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Academic literature on the topic 'Inside-out vesicles'

Author: Grafiati
Published: 6 September 2023

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Journal articles on the topic "Inside-out vesicles"

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Albertsson, Per-Åke, Per Svensson, Agneta Persson, G. Dallner, and Petter Gustafsson. "Subfractionation of Inside-Out Thylakoid Vesicles." Acta Chemica Scandinavica 41b (1987): 134–36. http://dx.doi.org/10.3891/acta.chem.scand.41b-0134.

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Palmgren, Michael Gjedde, Per Askerlund, Karin Fredrikson, Susanne Widell, Marianne Sommarin, and Christer Larsson. "Sealed Inside-Out and Right-Side-Out Plasma Membrane Vesicles." Plant Physiology 92, no. 4 (April 1, 1990): 871–80. http://dx.doi.org/10.1104/pp.92.4.871.

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Mankelow, Tosti J., Rebecca E. Griffiths, Joanna F. Flatt, and David J. Anstee. "Human Reticulocytes Extrude Inside-Out, Phosphatidylserine-Exposed, Autophagic Vesicles During The Final Step In The Formation Of Erythrocytes." Blood 122, no. 21 (November 15, 2013): 941. http://dx.doi.org/10.1182/blood.v122.21.941.941.

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Abstract During maturation to an erythrocyte, a reticulocyte must degrade or eliminate its residual cytosolic organelles and reduce its surface area. Using confocal microscopy, we show that in late reticulocytes produced from an in vitro culture system, this is achieved through a novel form of exocytosis whereby large (∼1.4um) intact, inside-out phosphatidylserine-exposed vesicles are expelled from the maturing reticulocyte. The vesicles contain organelle marker proteins and numerous erythroid membrane proteins, notably CD71, CD147 and stomatin. The presence of ubiquitin within these vesicles suggests a recognised mechanism for the targeting of proteins for extracellular export or degradation. The exocytosed vesicles are identical to intracellular GPA-decorated autophagic vesicles previously identified in cultured reticulocytes (Griffiths et al 2012). GPA-decorated vesicles are also seen in some cells in peripheral blood. Proteins involved in vesicle trafficking, SNARE (VAMP7), ESCRT (CHMP4B) and myosin, locate to defined positions at the point of vesicle extrusion. We hypothesize that the exposed “eat me” phosphatidylserine signal ensures that released autophagic vesicles are rapidly removed from circulation by professional phagocytic cells within the spleen thus ensuring maturation to erythrocytes without the release of potentially toxic material into circulation. Our results describe a previously unrecognised mode of exocytosis which may have significance beyond erythropoiesis particularly with respect to apoptosis and autophagy and reveal the final step in the formation of human erythrocytes. Reference Griffiths RE, Kupzig S, Cogan N, Mankelow TJ, Betin VM, Trakarnsanga K, Massey EJ, Lane JD, Parsons SF, Anstee DJ.Maturing reticulocytes internalize plasma membrane in glycophorin A-containing vesicles that fuse with autophagosomes before exocytosis. Blood. 2012 Jun 28;119(26):6296-306. Disclosures: No relevant conflicts of interest to declare.
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Schoenmakers, T. J., and G. Flik. "Sodium-extruding and calcium-extruding sodium/calcium exchangers display similar calcium affinities." Journal of Experimental Biology 168, no. 1 (July 1, 1992): 151–59. http://dx.doi.org/10.1242/jeb.168.1.151.

