Статті в журналах з теми "Rhodopsin proteins"
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Meng, Chao Luo, Gang Dai, and Tatsuo Iwasa. "Identification of Microbial Rhodopsin Genes from Salt Lake in Inner Mongolia." Advanced Materials Research 518-523 (May 2012): 380–83. http://dx.doi.org/10.4028/www.scientific.net/amr.518-523.380.
Повний текст джерелаShen, Libing, Chao Chen, Hongxiang Zheng, and Li Jin. "The Evolutionary Relationship between Microbial Rhodopsins and Metazoan Rhodopsins." Scientific World Journal 2013 (2013): 1–10. http://dx.doi.org/10.1155/2013/435651.
Повний текст джерелаTam, Beatrice M., Orson L. Moritz, Lawrence B. Hurd, and David S. Papermaster. "Identification of an Outer Segment Targeting Signal in the Cooh Terminus of Rhodopsin Using Transgenic Xenopus laevis." Journal of Cell Biology 151, no. 7 (December 25, 2000): 1369–80. http://dx.doi.org/10.1083/jcb.151.7.1369.
Повний текст джерелаFu, Hsu-Yuan, Yu-Cheng Lin, Yung-Ning Chang, Hsiaochu Tseng, Ching-Che Huang, Kang-Cheng Liu, Ching-Shin Huang, et al. "A Novel Six-Rhodopsin System in a Single Archaeon." Journal of Bacteriology 192, no. 22 (August 27, 2010): 5866–73. http://dx.doi.org/10.1128/jb.00642-10.
Повний текст джерелаPoupault, Clara, Diane Choi, Khanh Lam-Kamath, Deepshe Dewett, Ansa Razzaq, Joseph Bunker, Alexis Perry, Irene Cho, and Jens Rister. "A combinatorial cis-regulatory logic restricts color-sensing Rhodopsins to specific photoreceptor subsets in Drosophila." PLOS Genetics 17, no. 6 (June 23, 2021): e1009613. http://dx.doi.org/10.1371/journal.pgen.1009613.
Повний текст джерелаChuang, Jen-Zen, and Ching-Hwa Sung. "The Cytoplasmic Tail of Rhodopsin Acts as a Novel Apical Sorting Signal in Polarized MDCK Cells." Journal of Cell Biology 142, no. 5 (September 7, 1998): 1245–56. http://dx.doi.org/10.1083/jcb.142.5.1245.
Повний текст джерелаTarlachkov, Sergey V., Taras V. Shevchuk, Maria del Carmen Montero-Calasanz, and Irina P. Starodumova. "Diversity of rhodopsins in cultivated bacteria of the family Geodermatophilaceae associated with non-aquatic environments." Bioinformatics 36, no. 6 (November 11, 2019): 1668–72. http://dx.doi.org/10.1093/bioinformatics/btz840.
Повний текст джерелаAhrendt, Steven R., Edgar Mauricio Medina, Chia-en A. Chang, and Jason E. Stajich. "Exploring the binding properties and structural stability of an opsin in the chytridSpizellomyces punctatususing comparative and molecular modeling." PeerJ 5 (April 27, 2017): e3206. http://dx.doi.org/10.7717/peerj.3206.
Повний текст джерелаShtyrov, Andrey A., Dmitrii M. Nikolaev, Vladimir N. Mironov, Andrey V. Vasin, Maxim S. Panov, Yuri S. Tveryanovich, and Mikhail N. Ryazantsev. "Simple Models to Study Spectral Properties of Microbial and Animal Rhodopsins: Evaluation of the Electrostatic Effect of Charged and Polar Residues on the First Absorption Band Maxima." International Journal of Molecular Sciences 22, no. 6 (March 16, 2021): 3029. http://dx.doi.org/10.3390/ijms22063029.
Повний текст джерелаKonno, Masae, Yumeka Yamauchi, Keiichi Inoue, and Hideki Kandori. "Expression analysis of microbial rhodopsin-like genes in Guillardia theta." PLOS ONE 15, no. 12 (December 3, 2020): e0243387. http://dx.doi.org/10.1371/journal.pone.0243387.
