Статті в журналах з теми "Intramolecular signal transduction"
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Papavassiliou, A. G., M. Treier, and D. Bohmann. "Intramolecular signal transduction in c-Jun." EMBO Journal 14, no. 9 (May 1995): 2014–19. http://dx.doi.org/10.1002/j.1460-2075.1995.tb07193.x.
Повний текст джерелаMueller, Sylvia, Claus Liebmann, and Siegmund Reissmann. "Intramolecular signal transduction by the bradykinin B2 receptor." International Immunopharmacology 2, no. 13-14 (December 2002): 1763–70. http://dx.doi.org/10.1016/s1567-5769(02)00167-4.
Повний текст джерелаLee, Yoonji, Sun Choi, and Changbong Hyeon. "Mapping the intramolecular signal transduction of G-protein coupled receptors." Proteins: Structure, Function, and Bioinformatics 82, no. 5 (November 22, 2013): 727–43. http://dx.doi.org/10.1002/prot.24451.
Повний текст джерелаBasith, Shaherin, Balachandran Manavalan, Tae Shin та Gwang Lee. "A Molecular Dynamics Approach to Explore the Intramolecular Signal Transduction of PPAR-α". International Journal of Molecular Sciences 20, № 7 (3 квітня 2019): 1666. http://dx.doi.org/10.3390/ijms20071666.
Повний текст джерелаCalderwood, S. K., Y. Wang, X. Xie, M. A. Khaleque, S. D. Chou, A. Murshid, T. Prince, and Y. Zhang. "Signal Transduction Pathways Leading to Heat Shock Transcription." Signal Transduction Insights 2 (January 2010): STI.S3994. http://dx.doi.org/10.4137/sti.s3994.
Повний текст джерелаRohmer, Thierry, Holger Strauss, Jon Hughes, Huub de Groot, Wolfgang Gärtner, Peter Schmieder, and Jörg Matysik. "15N MAS NMR Studies of Cph1 Phytochrome: Chromophore Dynamics and Intramolecular Signal Transduction." Journal of Physical Chemistry B 110, no. 41 (October 2006): 20580–85. http://dx.doi.org/10.1021/jp062454+.
Повний текст джерелаWeng, Tan-Qing, Yi-Fan Huang, Lou-Sha Xue, Jie Cheng, Shan Jin, Sheng-Hua Liu, De-Yin Wu, and George Chen. "Anion-Binding-Induced Electrochemical Signal Transduction in Ferrocenylimidazolium: Combined Electrochemical Experimental and Theoretical Investigation." Molecules 24, no. 2 (January 10, 2019): 238. http://dx.doi.org/10.3390/molecules24020238.
Повний текст джерелаNeumann, Susanne, Maren Claus, and Ralf Paschke. "Interactions between the extracellular domain and the extracellular loops as well as the 6th transmembrane domain are necessary for TSH receptor activation." European Journal of Endocrinology 152, no. 4 (April 2005): 625–34. http://dx.doi.org/10.1530/eje.1.01891.
Повний текст джерелаRöhrig, Ute F., Leonardo Guidoni, and Ursula Rothlisberger. "Early Steps of the Intramolecular Signal Transduction in Rhodopsin Explored by Molecular Dynamics Simulations†." Biochemistry 41, no. 35 (September 2002): 10799–809. http://dx.doi.org/10.1021/bi026011h.
Повний текст джерелаBasith, Shaherin, Balachandran Manavalan, Tae Hwan Shin, and Gwang Lee. "Mapping the Intramolecular Communications among Different Glutamate Dehydrogenase States Using Molecular Dynamics." Biomolecules 11, no. 6 (May 27, 2021): 798. http://dx.doi.org/10.3390/biom11060798.
Повний текст джерелаAscano, Manuel, and David J. Robbins. "An Intramolecular Association between Two Domains of the Protein Kinase Fused Is Necessary for Hedgehog Signaling." Molecular and Cellular Biology 24, no. 23 (December 1, 2004): 10397–405. http://dx.doi.org/10.1128/mcb.24.23.10397-10405.2004.
