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Relevant bibliographies by topics / Mitochondrial targeting sequence

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Journal articles

Academic literature on the topic 'Mitochondrial targeting sequence'

Author: Grafiati

Published: 25 May 2024

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Journal articles on the topic "Mitochondrial targeting sequence"

1

LEISSRING, Malcolm A., Wesley FARRIS, Xining WU, et al. "Alternative translation initiation generates a novel isoform of insulin-degrading enzyme targeted to mitochondria." Biochemical Journal 383, no. 3 (2004): 439–46. http://dx.doi.org/10.1042/bj20041081.

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IDE (insulin-degrading enzyme) is a widely expressed zinc-metallopeptidase that has been shown to regulate both cerebral amyloid β-peptide and plasma insulin levels in vivo. Genetic linkage and allelic association have been reported between the IDE gene locus and both late-onset Alzheimer's disease and Type II diabetes mellitus, suggesting that altered IDE function may contribute to some cases of these highly prevalent disorders. Despite the potentially great importance of this peptidase to health and disease, many fundamental aspects of IDE biology remain unresolved. Here we identify a previo

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2

Faria, Rúben, Eric Vivés, Prisca Boisguerin, Angela Sousa, and Diana Costa. "Development of Peptide-Based Nanoparticles for Mitochondrial Plasmid DNA Delivery." Polymers 13, no. 11 (2021): 1836. http://dx.doi.org/10.3390/polym13111836.

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A mitochondrion is a cellular organelle able to produce cellular energy in the form of adenosine triphosphate (ATP). As in the nucleus, mitochondria contain their own genome: the mitochondrial DNA (mtDNA). This genome is particularly susceptible to mutations that are at the basis of a multitude of disorders, especially those affecting the heart, the central nervous system and muscles. Conventional clinical practice applied to mitochondrial diseases is very limited and ineffective; a clear need for innovative therapies is demonstrated. Gene therapy seems to be a promising approach. The use of m

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3

Baysal, Can, Ana Pérez-González, Álvaro Eseverri, et al. "Recognition motifs rather than phylogenetic origin influence the ability of targeting peptides to import nuclear-encoded recombinant proteins into rice mitochondria." Transgenic Research 29, no. 1 (2019): 37–52. http://dx.doi.org/10.1007/s11248-019-00176-9.

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Abstract Mitochondria fulfil essential functions in respiration and metabolism as well as regulating stress responses and apoptosis. Most native mitochondrial proteins are encoded by nuclear genes and are imported into mitochondria via one of several receptors that recognize N-terminal signal peptides. The targeting of recombinant proteins to mitochondria therefore requires the presence of an appropriate N-terminal peptide, but little is known about mitochondrial import in monocotyledonous plants such as rice (Oryza sativa). To gain insight into this phenomenon, we targeted nuclear-encoded enh

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4

Kaufmann, Thomas, Sarah Schlipf, Javier Sanz, Karin Neubert, Reuven Stein, and Christoph Borner. "Characterization of the signal that directs Bcl-xL, but not Bcl-2, to the mitochondrial outer membrane." Journal of Cell Biology 160, no. 1 (2003): 53–64. http://dx.doi.org/10.1083/jcb.200210084.

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It is assumed that the survival factors Bcl-2 and Bcl-xL are mainly functional on mitochondria and therefore must contain mitochondrial targeting sequences. Here we show, however, that only Bcl-xL is specifically targeted to the mitochondrial outer membrane (MOM) whereas Bcl-2 distributes on several intracellular membranes. Mitochondrial targeting of Bcl-xL requires the COOH-terminal transmembrane (TM) domain flanked at both ends by at least two basic amino acids. This sequence is a bona fide targeting signal for the MOM as it confers specific mitochondrial localization to soluble EGFP. The si

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5

Takada, Y., N. Kaneko, H. Esumi, P. E. Purdue, and C. J. Danpure. "Human peroxisomal l-alanine: glyoxylate aminotransferase. Evolutionary loss of a mitochondrial targeting signal by point mutation of the initiation codon." Biochemical Journal 268, no. 2 (1990): 517–20. http://dx.doi.org/10.1042/bj2680517.