Повний текст джерелаChiang, Wei-Chieh, Carissa Messah, and Jonathan H. Lin. "IRE1 directs proteasomal and lysosomal degradation of misfolded rhodopsin." Molecular Biology of the Cell 23, no. 5 (March 2012): 758–70. http://dx.doi.org/10.1091/mbc.e11-08-0663.
Повний текст джерелаPenn, Wesley D., Andrew G. McKee, Charles P. Kuntz, Hope Woods, Veronica Nash, Timothy C. Gruenhagen, Francis J. Roushar, et al. "Probing biophysical sequence constraints within the transmembrane domains of rhodopsin by deep mutational scanning." Science Advances 6, no. 10 (March 2020): eaay7505. http://dx.doi.org/10.1126/sciadv.aay7505.
Повний текст джерелаAsano, Y., S. Nakamura, S. Ishida, K. Azuma, and T. Shinozawa. "Rhodopsin-like proteins in planarian eye and auricle: detection and functional analysis." Journal of Experimental Biology 201, no. 9 (May 1, 1998): 1263–71. http://dx.doi.org/10.1242/jeb.201.9.1263.
Повний текст джерелаKirpichnikov, M. P., and М. А. Оstrovsky. "Optogenetics and vision." Вестник Российской академии наук 89, no. 2 (March 20, 2019): 125–30. http://dx.doi.org/10.31857/s0869-5873892125-130.
Повний текст джерелаKim, Benjamin, and Michael Z. Lin. "Optobiology: optical control of biological processes via protein engineering." Biochemical Society Transactions 41, no. 5 (September 23, 2013): 1183–88. http://dx.doi.org/10.1042/bst20130150.
Повний текст джерелаInoue, Keiichi. "Shining light on rhodopsin selectivity: How do proteins decide whether to transport H+ or Cl–?" Journal of Biological Chemistry 295, no. 44 (October 30, 2020): 14805–6. http://dx.doi.org/10.1074/jbc.h120.016032.
Повний текст джерелаChurch, Jonathan R., Jógvan Magnus Haugaard Olsen, and Igor Schapiro. "The Impact of Retinal Configuration on the Protein–Chromophore Interactions in Bistable Jumping Spider Rhodopsin-1." Molecules 27, no. 1 (December 23, 2021): 71. http://dx.doi.org/10.3390/molecules27010071.
Повний текст джерелаHuang, Huai-Wei, and Hyung Don Ryoo. "Drosophila fabp is required for light-dependent Rhodopsin-1 clearance and photoreceptor survival." PLOS Genetics 17, no. 10 (October 29, 2021): e1009551. http://dx.doi.org/10.1371/journal.pgen.1009551.
Повний текст джерелаZernii, Evgeni Yu, Konstantin E. Komolov, Sergei E. Permyakov, Tatiana Kolpakova, Daniele Dell'orco, Annika Poetzsch, Ekaterina L. Knyazeva, et al. "Involvement of the recoverin C-terminal segment in recognition of the target enzyme rhodopsin kinase." Biochemical Journal 435, no. 2 (March 29, 2011): 441–50. http://dx.doi.org/10.1042/bj20110013.
Повний текст джерелаKishigami, A., T. Ogasawara, Y. Watanabe, M. Hirata, T. Maeda, F. Hayashi, and Y. Tsukahara. "Inositol-1,4,5-trisphosphate-binding proteins controlling the phototransduction cascade of invertebrate visual cells." Journal of Experimental Biology 204, no. 3 (February 1, 2001): 487–93. http://dx.doi.org/10.1242/jeb.204.3.487.
Повний текст джерелаKakakhel, Mashal, Lars Tebbe, Mustafa S. Makia, Shannon M. Conley, David M. Sherry, Muayyad R. Al-Ubaidi, and Muna I. Naash. "Syntaxin 3 is essential for photoreceptor outer segment protein trafficking and survival." Proceedings of the National Academy of Sciences 117, no. 34 (August 10, 2020): 20615–24. http://dx.doi.org/10.1073/pnas.2010751117.