Повний текст джерелаVedamalai, Mani, Dhaval Kedaria, Rajesh Vasita, Shigeki Mori, and Iti Gupta. "Design and synthesis of BODIPY-clickate based Hg2+ sensors: the effect of triazole binding mode with Hg2+ on signal transduction." Dalton Transactions 45, no. 6 (2016): 2700–2708. http://dx.doi.org/10.1039/c5dt04042f.
Повний текст джерелаHamidi, Sepehr, Chun-Rong Chen, Yumiko Mizutori-Sasai, Sandra M. McLachlan, and Basil Rapoport. "Relationship between Thyrotropin Receptor Hinge Region Proteolytic Posttranslational Modification and Receptor Physiological Function." Molecular Endocrinology 25, no. 1 (January 1, 2011): 184–94. http://dx.doi.org/10.1210/me.2010-0401.
Повний текст джерелаWang, Mingxing, Qiong Guo, Kongfu Zhu, Bo Fang, Yifan Yang, Maikun Teng, Xu Li, and Yuyong Tao. "Interface switch mediates signal transmission in a two-component system." Proceedings of the National Academy of Sciences 117, no. 48 (November 16, 2020): 30433–40. http://dx.doi.org/10.1073/pnas.1912080117.
Повний текст джерелаMa, Cheng-Wei, Zhi-Long Xiu, and An-Ping Zeng. "Discovery of Intramolecular Signal Transduction Network Based on a New Protein Dynamics Model of Energy Dissipation." PLoS ONE 7, no. 2 (February 20, 2012): e31529. http://dx.doi.org/10.1371/journal.pone.0031529.
Повний текст джерелаJaggi, R. "The two opposing activities of adenylyl transferase reside in distinct homologous domains, with intramolecular signal transduction." EMBO Journal 16, no. 18 (September 15, 1997): 5562–71. http://dx.doi.org/10.1093/emboj/16.18.5562.
Повний текст джерелаHanique, Sophie, Maria-Luigi Colombo, Erik Goormaghtigh, Patrice Soumillion, Jean-Marie Frère, and Bernard Joris. "Evidence of an Intramolecular Interaction between the Two Domains of the BlaR1 Penicillin Receptor during the Signal Transduction." Journal of Biological Chemistry 279, no. 14 (January 21, 2004): 14264–72. http://dx.doi.org/10.1074/jbc.m313488200.
Повний текст джерелаRe, Sandra Da, Stéphane Bertagnoli, Joëlle Fourment, Jean-Marc Reyrat, and Daniel Kahn. "Intramolecular signal transduction within the FixJ transcriptional activator:in vitroevidence for the inhibitory effect of the phosphorylatable regulatory domain." Nucleic Acids Research 22, no. 9 (1994): 1555–61. http://dx.doi.org/10.1093/nar/22.9.1555.
Повний текст джерелаSchulam, P. G., and W. T. Shearer. "Evidence for 5-lipoxygenase activity in human B cell lines. A possible role for arachidonic acid metabolites during B cell signal transduction." Journal of Immunology 144, no. 7 (April 1, 1990): 2696–701. http://dx.doi.org/10.4049/jimmunol.144.7.2696.
Повний текст джерелаYamashita, Takahiro, Masataka Yanagawa, and Yoshinori Shichida. "2P342 Intramolecular signal transduction through helices II and IV of metabotropic glutamate receptor(Photobiology-vision and photoreception,Oral Presentations)." Seibutsu Butsuri 47, supplement (2007): S198. http://dx.doi.org/10.2142/biophys.47.s198_3.
Повний текст джерелаElliott, Kathryn T., Igor B. Zhulin, Jeanne A. Stuckey, and Victor J. DiRita. "Conserved Residues in the HAMP Domain Define a New Family of Proposed Bipartite Energy Taxis Receptors." Journal of Bacteriology 191, no. 1 (October 24, 2008): 375–87. http://dx.doi.org/10.1128/jb.00578-08.
