Статті в журналах з теми "Per Arnt Sim (PAS)"
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Hirose, K., M. Morita, M. Ema, J. Mimura, H. Hamada, H. Fujii, Y. Saijo, O. Gotoh, K. Sogawa, and Y. Fujii-Kuriyama. "cDNA cloning and tissue-specific expression of a novel basic helix-loop-helix/PAS factor (Arnt2) with close sequence similarity to the aryl hydrocarbon receptor nuclear translocator (Arnt)." Molecular and Cellular Biology 16, no. 4 (April 1996): 1706–13. http://dx.doi.org/10.1128/mcb.16.4.1706.
Повний текст джерелаYang, Jinsong, Lei Zhang, Paul J. A. Erbel, Kevin H. Gardner, Kan Ding, Joseph A. Garcia, and Richard K. Bruick. "Functions of the Per/ARNT/Sim Domains of the Hypoxia-inducible Factor." Journal of Biological Chemistry 280, no. 43 (August 29, 2005): 36047–54. http://dx.doi.org/10.1074/jbc.m501755200.
Повний текст джерелаde Souza, João V., Sylvia Reznikov, Ruidi Zhu, and Agnieszka K. Bronowska. "Druggability assessment of mammalian Per–Arnt–Sim [PAS] domains using computational approaches." MedChemComm 10, no. 7 (2019): 1126–37. http://dx.doi.org/10.1039/c9md00148d.
Повний текст джерелаMoffett, P., M. Reece, and J. Pelletier. "The murine Sim-2 gene product inhibits transcription by active repression and functional interference." Molecular and Cellular Biology 17, no. 9 (September 1997): 4933–47. http://dx.doi.org/10.1128/mcb.17.9.4933.
Повний текст джерелаReisz-Porszasz, S., M. R. Probst, B. N. Fukunaga, and O. Hankinson. "Identification of functional domains of the aryl hydrocarbon receptor nuclear translocator protein (ARNT)." Molecular and Cellular Biology 14, no. 9 (September 1994): 6075–86. http://dx.doi.org/10.1128/mcb.14.9.6075-6086.1994.
Повний текст джерелаReisz-Porszasz, S., M. R. Probst, B. N. Fukunaga, and O. Hankinson. "Identification of functional domains of the aryl hydrocarbon receptor nuclear translocator protein (ARNT)." Molecular and Cellular Biology 14, no. 9 (September 1994): 6075–86. http://dx.doi.org/10.1128/mcb.14.9.6075.
Повний текст джерелаWang, Feng, Shengli Shi, Ruixue Zhang, and Oliver Hankinson. "Identifying target genes of the aryl hydrocarbon receptor nuclear translocator (Arnt) using DNA microarray analysis." Biological Chemistry 387, no. 9 (September 1, 2006): 1215–18. http://dx.doi.org/10.1515/bc.2006.150.
Повний текст джерелаPongratz, Ingemar, Camilla Antonsson, Murray L. Whitelaw, and Lorenz Poellinger. "Role of the PAS Domain in Regulation of Dimerization and DNA Binding Specificity of the Dioxin Receptor." Molecular and Cellular Biology 18, no. 7 (July 1, 1998): 4079–88. http://dx.doi.org/10.1128/mcb.18.7.4079.
Повний текст джерелаZhao, J. M., H. Lee, R. A. Nome, S. Majid, N. F. Scherer, and W. D. Hoff. "Single-molecule detection of structural changes during Per-Arnt-Sim (PAS) domain activation." Proceedings of the National Academy of Sciences 103, no. 31 (July 19, 2006): 11561–66. http://dx.doi.org/10.1073/pnas.0601567103.
Повний текст джерелаMacDonald, P. E., and P. Rorsman. "Per-arnt-sim (PAS) domain kinase (PASK) as a regulator of glucagon secretion." Diabetologia 54, no. 4 (February 17, 2011): 719–21. http://dx.doi.org/10.1007/s00125-011-2072-1.
Повний текст джерелаAdaixo, Ricardo, and João Henrique Morais-Cabral. "Crystallization and preliminary crystallographic characterization of the PAS domains of EAG and ELK potassium channels." Acta Crystallographica Section F Structural Biology and Crystallization Communications 66, no. 9 (August 26, 2010): 1056–59. http://dx.doi.org/10.1107/s1744309110027880.
