Статті в журналах з теми "C-terminal loop"
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MONLEÓN, Daniel, Vicent ESTEVE, Helena KOVACS, Juan J. CALVETE, and Bernardo CELDA. "Conformation and concerted dynamics of the integrin-binding site and the C-terminal region of echistatin revealed by homonuclear NMR." Biochemical Journal 387, no. 1 (March 22, 2005): 57–66. http://dx.doi.org/10.1042/bj20041343.
Повний текст джерелаHarouaka, Djamila, and Gail W. Wertz. "Mutations in the C-Terminal Loop of the Nucleocapsid Protein Affect Vesicular Stomatitis Virus RNA Replication and Transcription Differentially." Journal of Virology 83, no. 22 (September 2, 2009): 11429–39. http://dx.doi.org/10.1128/jvi.00813-09.
Повний текст джерелаBurkhart, Michael D., Paul D'Agostino, Samuel C. Kayman, and Abraham Pinter. "Involvement of the C-Terminal Disulfide-Bonded Loop of Murine Leukemia Virus SU Protein in a Postbinding Step Critical for Viral Entry." Journal of Virology 79, no. 12 (June 15, 2005): 7868–76. http://dx.doi.org/10.1128/jvi.79.12.7868-7876.2005.
Повний текст джерелаQiao, Renping, Florian Weissmann, Masaya Yamaguchi, Nicholas G. Brown, Ryan VanderLinden, Richard Imre, Marc A. Jarvis, et al. "Mechanism of APC/CCDC20 activation by mitotic phosphorylation." Proceedings of the National Academy of Sciences 113, no. 19 (April 25, 2016): E2570—E2578. http://dx.doi.org/10.1073/pnas.1604929113.
Повний текст джерелаTakemoto, D. J., L. J. Takemoto, J. Hansen, and D. Morrison. "Regulation of retinal transducin by C-terminal peptides of rhodopsin." Biochemical Journal 232, no. 3 (December 15, 1985): 669–72. http://dx.doi.org/10.1042/bj2320669.
Повний текст джерелаRen, Chunguang, Satoshi Nagao, Masaru Yamanaka, Hirofumi Komori, Yasuhito Shomura, Yoshiki Higuchi, and Shun Hirota. "Oligomerization enhancement and two domain swapping mode detection for thermostable cytochrome c552via the elongation of the major hinge loop." Molecular BioSystems 11, no. 12 (2015): 3218–21. http://dx.doi.org/10.1039/c5mb00545k.
Повний текст джерелаBury, Loredana, Emanuela Falcinelli, Haripriya Kuchi Bhotla, Anna Maria Mezzasoma, Giuseppe Guglielmini, Alexander Tischer, Laurie Moon-Tasson, Matthew Auton та Paolo Gresele. "A p.Arg127Gln variant in GPIbα LRR5 allosterically enhances affinity for VWF: a novel form of platelet-type VWD". Blood Advances 6, № 7 (1 квітня 2022): 2236–46. http://dx.doi.org/10.1182/bloodadvances.2021005463.
Повний текст джерелаUesugi, Y., J. Arima, M. Iwabuchi, and T. Hatanaka. "C-terminal loop of Streptomyces phospholipase D has multiple functional roles." Protein Science 16, no. 2 (December 22, 2006): 197–207. http://dx.doi.org/10.1110/ps.062537907.
Повний текст джерелаYano, Yoshiaki, Takuya Shimbo, Yukihiko Sugimoto та Katsumi Matsuzaki. "Intracellular third loop–C-terminal tail interaction in prostaglandin EP3β receptor". Biochemical and Biophysical Research Communications 371, № 4 (липень 2008): 846–49. http://dx.doi.org/10.1016/j.bbrc.2008.04.180.
Повний текст джерелаGoch, G., H. Kozłowska, A. Wójtowicz, and A. Bierzyński. "A comparative CD and fluorescence study of a series of model calcium-binding peptides." Acta Biochimica Polonica 46, no. 3 (September 30, 1999): 673–77. http://dx.doi.org/10.18388/abp.1999_4139.
Повний текст джерелаBlodgett, David M., Julie K. De Zutter, Kara B. Levine, Pusha Karim, and Anthony Carruthers. "Structural Basis of GLUT1 Inhibition by Cytoplasmic ATP." Journal of General Physiology 130, no. 2 (July 16, 2007): 157–68. http://dx.doi.org/10.1085/jgp.200709818.