Повний текст джерелаWANG, Zhi-Xin, and Jia-Wei WU. "Autophosphorylation kinetics of protein kinases." Biochemical Journal 368, no. 3 (December 15, 2002): 947–52. http://dx.doi.org/10.1042/bj20020557.
Повний текст джерелаLang, Michael J., Bethany S. Strunk, Nadia Azad, Jason L. Petersen, and Lois S. Weisman. "An intramolecular interaction within the lipid kinase Fab1 regulates cellular phosphatidylinositol 3,5-bisphosphate lipid levels." Molecular Biology of the Cell 28, no. 7 (April 2017): 858–64. http://dx.doi.org/10.1091/mbc.e16-06-0390.
Повний текст джерелаKazemein Jasemi, Neda S., Christian Herrmann, Eva Magdalena Estirado, Lothar Gremer, Dieter Willbold, Luc Brunsveld, Radovan Dvorsky, and Mohammad R. Ahmadian. "The intramolecular allostery of GRB2 governing its interaction with SOS1 is modulated by phosphotyrosine ligands." Biochemical Journal 478, no. 14 (July 23, 2021): 2793–809. http://dx.doi.org/10.1042/bcj20210105.
Повний текст джерелаOishi, Koichiro, Mayu Nagamori, Yasuhiro Kashino, Hiroshi Sekiguchi, Yuji C. Sasaki, Atsuo Miyazawa, and Yuri Nishino. "Ligand-Dependent Intramolecular Motion of Native Nicotinic Acetylcholine Receptors Determined in Living Myotube Cells via Diffracted X-ray Tracking." International Journal of Molecular Sciences 24, no. 15 (July 28, 2023): 12069. http://dx.doi.org/10.3390/ijms241512069.
Повний текст джерелаSasidharan, Santanu, Kamalakannan Radhakrishnan, Jun-Yeong Lee, Prakash Saudagar, Vijayakumar Gosu та Donghyun Shin. "Molecular dynamics of the ERRγ ligand-binding domain bound with agonist and inverse agonist". PLOS ONE 18, № 4 (6 квітня 2023): e0283364. http://dx.doi.org/10.1371/journal.pone.0283364.
Повний текст джерелаJi, Inhae, ChangWoo Lee, YongSang Song, P. Michael Conn, and Tae H. Ji. "Cis- and Trans-Activation of Hormone Receptors: the LH Receptor." Molecular Endocrinology 16, no. 6 (June 1, 2002): 1299–308. http://dx.doi.org/10.1210/mend.16.6.0852.
Повний текст джерелаHu, Zhongjun, Dianne W. Taylor, Michael K. Reedy, Robert J. Edwards, and Kenneth A. Taylor. "Structure of myosin filaments from relaxed Lethocerus flight muscle by cryo-EM at 6 Å resolution." Science Advances 2, no. 9 (September 2016): e1600058. http://dx.doi.org/10.1126/sciadv.1600058.
Повний текст джерелаZhurinsky, J., M. Shtutman, and A. Ben-Ze'ev. "Plakoglobin and beta-catenin: protein interactions, regulation and biological roles." Journal of Cell Science 113, no. 18 (September 15, 2000): 3127–39. http://dx.doi.org/10.1242/jcs.113.18.3127.
Повний текст джерелаSadeghi, Maryam, Jens Balke, Timm Rafaluk-Mohr, and Ulrike Alexiev. "Long-Distance Protonation-Conformation Coupling in Phytochrome Species." Molecules 27, no. 23 (December 1, 2022): 8395. http://dx.doi.org/10.3390/molecules27238395.
Повний текст джерелаResh, Marilyn D. "Open Biology: overview for special issue on dynamics of protein fatty acylation." Open Biology 11, no. 9 (September 2021): 210228. http://dx.doi.org/10.1098/rsob.210228.
