Статті в журналах з теми "Membrance domains"
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Dale, B., E. Tosti, and M. Iaccarino. "Is the plasma membrane of the human oocyte reorganised following fertilisation and early cleavage?" Zygote 3, no. 1 (February 1995): 31–36. http://dx.doi.org/10.1017/s0967199400002355.
Повний текст джерелаSnead, Wilton T., Wade F. Zeno, Grace Kago, Ryan W. Perkins, J. Blair Richter, Chi Zhao, Eileen M. Lafer, and Jeanne C. Stachowiak. "BAR scaffolds drive membrane fission by crowding disordered domains." Journal of Cell Biology 218, no. 2 (November 30, 2018): 664–82. http://dx.doi.org/10.1083/jcb.201807119.
Повний текст джерелаGallop, Jennifer L., and Harvey T. McMahon. "BAR domains and membrane curvature: bringing your curves to the BAR." Biochemical Society Symposia 72 (January 1, 2005): 223–31. http://dx.doi.org/10.1042/bss0720223.
Повний текст джерелаGolantsova, Nina E., Elena E. Gorbunova, and Erich R. Mackow. "Discrete Domains within the Rotavirus VP5* Direct Peripheral Membrane Association and Membrane Permeability." Journal of Virology 78, no. 4 (February 15, 2004): 2037–44. http://dx.doi.org/10.1128/jvi.78.4.2037-2044.2004.
Повний текст джерелаChowdary, Tirumala Kumar, and Ekaterina E. Heldwein. "Syncytial Phenotype of C-Terminally Truncated Herpes Simplex Virus Type 1 gB Is Associated with Diminished Membrane Interactions." Journal of Virology 84, no. 10 (March 3, 2010): 4923–35. http://dx.doi.org/10.1128/jvi.00206-10.
Повний текст джерелаYamamoto, Eiji, Jan Domański, Fiona B. Naughton, Robert B. Best, Antreas C. Kalli, Phillip J. Stansfeld, and Mark S. P. Sansom. "Multiple lipid binding sites determine the affinity of PH domains for phosphoinositide-containing membranes." Science Advances 6, no. 8 (February 2020): eaay5736. http://dx.doi.org/10.1126/sciadv.aay5736.
Повний текст джерелаKarotki, Lena, Juha T. Huiskonen, Christopher J. Stefan, Natasza E. Ziółkowska, Robyn Roth, Michal A. Surma, Nevan J. Krogan, et al. "Eisosome proteins assemble into a membrane scaffold." Journal of Cell Biology 195, no. 5 (November 28, 2011): 889–902. http://dx.doi.org/10.1083/jcb.201104040.
Повний текст джерелаPennington, Edward Ross, E. Madison Sullivan, Amy Fix, Sahil Dadoo, Tonya N. Zeczycki, Anita DeSantis, Uwe Schlattner, et al. "Proteolipid domains form in biomimetic and cardiac mitochondrial vesicles and are regulated by cardiolipin concentration but not monolyso-cardiolipin." Journal of Biological Chemistry 293, no. 41 (August 29, 2018): 15933–46. http://dx.doi.org/10.1074/jbc.ra118.004948.
Повний текст джерелаMa, Alice D., Lawrence F. Brass, and Charles S. Abrams. "Pleckstrin Associates with Plasma Membranes and Induces the Formation of Membrane Projections: Requirements for Phosphorylation and the NH2-terminal PH Domain." Journal of Cell Biology 136, no. 5 (March 10, 1997): 1071–79. http://dx.doi.org/10.1083/jcb.136.5.1071.
Повний текст джерелаGILLOOLY, David J., Anne SIMONSEN, and Harald STENMARK. "Cellular functions of phosphatidylinositol 3-phosphate and FYVE domain proteins." Biochemical Journal 355, no. 2 (April 6, 2001): 249–58. http://dx.doi.org/10.1042/bj3550249.
