. O’Neil, and Deborah A. Court. "Two-Step Folding of Recombinant Mitochondrial Porin in Detergent." Biophysical Journal 94, no. 2 (2008): 457–68. http://dx.doi.org/10.1529/biophysj.107.115196.

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38

Guardiani, Carlo, Andrea Magrì, Andonis Karachitos, et al. "yVDAC2, the second mitochondrial porin isoform of Saccharomyces cerevisiae." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1859, no. 4 (2018): 270–79. http://dx.doi.org/10.1016/j.bbabio.2018.01.008.

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39

Pronevich, L. A., and T. A. Mirzabekov. "Reply: On interaction between mitochondrial porin and anion carriers." FEBS Letters 262, no. 1 (1990): 150–51. http://dx.doi.org/10.1016/0014-5793(90)80177-k.

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40

BENZ, Roland, Elke MAIER, Friedrich P. THINNES, Hilde GÖTZ, and Norbert HILSCHMANN. "Studies on Human Porin. VII. The Channel Properties of the Human B-Lymphocyte Membrane-Derived “Porin 31HL” are Similar to those of Mitochondrial Porins." Biological Chemistry Hoppe-Seyler 373, no. 1 (1992): 295–304. http://dx.doi.org/10.1515/bchm3.1992.373.1.295.

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41

Bayrhuber, Monika, Thomas Meins, Michael Habeck, et al. "Structure of the human voltage-dependent anion channel." Proceedings of the National Academy of Sciences 105, no. 40 (2008): 15370–75. http://dx.doi.org/10.1073/pnas.0808115105.

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The voltage-dependent anion channel (VDAC), also known as mitochondrial porin, is the most abundant protein in the mitochondrial outer membrane (MOM). VDAC is the channel known to guide the metabolic flux across the MOM and plays a key role in mitochondrially induced apoptosis. Here, we present the 3D structure of human VDAC1, which was solved conjointly by NMR spectroscopy and x-ray crystallography. Human VDAC1 (hVDAC1) adopts a β-barrel architecture composed of 19 β-strands with an α-helix located horizontally midway within the pore. Bioinformatic analysis indicates that this channel archite

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42

Kleene, R., N. Pfanner, R. Pfaller, et al. "Mitochondrial porin of Neurospora crassa: cDNA cloning, in vitro expression and import into mitochondria." EMBO Journal 6, no. 9 (1987): 2627–33. http://dx.doi.org/10.1002/j.1460-2075.1987.tb02553.x.

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43

Pinto, Vito De, Massimo Tommasino, Roland Benz, and Ferdinando Palmieri. "The 35 kDa DCCD-binding protein from pig heart mitochondria is the mitochondrial porin." Biochimica et Biophysica Acta (BBA) - Biomembranes 813, no. 2 (1985): 230–42. http://dx.doi.org/10.1016/0005-2736(85)90238-x.

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44

Harada, Takeshi, Ryota Sada, Yoshito Osugi, et al. "Palmitoylated CKAP4 regulates mitochondrial functions through an interaction with VDAC2 at ER–mitochondria contact sites." Journal of Cell Science 133, no. 21 (2020): jcs249045. http://dx.doi.org/10.1242/jcs.249045.

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ABSTRACTCytoskeleton-associated protein 4 (CKAP4) is a palmitoylated type II transmembrane protein localized to the endoplasmic reticulum (ER). Here, we found that knockout (KO) of CKAP4 in HeLaS3 cells induces the alteration of mitochondrial structures and increases the number of ER–mitochondria contact sites. To understand the involvement of CKAP4 in mitochondrial functions, the binding proteins of CKAP4 were explored, enabling identification of the mitochondrial porin voltage-dependent anion-selective channel protein 2 (VDAC2), which is localized to the outer mitochondrial membrane. Palmito

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45

Benz, Roland, Matthias Kottke, and Dieter Brdiczka. "The cationically selective state of the mitochondrial outer membrane pore: a study with intact mitochondria and reconstituted mitochondrial porin." Biochimica et Biophysica Acta (BBA) - Biomembranes 1022, no. 3 (1990): 311–18. http://dx.doi.org/10.1016/0005-2736(90)90279-w.

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46

Runke, Greg, Elke Maier, William A. T. Summers, Denice C. Bay, Roland Benz, and Deborah A. Court. "Deletion Variants of Neurospora Mitochondrial Porin: Electrophysiological and Spectroscopic Analysis." Biophysical Journal 90, no. 9 (2006): 3155–64. http://dx.doi.org/10.1529/biophysj.105.072520.

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47

Sakaue, Haruka, and Toshiya Endo. "Regulation of the protein entry gate assembly by mitochondrial porin." Current Genetics 65, no. 5 (2019): 1161–63. http://dx.doi.org/10.1007/s00294-019-00979-7.

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48

ONO, Hideyu, and Syozo TUBOI. "Integration of porin synthesized in vitro into outer mitochondrial membranes." European Journal of Biochemistry 168, no. 3 (1987): 509–14. http://dx.doi.org/10.1111/j.1432-1033.1987.tb13447.x.

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49

VELAZQUEZ, J. L. PEREZ, M. V. FRANTSEVA, D. HUZAR, C. GUEZURIAN, and P. L. CARLEN. "Mitochondrial Porin, a Novel Target to Prevent Ischemia-Induced Neurodegeneration?" Annals of the New York Academy of Sciences 893, no. 1 OXIDATIVE/ENE (1999): 369–71. http://dx.doi.org/10.1111/j.1749-6632.1999.tb07857.x.

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50

Pronevich, Ludmila A., Tajib A. Mirzabekov, and Zinaida E. Rozhdestvenskaya. "Mitochondrial porin regulates the sensitivity of anion carriers to inhibitors." FEBS Letters 247, no. 2 (1989): 330–32. http://dx.doi.org/10.1016/0014-5793(89)81363-8.

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