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Destination: inner nuclear membrane
Trends in Cell Biology, 2014The inner nuclear membrane (INM) of eukaryotic cells is enriched in proteins that are required for nuclear structure, chromosome organization, DNA repair, and transcriptional control. Mislocalization of INM proteins is observed in a wide spectrum of human diseases; however, the mechanism by which INM proteins reach their final destination is poorly ...
Santharam S, Katta +2 more
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Inner membrane dynamics in mitochondria
Journal of Structural Biology, 2013Combining the use of cells with sparse cristae marked with IMP-EGFP and short pulsed sub-saturating fluorescence excitation (non-saturation fluorescence microscopy/NSFM) revealed inhomogeneous fluorescence distribution along mitochondria in living cells.
Daniel, Dikov, Juergen, Bereiter-Hahn
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Bilirubin increases mitochondrial inner membrane conductance
Biochemical Medicine, 1985Bilirubin accumulates within, and induces loose coupling in, rat liver mitochondria. This state, characterized by a normal protonmotive force, but increased oxygen consumption and inner membrane conductance, could impair cellular energy metabolism. Loose coupling is observed at bilirubin concentrations (12-24 microM) attained in tissues of kernicteric ...
D A, Stumpf, L A, Eguren, J K, Parks
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Assembly of Bacterial Inner Membrane Proteins
Annual Review of Biochemistry, 2011Numerous membrane proteins form multisubunit protein complexes, which contain both integral and peripheral subunits, in addition to prosthetic groups. Bacterial membrane proteins are inserted into the inner membrane by the Sec translocase and YidC insertase.
Ross E, Dalbey +2 more
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Electrophysiology of the inner mitochondrial membrane
Journal of Bioenergetics and Biomembranes, 1994The application of electrophysiological techniques to mitochondrial membranes has allowed the observation and partial characterization of several ion channels, including an ATP-sensitive K(+)-selective one, a high-conductance "megachannel", a 107 pS anionic channel and three others studied at alkaline pH's.
Zoratti M, SZABO', ILDIKO'
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Permeability of the Inner Ear Membranes
Acta Oto-Laryngologica, 1969Soluted substances can penetrate through epithelial layers either by free diffusion through the intercellular spaces or by transcellular transport. By injection of th. as a tracer into peri- and endolymph we found a typical transcellular transport of the tracer through Reissner's membrane in micropinocytosis vesicles.
C V, Ilberg, K H, Vosteen
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Biogenesis of bacterial inner-membrane proteins
Cellular and Molecular Life Sciences, 2010All cells must traffic proteins into and across their membranes. In bacteria, several pathways have evolved to enable protein transfer across the inner membrane, the periplasm, and the outer membrane. The major route of protein translocation in and across the cytoplasmic membrane is the general secretion pathway (Sec-pathway).
Sandra J, Facey, Andreas, Kuhn
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Inner Membrane Translocases and Insertases
2019The inner membrane of Gram-negative bacteria is a ~6 nm thick phospholipid bilayer. It forms a semi-permeable barrier between the cytoplasm and periplasm allowing only regulated export and import of ions, sugar polymers, DNA and proteins. Inner membrane proteins, embedded via hydrophobic transmembrane α-helices, play an essential role in this regulated
Jozefien, De Geyter +3 more
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Biochimica et Biophysica Acta (BBA) - Biomembranes, 1992
The amino terminal 29 amino acids of the outer mitochondrial membrane protein of yeast, OMM70 (MAS70), consisting of the targeting and membrane anchor domains, has been fused to a reporter protein, dihydrofolate reductase. The hybrid protein, designated pOMD29, was efficiently imported into the outer membrane of rat heart mitochondria by a process ...
J M, Li, G C, Shore
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The amino terminal 29 amino acids of the outer mitochondrial membrane protein of yeast, OMM70 (MAS70), consisting of the targeting and membrane anchor domains, has been fused to a reporter protein, dihydrofolate reductase. The hybrid protein, designated pOMD29, was efficiently imported into the outer membrane of rat heart mitochondria by a process ...
J M, Li, G C, Shore
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Inner nuclear membrane and signal transduction
Journal of Cellular Biochemistry, 2005AbstractRecent research has shown that the inner nuclear membrane is a site for regulation of signal transduction from the plasma membrane to the nucleus. This has coincided with discoveries showing that mutations in extrinsic and intrinsic inner nuclear membrane proteins cause a variety of inherited diseases. In most instances, the mechanisms by which
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