Повний текст джерелаVoleti, Rashmi, Diana R. Tomchick, Thomas C. Südhof, and Josep Rizo. "Exceptionally tight membrane-binding may explain the key role of the synaptotagmin-7 C2A domain in asynchronous neurotransmitter release." Proceedings of the National Academy of Sciences 114, no. 40 (September 18, 2017): E8518—E8527. http://dx.doi.org/10.1073/pnas.1710708114.
Повний текст джерелаBeaulieu, Nadine, Bari Zahedi, Rebecca E. Goulding, Ghazaleh Tazmini, Kira V. Anthony, Stephanie L. Omeis, Danielle R. de Jong, and Robert J. Kay. "Regulation of RasGRP1 by B Cell Antigen Receptor Requires Cooperativity between Three Domains Controlling Translocation to the Plasma Membrane." Molecular Biology of the Cell 18, no. 8 (August 2007): 3156–68. http://dx.doi.org/10.1091/mbc.e06-10-0932.
Повний текст джерелаLü, Junhong, Steven W. Pipe, Hongzhi Miao, Marc Jacquemin, and Gary E. Gilbert. "A membrane-interactive surface on the factor VIII C1 domain cooperates with the C2 domain for cofactor function." Blood 117, no. 11 (March 17, 2011): 3181–89. http://dx.doi.org/10.1182/blood-2010-08-301663.
Повний текст джерелаGrados-Torrez, Ricardo Enrique, Carmen López-Iglesias, Joan Carles Ferrer, and Narciso Campos. "Loose Morphology and High Dynamism of OSER Structures Induced by the Membrane Domain of HMG-CoA Reductase." International Journal of Molecular Sciences 22, no. 17 (August 24, 2021): 9132. http://dx.doi.org/10.3390/ijms22179132.
Повний текст джерелаYoun, Ji-Young, Helena Friesen, Takuma Kishimoto, William M. Henne, Christoph F. Kurat, Wei Ye, Derek F. Ceccarelli, et al. "Dissecting BAR Domain Function in the Yeast Amphiphysins Rvs161 and Rvs167 during Endocytosis." Molecular Biology of the Cell 21, no. 17 (September 2010): 3054–69. http://dx.doi.org/10.1091/mbc.e10-03-0181.
Повний текст джерелаGarcía-Sáez, Ana J., Salvatore Chiantia, and Petra Schwille. "Effect of Line Tension on the Lateral Organization of Lipid Membranes." Journal of Biological Chemistry 282, no. 46 (September 11, 2007): 33537–44. http://dx.doi.org/10.1074/jbc.m706162200.
Повний текст джерелаLin, Sasa, Hussein Y. Naim, A. Chapin Rodriguez, and Michael G. Roth. "Mutations in the Middle of the Transmembrane Domain Reverse the Polarity of Transport of the Influenza Virus Hemagglutinin in MDCK Epithelial Cells." Journal of Cell Biology 142, no. 1 (July 13, 1998): 51–57. http://dx.doi.org/10.1083/jcb.142.1.51.
Повний текст джерелаWhitley, Paul, and Ismael Mingarro. "Stitching proteins into membranes, not sew simple." Biological Chemistry 395, no. 12 (December 1, 2014): 1417–24. http://dx.doi.org/10.1515/hsz-2014-0205.
Повний текст джерелаJohnson, Joanne E., Rebecca E. Goulding, Ziwei Ding, Amir Partovi, Kira V. Anthony, Nadine Beaulieu, Ghazaleh Tazmini, Rosemary B. Cornell, and Robert J. Kay. "Differential membrane binding and diacylglycerol recognition by C1 domains of RasGRPs." Biochemical Journal 406, no. 2 (August 13, 2007): 223–36. http://dx.doi.org/10.1042/bj20070294.
Повний текст джерелаScott, Jordan L., Cary T. Frick, Kristen A. Johnson, Haining Liu, Sylvia S. Yong, Allyson G. Varney, Olaf Wiest, and Robert V. Stahelin. "Molecular Analysis of Membrane Targeting by the C2 Domain of the E3 Ubiquitin Ligase Smurf1." Biomolecules 10, no. 2 (February 4, 2020): 229. http://dx.doi.org/10.3390/biom10020229.