Повний текст джерелаYonamine, Ikuko, Takeshi Bamba, Niraj K. Nirala, Nahid Jesmin, Teresa Kosakowska-Cholody, Kunio Nagashima, Eiichiro Fukusaki, Jairaj K. Acharya, and Usha Acharya. "Sphingosine kinases and their metabolites modulate endolysosomal trafficking in photoreceptors." Journal of Cell Biology 192, no. 4 (February 14, 2011): 557–67. http://dx.doi.org/10.1083/jcb.201004098.
Повний текст джерелаIslam, Md Sirajul, James P. Gaston, and Matthew A. B. Baker. "Fluorescence Approaches for Characterizing Ion Channels in Synthetic Bilayers." Membranes 11, no. 11 (November 4, 2021): 857. http://dx.doi.org/10.3390/membranes11110857.
Повний текст джерелаSakurai, Keisuke, Akishi Onishi, Hiroo Imai, Osamu Chisaka, Yoshiki Ueda, Jiro Usukura, Kei Nakatani, and Yoshinori Shichida. "Physiological Properties of Rod Photoreceptor Cells in Green-sensitive Cone Pigment Knock-in Mice." Journal of General Physiology 130, no. 1 (June 25, 2007): 21–40. http://dx.doi.org/10.1085/jgp.200609729.
Повний текст джерелаGeneva, Ivayla I., Han Yen Tan, and Peter D. Calvert. "Untangling ciliary access and enrichment of two rhodopsin-like receptors using quantitative fluorescence microscopy reveals cell-specific sorting pathways." Molecular Biology of the Cell 28, no. 4 (February 15, 2017): 554–66. http://dx.doi.org/10.1091/mbc.e16-07-0549.
Повний текст джерелаBelousov, Anatolii, Ivan Maslov, Polina Khorn, Alexander Mishin, Mikhail Baranov, Thomas Gensch, and Valentin Borshchevskiy. "Abstract P-10: Solvatochromic Fluorescent Dyes Tested for Spectroscopic Measurements of Protein Conformational Dynamics." International Journal of Biomedicine 11, Suppl_1 (June 1, 2021): S15. http://dx.doi.org/10.21103/ijbm.11.suppl_1.p10.
Повний текст джерелаPojer, Jonathan M., Abdul Jabbar Saiful Hilmi, Shu Kondo, and Kieran F. Harvey. "Crumbs and the apical spectrin cytoskeleton regulate R8 cell fate in the Drosophila eye." PLOS Genetics 17, no. 6 (June 7, 2021): e1009146. http://dx.doi.org/10.1371/journal.pgen.1009146.
Повний текст джерелаWieland, Thomas, Isabel Ulibarri, Klaus Aktories, Peter Gierschik, and Karl H. Jakobs. "Interaction of small G proteins with photoexcited rhodopsin." FEBS Letters 263, no. 2 (April 24, 1990): 195–98. http://dx.doi.org/10.1016/0014-5793(90)81372-u.
Повний текст джерелаXu, Xian-Zhong Shawn, Atish Choudhury, Xiaoling Li, and Craig Montell. "Coordination of an Array of Signaling Proteins through Homo- and Heteromeric Interactions Between PDZ Domains and Target Proteins." Journal of Cell Biology 142, no. 2 (July 27, 1998): 545–55. http://dx.doi.org/10.1083/jcb.142.2.545.
Повний текст джерелаShirzad-Wasei, Nazhat, Jenny van Oostrum, Petra H. M. Bovee-Geurts, Lisanne J. A. Kusters, Giel J. C. G. M. Bosman, and Willem J. DeGrip. "Rapid transfer of overexpressed integral membrane protein from the host membrane into soluble lipid nanodiscs without previous purification." Biological Chemistry 396, no. 8 (August 1, 2015): 903–15. http://dx.doi.org/10.1515/hsz-2015-0100.
Повний текст джерелаNeedham, David M., Susumu Yoshizawa, Toshiaki Hosaka, Camille Poirier, Chang Jae Choi, Elisabeth Hehenberger, Nicholas A. T. Irwin, et al. "A distinct lineage of giant viruses brings a rhodopsin photosystem to unicellular marine predators." Proceedings of the National Academy of Sciences 116, no. 41 (September 23, 2019): 20574–83. http://dx.doi.org/10.1073/pnas.1907517116.