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Na+/Ca2+ exchange activities in purely inside-out and mixed inside-out and right-side-out fish enterocyte basolateral plasma membrane vesicle preparations display equal affinities for Ca2+, showing that only the intracellular Ca2+ transport site of the Na+/Ca2+ exchanger is detected in experiments on vesicle preparations with mixed orientation. Therefore, Ca2+ pump and Na+/Ca2+ exchange activity may be compared directly without correction for vesicle orientation. The Na+/Ca2+ exchange activity in fish enterocyte vesicles is compared to the activity found in dog erythrocyte vesicles. The calcium-extruding exchanger in fish basolateral plasma membranes shows values of Km and V(max) for calcium similar to those found for the sodium-extruding exchanger in dog erythrocyte membranes, indicating that differences in electrochemical gradients underlie the difference in cellular function of the two exchangers.
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LaBelle, E. F., S. V. Singh, S. K. Srivastava, and Y. C. Awasthi. "Dinitrophenyl glutathione efflux from human erythrocytes is primary active ATP-dependent transport." Biochemical Journal 238, no. 2 (September 1, 1986): 443–49. http://dx.doi.org/10.1042/bj2380443.

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Dinitrophenyl S-glutathione is accumulated by inside-out vesicles made from human erythrocytes in a process totally dependent on ATP and Mg2+. The vesicles were shown to accumulate dinitrophenyl S-glutathione against a concentration gradient. The vesicles were able to concentrate this glutathione derivative even in the absence of membrane potential. This indicated that the ATP-dependent uptake of dinitrophenyl S-glutathione by inside-out vesicles represented an active transport process. Neither extravesicular EGTA nor intravesicular ouabain inhibited the transport process, indicating that neither the Ca2+-ATPase nor the Na+, K+-ATPase were involved. These results indicated that dinitrophenyl S-glutathione uptake by inside-out vesicles probably represented primary active transport. The uptake of dinitrophenyl S-glutathione was a linear function of time (up to 5 h) and vesicle protein. The rate of uptake was optimal between pH 7.0 and 8.0 and at 37 degrees C. The Km values determined for dinitrophenyl S-glutathione and ATP were 0.29 mM and 1 mM, respectively. The transport process was completely inhibited by vanadate and by p-hydroxymercuribenzene sulphonate and inhibited to a lesser extent by N-ethylmaleimide. GTP could efficiently substitute for ATP as an energy source for the transport process, but CTP and UTP were comparatively much less effective.
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Ames, G. F., K. Nikaido, J. Groarke, and J. Petithory. "Reconstitution of periplasmic transport in inside-out membrane vesicles." Journal of Biological Chemistry 264, no. 7 (March 1989): 3998–4002. http://dx.doi.org/10.1016/s0021-9258(19)84951-7.

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Nilsson, Fredrik, David J. Simpson, Alison C. Stewart, and Bertil Andersson. "Generation and isolation of cyanobacterial inside-out thylakoid vesicles." Archives of Biochemistry and Biophysics 265, no. 2 (September 1988): 321–28. http://dx.doi.org/10.1016/0003-9861(88)90134-8.

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ERICKSON, Hans K., and Jack KYTE. "Lysine-691 of the anion exchanger from human erythrocytes is located on its cytoplasmic surface." Biochemical Journal 336, no. 2 (December 1, 1998): 443–49. http://dx.doi.org/10.1042/bj3360443.

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A combination of vectorial modification and site-directed immunochemistry has been used to determine the disposition, with respect to the membrane, of Lys-691 of the anion exchanger from human erythrocytes. Intact erythrocytes and inside-out vesicles were vectorially modified in the same container with pyridoxal phosphate and sodium [3H]borohydride. The modified inside-out vesicles were separated from erythrocytes by differential centrifugation and the vesicles and erythrocyte membranes were treated with alkali and digested with trypsin and thermolysin to liberate the peptides IVSKPER and IVSK{Nε-[4´-(5´-phospho-[4-3H]pyridoxyl)]}PER. These peptides, containing the unmodified and modified versions of Lys-691, were retrieved from the digests by site-directed immunochemistry and were identified by HPLC and liquid scintillation spectroscopy. Both the inside-out vesicles and the intact erythrocytes contained the peptide IVSKPER, however, the 3H-label from the phosphopyridoxylated peptide could be detected only in the inside-out vesicles. The incorporation of 3H into Lys-691 of the anion exchanger from inside-out vesicles was at least 30-fold greater than the incorporation into Lys-691 of the anion exchanger from intact erythrocytes. It follows that Lys-691 of the anion exchanger is located on the cytoplasmic surface of the plasma membrane.
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Lew, Virgilio L., Austin Hockaday, Maria-Isabel Sepulveda, Andrew P. Somlyo, Avril V. Somlyo, Olga E. Ortiz, and Robert M. Bookchin. "Compartmentalization of sickle-cell calcium in endocytic inside-out vesicles." Nature 315, no. 6020 (June 1985): 586–89. http://dx.doi.org/10.1038/315586a0.