Повний текст джерелаMoreau, A., M. Maurice, and G. Feldmann. "Analysis of hepatocyte plasma membrane domains during rat development using monoclonal antibodies." Journal of Histochemistry & Cytochemistry 36, no. 1 (January 1988): 87–94. http://dx.doi.org/10.1177/36.1.3275714.
Повний текст джерелаAlsop, Richard J., Sebastian Himbert, Alexander Dhaliwal, Karin Schmalzl, and Maikel C. Rheinstädter. "Aspirin locally disrupts the liquid-ordered phase." Royal Society Open Science 5, no. 2 (February 2018): 171710. http://dx.doi.org/10.1098/rsos.171710.
Повний текст джерелаBrône, Bert, and Jan Eggermont. "PDZ proteins retain and regulate membrane transporters in polarized epithelial cell membranes." American Journal of Physiology-Cell Physiology 288, no. 1 (January 2005): C20—C29. http://dx.doi.org/10.1152/ajpcell.00368.2004.
Повний текст джерелаCorbalán-García, S., M. Guerrero-Valero, C. Marín-Vicente, and J. C. Gómez-Fernández. "The C2 domains of classical/conventional PKCs are specific PtdIns(4,5)P2-sensing domains." Biochemical Society Transactions 35, no. 5 (October 25, 2007): 1046–48. http://dx.doi.org/10.1042/bst0351046.
Повний текст джерелаFrisz, Jessica F., Haley A. Klitzing, Kaiyan Lou, Ian D. Hutcheon, Peter K. Weber, Joshua Zimmerberg, and Mary L. Kraft. "Sphingolipid Domains in the Plasma Membranes of Fibroblasts Are Not Enriched with Cholesterol." Journal of Biological Chemistry 288, no. 23 (April 22, 2013): 16855–61. http://dx.doi.org/10.1074/jbc.m113.473207.
Повний текст джерелаSTÖGBAUER, T., M. HENNIG, and J. O. RÄDLER. "ALIGNMENT AND DEFORMATION OF LIPID BILAYER DOMAINS IN VESICLES ADHERING TO MICROSTRUCTURED SUBSTRATES." Biophysical Reviews and Letters 05, no. 03 (September 2010): 153–61. http://dx.doi.org/10.1142/s1793048010001160.
Повний текст джерелаScott, Angela M., Corina E. Antal та Alexandra C. Newton. "Electrostatic and Hydrophobic Interactions Differentially Tune Membrane Binding Kinetics of the C2 Domain of Protein Kinase Cα". Journal of Biological Chemistry 288, № 23 (15 квітня 2013): 16905–15. http://dx.doi.org/10.1074/jbc.m113.467456.
Повний текст джерелаKaykas, Ajamete, Kathleen Worringer, and Bill Sugden. "LMP-1's Transmembrane Domains Encode Multiple Functions Required for LMP-1's Efficient Signaling." Journal of Virology 76, no. 22 (November 15, 2002): 11551–60. http://dx.doi.org/10.1128/jvi.76.22.11551-11560.2002.
Повний текст джерелаLondon, Erwin. "Ordered Domain (Raft) Formation in Asymmetric Vesicles and Its Induction upon Loss of Lipid Asymmetry in Artificial and Natural Membranes." Membranes 12, no. 9 (September 9, 2022): 870. http://dx.doi.org/10.3390/membranes12090870.
Повний текст джерелаOancea, Elena, Mary N. Teruel, Andrew F. G. Quest, and Tobias Meyer. "Green Fluorescent Protein (GFP)-tagged Cysteine-rich Domains from Protein Kinase C as Fluorescent Indicators for Diacylglycerol Signaling in Living Cells." Journal of Cell Biology 140, no. 3 (February 9, 1998): 485–98. http://dx.doi.org/10.1083/jcb.140.3.485.