Повний текст джерелаNichols, James T., Alison Miyamoto, Samantha L. Olsen, Brendan D'Souza, Christine Yao, and Gerry Weinmaster. "DSL ligand endocytosis physically dissociates Notch1 heterodimers before activating proteolysis can occur." Journal of Cell Biology 176, no. 4 (February 12, 2007): 445–58. http://dx.doi.org/10.1083/jcb.200609014.
Повний текст джерелаNagy, Szilvia K., Zsuzsanna Darula, Brigitta M. Kállai, László Bögre, Gábor Bánhegyi, Katalin F. Medzihradszky, Gábor V. Horváth, and Tamás Mészáros. "Activation of AtMPK9 through autophosphorylation that makes it independent of the canonical MAPK cascades." Biochemical Journal 467, no. 1 (March 20, 2015): 167–75. http://dx.doi.org/10.1042/bj20141176.
Повний текст джерелаStamperna, Konstantina, Themistoklis Giannoulis, Eleni Dovolou, Maria Kalemkeridou, Ioannis Nanas, Katerina Dadouli, Katerina Moutou, Zissis Mamuris, and Georgios S. Amiridis. "Heat Shock Protein 70 Improves In Vitro Embryo Yield and Quality from Heat Stressed Bovine Oocytes." Animals 11, no. 6 (June 16, 2021): 1794. http://dx.doi.org/10.3390/ani11061794.
Повний текст джерелаToutant, Madeleine, Alicia Costa, Jeanne-Marie Studler, Gress Kadaré, Michèle Carnaud, and Jean-Antoine Girault. "Alternative Splicing Controls the Mechanisms of FAK Autophosphorylation." Molecular and Cellular Biology 22, no. 22 (November 15, 2002): 7731–43. http://dx.doi.org/10.1128/mcb.22.22.7731-7743.2002.
Повний текст джерелаChin, Arnold I.-Dah, Junyan Shu, Chong Shan Shi, Zhengbin Yao, John H. Kehrl, and Genhong Cheng. "TANK Potentiates Tumor Necrosis Factor Receptor-Associated Factor-Mediated c-Jun N-Terminal Kinase/Stress-Activated Protein Kinase Activation through the Germinal Center Kinase Pathway." Molecular and Cellular Biology 19, no. 10 (October 1, 1999): 6665–72. http://dx.doi.org/10.1128/mcb.19.10.6665.
Повний текст джерелаPasquale, E. B. "Identification of chicken embryo kinase 5, a developmentally regulated receptor-type tyrosine kinase of the Eph family." Cell Regulation 2, no. 7 (July 1991): 523–34. http://dx.doi.org/10.1091/mbc.2.7.523.
Повний текст джерелаGottardi, Cara J., та Barry M. Gumbiner. "Distinct molecular forms of β-catenin are targeted to adhesive or transcriptional complexes". Journal of Cell Biology 167, № 2 (18 жовтня 2004): 339–49. http://dx.doi.org/10.1083/jcb.200402153.
Повний текст джерелаAdolph, Dörte, Nadine Flach, Katharina Mueller, Dirk H. Ostareck, and Antje Ostareck-Lederer. "Deciphering the Cross Talk between hnRNP K and c-Src: the c-Src Activation Domain in hnRNP K Is Distinct from a Second Interaction Site." Molecular and Cellular Biology 27, no. 5 (December 18, 2006): 1758–70. http://dx.doi.org/10.1128/mcb.02014-06.
Повний текст джерелаLehtonen, Siri T., Piia M. H. Markkanen, Mirva Peltoniemi, Sang Won Kang, and Vuokko L. Kinnula. "Variable overoxidation of peroxiredoxins in human lung cells in severe oxidative stress." American Journal of Physiology-Lung Cellular and Molecular Physiology 288, no. 5 (May 2005): L997—L1001. http://dx.doi.org/10.1152/ajplung.00432.2004.