Повний текст джерелаPhilip, A. F., M. Kumauchi, and W. D. Hoff. "Robustness and evolvability in the functional anatomy of a PER-ARNT-SIM (PAS) domain." Proceedings of the National Academy of Sciences 107, no. 42 (October 1, 2010): 17986–91. http://dx.doi.org/10.1073/pnas.1004823107.
Повний текст джерелаde Souza, João Victor, Piotr Zaborniak, Sylvia Reznikov, Matthew Kondal, Ruidi Zhu, and Agnieszka K. Bronowska. "Molecular Forces Governing the Biological Function of Per-Arnt-Sim-B (PAS-B) Domains: A Comparative Computational Study." Biophysica 1, no. 1 (February 5, 2021): 1–14. http://dx.doi.org/10.3390/biophysica1010001.
Повний текст джерелаXu, Xingjian, Igor Dikiy, Matthew R. Evans, Leandro P. Marcelino, and Kevin H. Gardner. "Fragile protein folds: sequence and environmental factors affecting the equilibrium of two interconverting, stably folded protein conformations." Magnetic Resonance 2, no. 1 (March 10, 2021): 63–76. http://dx.doi.org/10.5194/mr-2-63-2021.
Повний текст джерелаGradin, K., J. McGuire, R. H. Wenger, I. Kvietikova, M. L. fhitelaw, R. Toftgård, L. Tora, M. Gassmann, and L. Poellinger. "Functional interference between hypoxia and dioxin signal transduction pathways: competition for recruitment of the Arnt transcription factor." Molecular and Cellular Biology 16, no. 10 (October 1996): 5221–31. http://dx.doi.org/10.1128/mcb.16.10.5221.
Повний текст джерелаAitola, Marjo, Christine M. Sadek, Jan-Åke Gustafsson, and Markku Pelto-Huikko. "Aint/Tacc3 Is Highly Expressed in Proliferating Mouse Tissues During Development, Spermatogenesis, and Oogenesis." Journal of Histochemistry & Cytochemistry 51, no. 4 (April 2003): 455–69. http://dx.doi.org/10.1177/002215540305100407.
Повний текст джерелаSeok, Seung-Hyeon, Woojong Lee, Li Jiang, Kaivalya Molugu, Aiping Zheng, Yitong Li, Sanghyun Park, Christopher A. Bradfield, and Yongna Xing. "Structural hierarchy controlling dimerization and target DNA recognition in the AHR transcriptional complex." Proceedings of the National Academy of Sciences 114, no. 21 (April 10, 2017): 5431–36. http://dx.doi.org/10.1073/pnas.1617035114.
Повний текст джерелаAntonsson, C., M. L. Whitelaw, J. McGuire, J. A. Gustafsson, and L. Poellinger. "Distinct roles of the molecular chaperone hsp90 in modulating dioxin receptor function via the basic helix-loop-helix and PAS domains." Molecular and Cellular Biology 15, no. 2 (February 1995): 756–65. http://dx.doi.org/10.1128/mcb.15.2.756.
Повний текст джерелаSemplici, Francesca, Martine Vaxillaire, Sarah Fogarty, Meriem Semache, Amélie Bonnefond, Ghislaine Fontés, Julien Philippe, et al. "Human Mutation within Per-Arnt-Sim (PAS) Domain-containing Protein Kinase (PASK) Causes Basal Insulin Hypersecretion." Journal of Biological Chemistry 286, no. 51 (November 7, 2011): 44005–14. http://dx.doi.org/10.1074/jbc.m111.254995.
Повний текст джерелаChapman-Smith, Anne, Jodi K. Lutwyche, and Murray L. Whitelaw. "Contribution of the Per/Arnt/Sim (PAS) Domains to DNA Binding by the Basic Helix-Loop-Helix PAS Transcriptional Regulators." Journal of Biological Chemistry 279, no. 7 (November 24, 2003): 5353–62. http://dx.doi.org/10.1074/jbc.m310041200.
Повний текст джерелаDardente, Hugues, Erin E. Fortier, Vincent Martineau, and Nicolas Cermakian. "Cryptochromes impair phosphorylation of transcriptional activators in the clock: a general mechanism for circadian repression." Biochemical Journal 402, no. 3 (February 26, 2007): 525–36. http://dx.doi.org/10.1042/bj20060827.