Повний текст джерелаO’Neil, Patrick K., Lynn G. L. Richardson, Yamuna D. Paila, Grzegorz Piszczek, Srinivas Chakravarthy, Nicholas Noinaj, and Danny Schnell. "The POTRA domains of Toc75 exhibit chaperone-like function to facilitate import into chloroplasts." Proceedings of the National Academy of Sciences 114, no. 24 (May 30, 2017): E4868—E4876. http://dx.doi.org/10.1073/pnas.1621179114.
Повний текст джерелаKumar, Shekhar, Steven Stayrook, James A. Huntington, Rodney M. Camire, and Sriram Krishnaswamy. "New Structural Insights into High Affinity Membrane Binding By Coagulation Factor V/Va." Blood 124, no. 21 (December 6, 2014): 4216. http://dx.doi.org/10.1182/blood.v124.21.4216.4216.
Повний текст джерелаPuchulu-Campanella, Estela, Francesco M. Turrini, Yen-Hsing Li, and Philip S. Low. "Global transformation of erythrocyte properties via engagement of an SH2-like sequence in band 3." Proceedings of the National Academy of Sciences 113, no. 48 (November 15, 2016): 13732–37. http://dx.doi.org/10.1073/pnas.1611904113.
Повний текст джерелаMcKiernan, C. J., P. F. Stabila, and I. G. Macara. "Role of the Rab3A-binding domain in targeting of rabphilin-3A to vesicle membranes of PC12 cells." Molecular and Cellular Biology 16, no. 9 (September 1996): 4985–95. http://dx.doi.org/10.1128/mcb.16.9.4985.
Повний текст джерелаPinigin, Konstantin V., Timur R. Galimzyanov, and Sergey A. Akimov. "Amphipathic Peptides Impede Lipid Domain Fusion in Phase-Separated Membranes." Membranes 11, no. 11 (October 20, 2021): 797. http://dx.doi.org/10.3390/membranes11110797.
Повний текст джерелаUeyama, Takehiko, Toshihiko Tatsuno, Takumi Kawasaki, Satoshi Tsujibe, Yasuhito Shirai, Hideki Sumimoto, Thomas L. Leto, and Naoaki Saito. "A Regulated Adaptor Function of p40phox: Distinct p67phoxMembrane Targeting by p40phoxand by p47phox." Molecular Biology of the Cell 18, no. 2 (February 2007): 441–54. http://dx.doi.org/10.1091/mbc.e06-08-0731.
Повний текст джерелаNagel, Wolfgang, Pierre Schilcher, Lutz Zeitlmann, and Waldemar Kolanus. "The PH Domain and the Polybasic c Domain of Cytohesin-1 Cooperate specifically in Plasma Membrane Association and Cellular Function." Molecular Biology of the Cell 9, no. 8 (August 1998): 1981–94. http://dx.doi.org/10.1091/mbc.9.8.1981.
Повний текст джерелаGill, David J., Hsiangling Teo, Ji Sun, Olga Perisic, Dmitry B. Veprintsev, Yvonne Vallis, Scott D. Emr, and Roger L. Williams. "Structural studies of phosphoinositide 3-kinase-dependent traffic to multivesicular bodies." Biochemical Society Symposia 74 (January 12, 2007): 47–57. http://dx.doi.org/10.1042/bss2007c05.
Повний текст джерелаStanishneva-Konovalova, T. B., N. I. Derkacheva, S. V. Polevova, and O. S. Sokolova. "The Role of BAR Domain Proteins in the Regulation of Membrane Dynamics." Acta Naturae 8, no. 4 (December 15, 2016): 60–69. http://dx.doi.org/10.32607/20758251-2016-8-4-60-69.
Повний текст джерелаHokanson, David E., Joseph M. Laakso, Tianming Lin, David Sept, and E. Michael Ostap. "Myo1c Binds Phosphoinositides through a Putative Pleckstrin Homology Domain." Molecular Biology of the Cell 17, no. 11 (November 2006): 4856–65. http://dx.doi.org/10.1091/mbc.e06-05-0449.