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Lew, V. L., A. Hockaday, C. J. Freeman, and R. M. Bookchin. "Mechanism of spontaneous inside-out vesiculation of red cell membranes." Journal of Cell Biology 106, no. 6 (June 1, 1988): 1893–901. http://dx.doi.org/10.1083/jcb.106.6.1893.

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In certain conditions, human red cell membranes spontaneously form inside out vesicles within 20 min after hypotonic lysis. Study of the geometry of this process now reveals that, contrary to earlier views of vesiculation by endocytosis or by the mechanical shearing of cytoskeleton-depleted membrane, lysis generates a persistent membrane edge which spontaneously curls, cuts, and splices the membrane surface to form single or concentric vesicles. Analysis of the processes by which proteins may stabilize a free membrane edge led us to formulate a novel zip-type mechanism for membrane cutting-splicing and fusion even in the absence of free edges. Such protein-led membrane fusion represents an alternative to mechanisms of membrane fusion based on phospholipid interactions, and may prove relevant to processes of secretion, endocytosis, phagocytosis, and membrane recycling in many cell types.
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Book chapters on the topic "Inside-out vesicles"

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Zak, Elena, Birgitta Norling, Bertil Andersson, and Himadri B. Pakrasi. "Isolation of Inside-Out and Right-Side-Out Thylakoid Membrane Vesicles from the Cyanobacterium Synechocystis 6803." In Photosynthesis: Mechanisms and Effects, 3103–6. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-011-3953-3_726.

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Dädelow, J., A. Radunz, and G. H. Schmid. "Localization of Lipids and Xanthophylls in Inside-Out Vesicles from Thylakoids of Nicotiana Tabacum." In Plant Lipid Metabolism, 164–69. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-015-8394-7_45.

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Svensson, Per, and Per-Åke Albertsson. "Subfractionation of Inside-Out Thylakoid Vesicles-Preparation of Pure Photosystem II Particles without using Detergent." In Progress in Photosynthesis Research, 281–84. Dordrecht: Springer Netherlands, 1987. http://dx.doi.org/10.1007/978-94-009-3535-8_68.

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Kurreck, J., A. G. Seeliger, F. Reifarth, M. Karge, and G. Renger. "Reconstitution of the Plastoquinone Pool of Inside Out Vesicles, PSII Membrane Fragments and Core Complexes from Higher Plants." In Photosynthesis: from Light to Biosphere, 551–54. Dordrecht: Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-009-0173-5_128.

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Askerlund, Per, Christer Larsson, and Susanne Widell. "Localisation of Donor and Acceptor Sites of NAD(P)H Dehydrogenase(S) Using “Inside-Out” and “Right-Side-Out” Plant Plasma Membrane Vesicles, and Characterization of Plasma Membrane-Bound b-Cytochromes." In Plasma Membrane Oxidoreductases in Control of Animal and Plant Growth, 397–98. Boston, MA: Springer US, 1988. http://dx.doi.org/10.1007/978-1-4684-8029-0_44.

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Åkerlund, Hans-Erik, and Bertil Andersson. "[26] Isolation procedures for inside-out thylakoid vesicles." In Methods in Enzymology, 252–59. Elsevier, 1987. http://dx.doi.org/10.1016/0076-6879(87)48028-2.

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García-Sancho, Javier, and Javier Alvarez. "[22] Preparation and properties of one-step inside-out vesicles from red cell membranes." In Biomembranes Part T, 368–76. Elsevier, 1989. http://dx.doi.org/10.1016/s0076-6879(89)73024-x.