Повний текст джерелаBrody, Stuart. "A Comparison of the Neurospora and Drosophila Clocks." Journal of Biological Rhythms 35, no. 2 (December 26, 2019): 119–33. http://dx.doi.org/10.1177/0748730419892434.
Повний текст джерелаBersten, David C., John B. Bruning, Daniel J. Peet, and Murray L. Whitelaw. "Human Variants in the Neuronal Basic Helix-Loop-Helix/Per-Arnt-Sim (bHLH/PAS) Transcription Factor Complex NPAS4/ARNT2 Disrupt Function." PLoS ONE 9, no. 1 (January 17, 2014): e85768. http://dx.doi.org/10.1371/journal.pone.0085768.
Повний текст джерелаYun, Jaesuk, Taku Nagai, Yoko Furukawa-Hibi, Keisuke Kuroda, Kozo Kaibuchi, Michael E. Greenberg, and Kiyofumi Yamada. "Neuronal Per Arnt Sim (PAS) Domain Protein 4 (NPAS4) Regulates Neurite Outgrowth and Phosphorylation of Synapsin I." Journal of Biological Chemistry 288, no. 4 (November 21, 2012): 2655–64. http://dx.doi.org/10.1074/jbc.m112.413310.
Повний текст джерелаCoban, Mathew A., Patrick R. Blackburn, Murray L. Whitelaw, Mieke M. van Haelst, Paldeep S. Atwal, and Thomas R. Caulfield. "Structural Models for the Dynamic Effects of Loss-of-Function Variants in the Human SIM1 Protein Transcriptional Activation Domain." Biomolecules 10, no. 9 (September 12, 2020): 1314. http://dx.doi.org/10.3390/biom10091314.
Повний текст джерелаBeischlag, Timothy V., Song Wang, David W. Rose, Joseph Torchia, Suzanne Reisz-Porszasz, Khurshid Muhammad, Walter E. Nelson, Markus R. Probst, Michael G. Rosenfeld, and Oliver Hankinson. "Recruitment of the NCoA/SRC-1/p160 Family of Transcriptional Coactivators by the Aryl Hydrocarbon Receptor/Aryl Hydrocarbon Receptor Nuclear Translocator Complex." Molecular and Cellular Biology 22, no. 12 (June 15, 2002): 4319–33. http://dx.doi.org/10.1128/mcb.22.12.4319-4333.2002.
Повний текст джерелаYamashita, Toshiharu, Osamu Ohneda, Masumi Nagano, Motoyuki Iemitsu, Yuichi Makino, Hirotoshi Tanaka, Takashi Miyauchi, et al. "Abnormal Heart Development and Lung Remodeling in Mice Lacking the Hypoxia-Inducible Factor-Related Basic Helix-Loop-Helix PAS Protein NEPAS." Molecular and Cellular Biology 28, no. 4 (December 10, 2007): 1285–97. http://dx.doi.org/10.1128/mcb.01332-07.
Повний текст джерелаLiu, Yu C., Mayra A. Machuca, Simone A. Beckham, Menachem J. Gunzburg, and Anna Roujeinikova. "Structural basis for amino-acid recognition and transmembrane signalling by tandem Per–Arnt–Sim (tandem PAS) chemoreceptor sensory domains." Acta Crystallographica Section D Biological Crystallography 71, no. 10 (September 30, 2015): 2127–36. http://dx.doi.org/10.1107/s139900471501384x.
Повний текст джерелаTang, Xue, Juan Shao, and Xiaohong Qin. "Crystal structure of the PAS domain of the hEAG potassium channel." Acta Crystallographica Section F Structural Biology Communications 72, no. 8 (July 13, 2016): 578–85. http://dx.doi.org/10.1107/s2053230x16009419.
Повний текст джерелаAn, R., G. da Silva Xavier, H. X. Hao, F. Semplici, J. Rutter та G. A. Rutter. "Regulation by Per-Arnt-Sim (PAS) kinase of pancreatic duodenal homeobox-1 nuclear import in pancreatic β-cells". Biochemical Society Transactions 34, № 5 (1 жовтня 2006): 791–93. http://dx.doi.org/10.1042/bst0340791.