Повний текст джерелаPing, Holly A., Lauren M. Kraft, WeiTing Chen, Amy E. Nilles, and Laura L. Lackner. "Num1 anchors mitochondria to the plasma membrane via two domains with different lipid binding specificities." Journal of Cell Biology 213, no. 5 (May 30, 2016): 513–24. http://dx.doi.org/10.1083/jcb.201511021.
Повний текст джерелаDavis-Harrison, Rebecca L., Narjes Tavoosi, Mary Clay, John M. Boettcher, Chad M. Rienstra, and James H. Morrissey. "Structural Insights Into How Clotting Proteins with GLA Domains Bind to Membrane Surfaces." Blood 116, no. 21 (November 19, 2010): 1141. http://dx.doi.org/10.1182/blood.v116.21.1141.1141.
Повний текст джерелаBecalska, Agata N., Charlotte F. Kelley, Cristina Berciu, Tatiana B. Stanishneva-Konovalova, Xiaofeng Fu, ShiYu Wang, Olga S. Sokolova, Daniela Nicastro, and Avital A. Rodal. "Formation of membrane ridges and scallops by the F-BAR protein Nervous Wreck." Molecular Biology of the Cell 24, no. 15 (August 2013): 2406–18. http://dx.doi.org/10.1091/mbc.e13-05-0271.
Повний текст джерелаMoczko, M., U. Bömer, M. Kübrich, N. Zufall, A. Hönlinger, and N. Pfanner. "The intermembrane space domain of mitochondrial Tom22 functions as a trans binding site for preproteins with N-terminal targeting sequences." Molecular and Cellular Biology 17, no. 11 (November 1997): 6574–84. http://dx.doi.org/10.1128/mcb.17.11.6574.
Повний текст джерелаMolotkovsky, Galimzyanov, Batishchev, and Akimov. "The Effect of Transmembrane Protein Shape on Surrounding Lipid Domain Formation by Wetting." Biomolecules 9, no. 11 (November 12, 2019): 729. http://dx.doi.org/10.3390/biom9110729.
Повний текст джерелаde Almeida, J. B., E. J. Holtzman, P. Peters, L. Ercolani, D. A. Ausiello, and J. L. Stow. "Targeting of chimeric G alpha i proteins to specific membrane domains." Journal of Cell Science 107, no. 3 (March 1, 1994): 507–15. http://dx.doi.org/10.1242/jcs.107.3.507.
Повний текст джерелаLipowsky, Reinhard. "Remodeling of membrane compartments: some consequences of membrane fluidity." Biological Chemistry 395, no. 3 (March 1, 2014): 253–74. http://dx.doi.org/10.1515/hsz-2013-0244.
Повний текст джерелаLi, Guangtao, Qing Wang, Shinako Kakuda, and Erwin London. "Nanodomains can persist at physiologic temperature in plasma membrane vesicles and be modulated by altering cell lipids." Journal of Lipid Research 61, no. 5 (January 21, 2020): 758–66. http://dx.doi.org/10.1194/jlr.ra119000565.
Повний текст джерелаEdidin, M., and I. Stroynowski. "Differences between the lateral organization of conventional and inositol phospholipid-anchored membrane proteins. A further definition of micrometer scale membrane domains." Journal of Cell Biology 112, no. 6 (March 15, 1991): 1143–50. http://dx.doi.org/10.1083/jcb.112.6.1143.
Повний текст джерелаLiao, Maofu, Claudia Sánchez-San Martín, Aihua Zheng, and Margaret Kielian. "In Vitro Reconstitution Reveals Key Intermediate States of Trimer Formation by the Dengue Virus Membrane Fusion Protein." Journal of Virology 84, no. 11 (March 24, 2010): 5730–40. http://dx.doi.org/10.1128/jvi.00170-10.
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