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Larsson, Christer, Marianne Sommarin, and Susanne Widell. "[44] Isolation of highly purified plant plasma membranes and separation of inside-out and right-side-out vesicles." In Methods in Enzymology, 451–69. Elsevier, 1994. http://dx.doi.org/10.1016/0076-6879(94)28046-0.

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Blostein, Rhoda, and William J. Harvey. "[23] Na+,K+-pump stoichiometry and coupling in inside-out vesicles from red blood cell membranes." In Biomembranes Part T, 377–80. Elsevier, 1989. http://dx.doi.org/10.1016/s0076-6879(89)73025-1.

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Blostein, Rhoda. "[16] Measurement of Na+ and K+ transport and Na+,K+-ATPase activity in inside-out vesicles from mammalian erythrocytes." In Methods in Enzymology, 171–78. Elsevier, 1988. http://dx.doi.org/10.1016/0076-6879(88)56019-6.

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Conference papers on the topic "Inside-out vesicles"

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EzzEldin, Hussein M., and Santiago D. Solares. "Calculation of Isothermal Intrinsic Compressibility and Compression of GvpA Protein in Halobacterium sp. NRC-1 Using Molecular Modeling and Dynamics." In ASME 2009 International Design Engineering Technical Conferences and Computers and Information in Engineering Conference. ASMEDC, 2009. http://dx.doi.org/10.1115/detc2009-86265.

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Gas vesicles are low-density, gas-filled protein organelles found inside various microorganisms. They have a lipid-free membrane with an average thickness of 2 nm and provide their hosts with buoyancy. In this study we characterized gas vesicle proteins synthesized by the Halobacterium sp. NRC-1 strain making use of molecular modeling methods and molecular dynamics (MD) simulations. The tertiary structure of GvpA protein, the major constituent of the gas vesicle membrane, was predicted using the De Novo computational design method available in the Rosetta Suite 2.3.1 software and was found to be in agreement with experimental data available from previous studies conducted by others and the consensus of different secondary structure prediction web servers. Optimization of the predicted structure was first carried out by energy minimization and simulated annealing. Subsequently, the mechanical properties of GvpA were investigated via constant pressure and temperature (NPT) aqueous MD simulations, in which two approaches were used to study the isothermal compressibility: quantification of the fluctuations in protein volume at constant pressure and temperature, and quantification of the volume changes induced through changes in the simulation pressure. Long term we plan to incorporate this information into multi-scale models of whole gas vesicles.
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Windes, Peter W., Danesh K. Tafti, and Bahareh Behkam. "Computational Model of Human Capillary Hydrodynamics." In ASME 2016 Fluids Engineering Division Summer Meeting collocated with the ASME 2016 Heat Transfer Summer Conference and the ASME 2016 14th International Conference on Nanochannels, Microchannels, and Minichannels. American Society of Mechanical Engineers, 2016. http://dx.doi.org/10.1115/fedsm2016-7858.

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The present work lays out an accurate, three-dimensional computational fluid dynamics (CFD) model of a human blood capillary. This model is composed of red blood cells and blood plasma inside a cylindrical section of a capillary. The plasma flow is resolved using an incompressible Navier-Stokes solver. At the level of capillaries, red blood cells must be individually handled to correctly resolve the hydrodynamics in the system. They cannot be lumped in with the plasma and considered as a non-Newtonian suspension because of the relative scale of the capillaries and the blood cells. Red blood cells act as highly deformable, fluid filled vesicles which readily deform from their typical biconcave shape when passing through narrow capillaries. In the present model, the deformed shape of red blood cells is predicted using a combination of analytical models and experimental data on cell deformation. The cell volume, cell surface area, and plasma layer thickness are found to be the key parameters which define red blood cell deformation in capillaries. The red blood cells are imposed in the flow using the immersed boundary method (IBM). To save computational resources while still yielding an accurate model, the deformed shape of each red blood cell is calculated once prior to running the simulation and then held constant throughout the run. In order to validate the model, two parameters — apparent relative viscosity and hematocrit ratio — were examined. The present model shows good comparison to experimental values for both these parameters.
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