Повний текст джерелаDumont, Mark E., та James B. Konopka. "Comparison of Experimental Approaches Used to Determine the Structure and Function of the Class D G Protein-Coupled Yeast α-Factor Receptor". Biomolecules 12, № 6 (30 травня 2022): 761. http://dx.doi.org/10.3390/biom12060761.
Повний текст джерелаWilliams, Danielle M., David C. Thorn, Christopher M. Dobson, Sarah Meehan, Sophie E. Jackson, Joanna M. Woodcock та John A. Carver. "The Amyloid Fibril-Forming β-Sheet Regions of Amyloid β and α-Synuclein Preferentially Interact with the Molecular Chaperone 14-3-3ζ". Molecules 26, № 20 (11 жовтня 2021): 6120. http://dx.doi.org/10.3390/molecules26206120.
Повний текст джерелаMartín-Moldes, Zaira, Blas Blázquez, Claudine Baraquet, Caroline S. Harwood, María T. Zamarro, and Eduardo Díaz. "Degradation of cyclic diguanosine monophosphate by a hybrid two-component protein protects Azoarcus sp. strain CIB from toluene toxicity." Proceedings of the National Academy of Sciences 113, no. 46 (October 31, 2016): 13174–79. http://dx.doi.org/10.1073/pnas.1615981113.
Повний текст джерелаBauer, Carl, Sylvie Elsen, Lee R. Swem, Danielle L. Swem, and Shinji Masuda. "Redox and light regulation of gene expression in photosynthetic prokaryotes." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 358, no. 1429 (January 29, 2003): 147–54. http://dx.doi.org/10.1098/rstb.2002.1189.
Повний текст джерелаHuang, Jun, and Dibyendu K. Sasmal. "TCR-pMHC bond length controls TCR ligand discrimination." Journal of Immunology 202, no. 1_Supplement (May 1, 2019): 184.10. http://dx.doi.org/10.4049/jimmunol.202.supp.184.10.
Повний текст джерелаBender, Kyle W., Raymond E. Zielinski, and Steven C. Huber. "Revisiting paradigms of Ca2+ signaling protein kinase regulation in plants." Biochemical Journal 475, no. 1 (January 5, 2018): 207–23. http://dx.doi.org/10.1042/bcj20170022.
Повний текст джерелаCheng, Haiyun, Jim A. Rogers, Nancy A. Dunham, and Thomas E. Smithgall. "Regulation of c-Fes Tyrosine Kinase and Biological Activities by N-Terminal Coiled-Coil Oligomerization Domains." Molecular and Cellular Biology 19, no. 12 (December 1, 1999): 8335–43. http://dx.doi.org/10.1128/mcb.19.12.8335.
Повний текст джерелаHaruta, T., T. Sawa, Y. Takata, T. Imamura, Y. Takada, H. Morioka, G. H. Yang та M. Kobayashi. "An extracellular domain of the β subunit is essential for processing, transport and kinase activity of insulin receptor". Biochemical Journal 305, № 2 (15 січня 1995): 599–604. http://dx.doi.org/10.1042/bj3050599.
Повний текст джерелаZhang, Yan-Liang, John A. Frangos, and Mirianas Chachisvilis. "Mechanical stimulus alters conformation of type 1 parathyroid hormone receptor in bone cells." American Journal of Physiology-Cell Physiology 296, no. 6 (June 2009): C1391—C1399. http://dx.doi.org/10.1152/ajpcell.00549.2008.
Повний текст джерелаLee, Seung-Yub, Fubo Liang, Xiao-Ling Guo, Laiping Xie, Sean M. Cahill, Michael Blumenstein, Heyi Yang, David S. Lawrence, and Zhong-Yin Zhang. "Design, Construction, and Intracellular Activation of an Intramolecularly Self-Silenced Signal Transduction Inhibitor." Angewandte Chemie International Edition 44, no. 27 (July 4, 2005): 4242–44. http://dx.doi.org/10.1002/anie.200462004.
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