Повний текст джерелаKunduri, Govind, Changqing Yuan, Velayoudame Parthibane, Katherine M. Nyswaner, Ritu Kanwar, Kunio Nagashima, Steven G. Britt, et al. "Phosphatidic acid phospholipase A1 mediates ER–Golgi transit of a family of G protein–coupled receptors." Journal of Cell Biology 206, no. 1 (July 7, 2014): 79–95. http://dx.doi.org/10.1083/jcb.201405020.
Повний текст джерелаKLAASSEN, Corné H. W., Petra H. M. BOVEE-GEURTS, Godelieve L. J. DECALUWÉ, and Willem J. DEGRIP. "Large-scale production and purification of functional recombinant bovine rhodopsin with the use of the baculovirus expression system." Biochemical Journal 342, no. 2 (August 24, 1999): 293–300. http://dx.doi.org/10.1042/bj3420293.
Повний текст джерелаVan Eps, Ned, Christian Altenbach, Lydia N. Caro, Naomi R. Latorraca, Scott A. Hollingsworth, Ron O. Dror, Oliver P. Ernst, and Wayne L. Hubbell. "Gi- and Gs-coupled GPCRs show different modes of G-protein binding." Proceedings of the National Academy of Sciences 115, no. 10 (February 20, 2018): 2383–88. http://dx.doi.org/10.1073/pnas.1721896115.
Повний текст джерелаDizhoor, Alexander M., Elina R. Nekrasova, and Pavel P. Philippov. "The binding of G proteins to immobilized delipidated rhodopsin." Biochemical and Biophysical Research Communications 162, no. 1 (July 1989): 544–49. http://dx.doi.org/10.1016/0006-291x(89)92031-7.
Повний текст джерелаFujita, Jun, Norika Sakurai, and Takao Shinozawa. "Presence of rhodopsin-like proteins in the planarian head." Hydrobiologia 227, no. 1 (December 1991): 93–94. http://dx.doi.org/10.1007/bf00027587.
Повний текст джерелаSchopf, Krystina, Thomas K. Smylla, and Armin Huber. "Immunocytochemical Labeling of Rhabdomeric Proteins inDrosophilaPhotoreceptor Cells Is Compromised by a Light-dependent Technical Artifact." Journal of Histochemistry & Cytochemistry 67, no. 10 (June 27, 2019): 745–57. http://dx.doi.org/10.1369/0022155419859870.
Повний текст джерелаBesaw, Jessica E., Wei-Lin Ou, Takefumi Morizumi, Bryan T. Eger, Juan D. Sanchez Vasquez, Jessica H. Y. Chu, Andrew Harris, Leonid S. Brown, R. J. Dwayne Miller, and Oliver P. Ernst. "The crystal structures of a chloride-pumping microbial rhodopsin and its proton-pumping mutant illuminate proton transfer determinants." Journal of Biological Chemistry 295, no. 44 (July 23, 2020): 14793–804. http://dx.doi.org/10.1074/jbc.ra120.014118.
Повний текст джерелаGrime, Rachael L., Richard T. Logan, Stephanie A. Nestorow, Pooja Sridhar, Patricia C. Edwards, Christopher G. Tate, Bert Klumperman, et al. "Differences in SMA-like polymer architecture dictate the conformational changes exhibited by the membrane protein rhodopsin encapsulated in lipid nano-particles." Nanoscale 13, no. 31 (2021): 13519–28. http://dx.doi.org/10.1039/d1nr02419a.
Повний текст джерелаPaolicchi, Fabio, Lara Lombardi, Nello Ceccarelli, and Roberto Lorenzi. "Are retinal and retinal-binding proteins involved in stomatal response to blue light?" Functional Plant Biology 32, no. 12 (2005): 1135. http://dx.doi.org/10.1071/fp05054.