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The amino acid sequence of human hepatic peroxisomal L-alanine: glyoxylate aminotransferase 1 (AGTI) deduced from cDNA shows 78% sequence identity with that of rat mitochondrial AGTI, but lacks the N-terminal 22 amino acids (the putative mitochondrial targeting signal). In humans this signal appears to have been deleted during evolution by a point mutation of the initiation codon ATG to ATA. These data suggest that the targeting defect in primary hyperoxaluria type 1, in which AGT1 is diverted from the peroxisomes to the mitochondria, could be due to a point mutation that reintroduces all or p

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6

Majumdar, Ramanath, та William A. Bridger. "Mitochondrial translocation and processing of the precursor to the α-subunit of rat liver succinyl-CoA synthetase". Biochemistry and Cell Biology 68, № 1 (1990): 292–99. http://dx.doi.org/10.1139/o90-040.

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Succinyl-CoA synthetase functions in the mitochondrial matrix as an αβ-dimer. Its constitutive subunits are thus expected to be encoded in the nucleus and synthesized in the cytoplasm as precursors containing signal sequences for mitochondrial translocation. We have previously reported the isolation and sequence of a rat liver cDNA clone (λSCS19) that apparently encodes the cytoplasmic precursor to the α-subunit. Here we report the preparation of mRNA transcripts of this cDNA insert and their in vitro translation to produce labeled protein that can be translocated across the membranes of subse

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7

Miyazaki, Emi, Yuichiro Kida, Katsuyoshi Mihara, and Masao Sakaguchi. "Switching the Sorting Mode of Membrane Proteins from Cotranslational Endoplasmic Reticulum Targeting to Posttranslational Mitochondrial Import." Molecular Biology of the Cell 16, no. 4 (2005): 1788–99. http://dx.doi.org/10.1091/mbc.e04-08-0707.

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Hydrophobic membrane proteins are cotranslationally targeted to the endoplasmic reticulum (ER) membrane, mediated by hydrophobic signal sequence. Mitochondrial membrane proteins escape this mechanism despite their hydrophobic character. We examined sorting of membrane proteins into the mitochondria, by using mitochondrial ATP-binding cassette (ABC) transporter isoform (ABC-me). In the absence of 135-residue N-terminal hydrophilic segment (N135), the membrane domain was integrated into the ER membrane in COS7 cells. Other sequences that were sufficient to import soluble protein into mitochondri

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8

Romesberg, Amy, and Bennett Van Houten. "Targeting Mitochondrial Function with Chemoptogenetics." Biomedicines 10, no. 10 (2022): 2459. http://dx.doi.org/10.3390/biomedicines10102459.

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Mitochondria are ATP-generating organelles in eukaryotic cells that produce reactive oxygen species (ROS) during oxidative phosphorylation (OXPHOS). Mitochondrial DNA (mtDNA) is packaged within nucleoids and, due to its close proximity to ROS production, endures oxidative base damage. This damage can be repaired by base excision repair (BER) within the mitochondria, or it can be degraded via exonucleases or mitophagy. Persistent mtDNA damage may drive the production of dysfunctional OXPHOS components that generate increased ROS, or OXPHOS components may be directly damaged by ROS, which then c

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9

Chang, Yu-Jung, Kuan-Wei Chen, and Linyi Chen. "Mitochondrial ROS1 Increases Mitochondrial Fission and Respiration in Oral Squamous Cancer Carcinoma." Cancers 12, no. 10 (2020): 2845. http://dx.doi.org/10.3390/cancers12102845.

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Increased ROS proto-oncogene 1 (ROS1) expression has been implicated in the invasiveness of human oral squamous cell carcinoma (OSCC). The cellular distribution of ROS1 has long-been assumed at the plasma membrane. However, a previous work reported a differential cellular distribution of mutant ROS1 derived from chromosomal translocation, resulting in increased carcinogenesis. We thus hypothesized that cellular distribution of upregulated ROS1 in OSCC may correlate with invasiveness. We found that ROS1 can localize to mitochondria in the highly invasive OSCC and identified a mitochondria-targe

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10

Santos, Herbert J., Yoko Chiba, Takashi Makiuchi, et al. "Import of Entamoeba histolytica Mitosomal ATP Sulfurylase Relies on Internal Targeting Sequences." Microorganisms 8, no. 8 (2020): 1229. http://dx.doi.org/10.3390/microorganisms8081229.

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Mitochondrial matrix proteins synthesized in the cytosol often contain amino (N)-terminal targeting sequences (NTSs), or alternately internal targeting sequences (ITSs), which enable them to be properly translocated to the organelle. Such sequences are also required for proteins targeted to mitochondrion-related organelles (MROs) that are present in a few species of anaerobic eukaryotes. Similar to other MROs, the mitosomes of the human intestinal parasite Entamoeba histolytica are highly degenerate, because a majority of the components involved in various processes occurring in the canonical

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