Повний текст джерелаGilles-Gonzalez, Marie-Alda, and Gonzalo Gonzalez. "Signal transduction by heme-containing PAS-domain proteins." Journal of Applied Physiology 96, no. 2 (February 2004): 774–83. http://dx.doi.org/10.1152/japplphysiol.00941.2003.
Повний текст джерелаMiliti, Stefania, Elizabeth S. Maywood, Colby R. Sandate, Johanna E. Chesham, Alun R. Barnard, Michael J. Parsons, Jennifer L. Vibert, et al. "Early doors (Edo) mutant mouse reveals the importance of period 2 (PER2) PAS domain structure for circadian pacemaking." Proceedings of the National Academy of Sciences 113, no. 10 (February 22, 2016): 2756–61. http://dx.doi.org/10.1073/pnas.1517549113.
Повний текст джерелаKolonko, Marta, and Beata Greb-Markiewicz. "bHLH–PAS Proteins: Their Structure and Intrinsic Disorder." International Journal of Molecular Sciences 20, no. 15 (July 26, 2019): 3653. http://dx.doi.org/10.3390/ijms20153653.
Повний текст джерелаDeMille, Desiree, Benjamin T. Bikman, Andrew D. Mathis, John T. Prince, Jordan T. Mackay, Steven W. Sowa, Tacie D. Hall, and Julianne H. Grose. "A comprehensive protein–protein interactome for yeast PAS kinase 1 reveals direct inhibition of respiration through the phosphorylation of Cbf1." Molecular Biology of the Cell 25, no. 14 (July 15, 2014): 2199–215. http://dx.doi.org/10.1091/mbc.e13-10-0631.
Повний текст джерелаChen, Jun, Anrou Zou, Igor Splawski, Mark T. Keating, and Michael C. Sanguinetti. "Long QT Syndrome-associated Mutations in the Per-Arnt-Sim (PAS) Domain of HERG Potassium Channels Accelerate Channel Deactivation." Journal of Biological Chemistry 274, no. 15 (April 9, 1999): 10113–18. http://dx.doi.org/10.1074/jbc.274.15.10113.
Повний текст джерелаKe, Ying, Chai Ann Ng, Mark J. Hunter, Stefan A. Mann, Juliane Heide, Adam P. Hill, and Jamie I. Vandenberg. "Trafficking defects in PAS domain mutant Kv11.1 channels: roles of reduced domain stability and altered domain–domain interactions." Biochemical Journal 454, no. 1 (July 26, 2013): 69–77. http://dx.doi.org/10.1042/bj20130328.
Повний текст джерелаHarley, Carol A., Greg Starek, David K. Jones, Andreia S. Fernandes, Gail A. Robertson, and João H. Morais-Cabral. "Enhancement of hERG channel activity by scFv antibody fragments targeted to the PAS domain." Proceedings of the National Academy of Sciences 113, no. 35 (August 11, 2016): 9916–21. http://dx.doi.org/10.1073/pnas.1601116113.
Повний текст джерелаPape, Jenny, Colleen Newey, Haley Burrell, Audrey Workman, Katelyn Perry, Benjamin Bikman, Laura Bridgewater, and Julianne Grose. "Per-Arnt-Sim Kinase (PASK) Deficiency Increases Cellular Respiration on a Standard Diet and Decreases Liver Triglyceride Accumulation on a Western High-Fat High-Sugar Diet." Nutrients 10, no. 12 (December 15, 2018): 1990. http://dx.doi.org/10.3390/nu10121990.
Повний текст джерелаSoshilov, Anatoly A., Stefano Motta, Laura Bonati, and Michael S. Denison. "Transitional States in Ligand-Dependent Transformation of the Aryl Hydrocarbon Receptor into Its DNA-Binding Form." International Journal of Molecular Sciences 21, no. 7 (April 2, 2020): 2474. http://dx.doi.org/10.3390/ijms21072474.
Повний текст джерелаKolonko-Adamska, Marta, Vladimir N. Uversky, and Beata Greb-Markiewicz. "The Participation of the Intrinsically Disordered Regions of the bHLH-PAS Transcription Factors in Disease Development." International Journal of Molecular Sciences 22, no. 6 (March 11, 2021): 2868. http://dx.doi.org/10.3390/ijms22062868.