Повний текст джерелаGerrard, Elliot, Eshita Mutt, Takashi Nagata, Mitsumasa Koyanagi, Tilman Flock, Elena Lesca, Gebhard F. X. Schertler, Akihisa Terakita, Xavier Deupi, and Robert J. Lucas. "Convergent evolution of tertiary structure in rhodopsin visual proteins from vertebrates and box jellyfish." Proceedings of the National Academy of Sciences 115, no. 24 (May 23, 2018): 6201–6. http://dx.doi.org/10.1073/pnas.1721333115.
Повний текст джерелаDeretic, D., and D. S. Papermaster. "Polarized sorting of rhodopsin on post-Golgi membranes in frog retinal photoreceptor cells." Journal of Cell Biology 113, no. 6 (June 15, 1991): 1281–93. http://dx.doi.org/10.1083/jcb.113.6.1281.
Повний текст джерелаYun, Ji-Hye, Mio Ohki, Jae-Hyun Park, Naito Ishimoto, Ayana Sato-Tomita, Wonbin Lee, Zeyu Jin, et al. "Pumping mechanism of NM-R3, a light-driven bacterial chloride importer in the rhodopsin family." Science Advances 6, no. 6 (February 2020): eaay2042. http://dx.doi.org/10.1126/sciadv.aay2042.
Повний текст джерелаNakao, Yutaka, Kazumi Shimono, Takashi Kikukawa, Kunio Ihara, and Naoki Kamo. "1P090 Photochemistry of Sensory Rhodopsin III from Haloarcula marismortui(HmSRIII)(Membrane proteins,Poster Presentations)." Seibutsu Butsuri 47, supplement (2007): S46. http://dx.doi.org/10.2142/biophys.47.s46_1.
Повний текст джерелаYe, Shixin, Caroline Köhrer, Thomas Huber, Manija Kazmi, Pallavi Sachdev, Elsa C. Y. Yan, Aditi Bhagat, Uttam L. RajBhandary, and Thomas P. Sakmar. "Site-specific Incorporation of Keto Amino Acids into Functional G Protein-coupled Receptors Using Unnatural Amino Acid Mutagenesis." Journal of Biological Chemistry 283, no. 3 (November 8, 2007): 1525–33. http://dx.doi.org/10.1074/jbc.m707355200.
Повний текст джерелаUlshafer, R. J., W. W. Hauswirth, and A. van der Langerijt. "EM immunocytochemical localization of rhodopsin and IRBP during retinal development." Proceedings, annual meeting, Electron Microscopy Society of America 47 (August 6, 1989): 800–801. http://dx.doi.org/10.1017/s0424820100155979.
Повний текст джерелаKhorana, H. G. "Two light-transducing membrane proteins: bacteriorhodopsin and the mammalian rhodopsin." Proceedings of the National Academy of Sciences 90, no. 4 (February 15, 1993): 1166–71. http://dx.doi.org/10.1073/pnas.90.4.1166.
Повний текст джерелаCastiglione, Gianni M., Frances E. Hauser, Brian S. Liao, Nathan K. Lujan, Alexander Van Nynatten, James M. Morrow, Ryan K. Schott, Nihar Bhattacharyya, Sarah Z. Dungan, and Belinda S. W. Chang. "Evolution of nonspectral rhodopsin function at high altitudes." Proceedings of the National Academy of Sciences 114, no. 28 (June 22, 2017): 7385–90. http://dx.doi.org/10.1073/pnas.1705765114.
Повний текст джерелаDeretic, D., and D. S. Papermaster. "Rab6 is associated with a compartment that transports rhodopsin from the trans-Golgi to the site of rod outer segment disk formation in frog retinal photoreceptors." Journal of Cell Science 106, no. 3 (November 1, 1993): 803–13. http://dx.doi.org/10.1242/jcs.106.3.803.
Повний текст джерелаDeretic, D., L. A. Huber, N. Ransom, M. Mancini, K. Simons, and D. S. Papermaster. "rab8 in retinal photoreceptors may participate in rhodopsin transport and in rod outer segment disk morphogenesis." Journal of Cell Science 108, no. 1 (January 1, 1995): 215–24. http://dx.doi.org/10.1242/jcs.108.1.215.
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