Повний текст джерелаBurton, Mark J., Joel Cresser-Brown, Morgan Thomas, Nicola Portolano, Jaswir Basran, Samuel L. Freeman, Hanna Kwon, et al. "Discovery of a heme-binding domain in a neuronal voltage-gated potassium channel." Journal of Biological Chemistry 295, no. 38 (July 28, 2020): 13277–86. http://dx.doi.org/10.1074/jbc.ra120.014150.
Повний текст джерелаKe, Ying, Mark J. Hunter, Chai Ann Ng, Matthew D. Perry, and Jamie I. Vandenberg. "Role of the Cytoplasmic N-terminal Cap and Per-Arnt-Sim (PAS) Domain in Trafficking and Stabilization of Kv11.1 Channels." Journal of Biological Chemistry 289, no. 20 (April 2, 2014): 13782–91. http://dx.doi.org/10.1074/jbc.m113.531277.
Повний текст джерелаWang, Ze-Jun, Stephanie M. Soohoo, Purushottam B. Tiwari, Grzegorz Piszczek, and Tinatin I. Brelidze. "Chlorpromazine binding to the PAS domains uncovers the effect of ligand modulation on EAG channel activity." Journal of Biological Chemistry 295, no. 13 (February 11, 2020): 4114–23. http://dx.doi.org/10.1074/jbc.ra119.012377.
Повний текст джерелаda Silva Xavier, G., J. Rutter, and G. A. Rutter. "Involvement of Per-Arnt-Sim (PAS) kinase in the stimulation of preproinsulin and pancreatic duodenum homeobox 1 gene expression by glucose." Proceedings of the National Academy of Sciences 101, no. 22 (May 17, 2004): 8319–24. http://dx.doi.org/10.1073/pnas.0307737101.
Повний текст джерелаda Silva Xavier, G., H. Farhan, H. Kim, S. Caxaria, P. Johnson, S. Hughes, M. Bugliani, et al. "Per-arnt-sim (PAS) domain-containing protein kinase is downregulated in human islets in type 2 diabetes and regulates glucagon secretion." Diabetologia 54, no. 4 (December 23, 2010): 819–27. http://dx.doi.org/10.1007/s00125-010-2010-7.
Повний текст джерелаHeintz, Udo, Anton Meinhart, and Andreas Winkler. "Multi-PAS domain-mediated protein oligomerization of PpsR fromRhodobacter sphaeroides." Acta Crystallographica Section D Biological Crystallography 70, no. 3 (February 27, 2014): 863–76. http://dx.doi.org/10.1107/s1399004713033634.
Повний текст джерелаTorii, Satoru, Shuya Kasai, Tatsushi Yoshida, Ken-ichi Yasumoto, and Shigeomi Shimizu. "Mitochondrial E3 Ubiquitin Ligase Parkin: Relationships with Other Causal Proteins in Familial Parkinson’s Disease and Its Substrate-Involved Mouse Experimental Models." International Journal of Molecular Sciences 21, no. 4 (February 11, 2020): 1202. http://dx.doi.org/10.3390/ijms21041202.
Повний текст джерелаKarakkat, Jimsheena V., Suneesh Kaimala, Sreejisha P. Sreedharan, Princy Jayaprakash, Ernest A. Adeghate, Suraiya A. Ansari, Ernesto Guccione, Eric P. K. Mensah-Brown, and Bright Starling Emerald. "The metabolic sensor PASK is a histone 3 kinase that also regulates H3K4 methylation by associating with H3K4 MLL2 methyltransferase complex." Nucleic Acids Research 47, no. 19 (September 16, 2019): 10086–103. http://dx.doi.org/10.1093/nar/gkz786.
Повний текст джерелаKimura, Satoshi, Yoshihiro Shiraiwa, and Iwane Suzuki. "Function of the N-terminal region of the phosphate-sensing histidine kinase, SphS, in Synechocystis sp. PCC 6803." Microbiology 155, no. 7 (July 1, 2009): 2256–64. http://dx.doi.org/10.1099/mic.0.028514-0.
Повний текст джерелаKatschinski, Dörthe M., Hugo H. Marti, Klaus F. Wagner, Junpei Shibata, Katrin Eckhardt, Falk Martin, Reinhard Depping, et al. "Targeted Disruption of the Mouse PAS Domain Serine/Threonine Kinase PASKIN." Molecular and Cellular Biology 23, no. 19 (October 1, 2003): 6780–89. http://dx.doi.org/10.1128/mcb.23.19.6780-6789.2003.
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