Повний текст джерелаBannister, Roger A., Symeon Papadopoulos, Claudia S. Haarmann та Kurt G. Beam. "Effects of inserting fluorescent proteins into the α1S II–III loop: insights into excitation–contraction coupling". Journal of General Physiology 134, № 1 (29 червня 2009): 35–51. http://dx.doi.org/10.1085/jgp.200910241.
Повний текст джерелаShen, Yang, Jing-fei Dong, Gabriel M. Romo, Wendy Arceneaux, Andrea Aprico, Elizabeth E. Gardiner, José A. López, Michael C. Berndt та Robert K. Andrews. "Functional analysis of the C-terminal flanking sequence of platelet glycoprotein Ibα using canine–human chimeras". Blood 99, № 1 (1 січня 2002): 145–50. http://dx.doi.org/10.1182/blood.v99.1.145.
Повний текст джерелаSenda, Toshiya, Miki Senda, Takeru Hayashi, and Masanori Hatakeyama. "Structure and function of the CagA oncoprotein from Helicobacter pylori." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C839. http://dx.doi.org/10.1107/s2053273314091608.
Повний текст джерелаMason, A. B., S. A. Brown, and W. R. Church. "A highly conserved surface loop in the C-terminal domain of ovotransferrin (residues 570-584) is remote from the receptor-binding site." Biochemical Journal 266, no. 2 (March 1, 1990): 393–98. http://dx.doi.org/10.1042/bj2660393.
Повний текст джерелаCherry, Amy L., Caitriona A. Dennis, Andrew Baron, Leslie E. Eisele, Pia A. Thommes, and Joachim Jaeger. "Hydrophobic and Charged Residues in the C-Terminal Arm of Hepatitis C Virus RNA-Dependent RNA Polymerase Regulate Initiation and Elongation." Journal of Virology 89, no. 4 (November 26, 2014): 2052–63. http://dx.doi.org/10.1128/jvi.01106-14.
Повний текст джерелаTOMOO, Koji, Xu SHEN, Koumei OKABE, Yoshiaki NOZOE, Shoichi FUKUHARA, Shigenobu MORINO, Toshimasa ISHIDA, et al. "Crystal structures of 7-methylguanosine 5′-triphosphate (m7GTP)- and P1-7-methylguanosine-P3-adenosine-5′,5′-triphosphate (m7GpppA)-bound human full-length eukaryotic initiation factor 4E: biological importance of the C-terminal flexible region." Biochemical Journal 362, no. 3 (March 8, 2002): 539–44. http://dx.doi.org/10.1042/bj3620539.
Повний текст джерелаJ. S. Loureiro, Rui, Diogo Vila-Viçosa, Miguel Machuqueiro, Eugene I. Shakhnovich та Patrícia F. N. Faísca. "The Early Phase of β2m Aggregation: An Integrative Computational Study Framed on the D76N Mutant and the ΔN6 Variant". Biomolecules 9, № 8 (14 серпня 2019): 366. http://dx.doi.org/10.3390/biom9080366.
Повний текст джерелаSugishima, Masakazu, Kei Wada, Keiichi Fukuyama та Ken Yamamoto. "Crystal structure of phytochromobilin synthase in complex with biliverdin IXα, a key enzyme in the biosynthesis of phytochrome". Journal of Biological Chemistry 295, № 3 (10 грудня 2019): 771–82. http://dx.doi.org/10.1074/jbc.ra119.011431.
Повний текст джерелаStrzelecka-Gołaszewska, H., M. Mossakowska, A. Woźniak, J. Moraczewska, and H. Nakayama. "Long-range conformational effects of proteolytic removal of the last three residues of actin." Biochemical Journal 307, no. 2 (April 15, 1995): 527–34. http://dx.doi.org/10.1042/bj3070527.
Повний текст джерелаLangedijk, Johannes P. M. "Translocation Activity of C-terminal Domain of Pestivirus Ernsand Ribotoxin L3 Loop." Journal of Biological Chemistry 277, no. 7 (October 22, 2001): 5308–14. http://dx.doi.org/10.1074/jbc.m104147200.
Повний текст джерелаTruong, Amy B., Shane C. Masters, Hongzhu Yang, and Haian Fu. "Role of the 14-3-3 C-terminal loop in ligand interaction." Proteins: Structure, Function, and Bioinformatics 49, no. 3 (November 15, 2002): 321–25. http://dx.doi.org/10.1002/prot.10210.
Повний текст джерелаKoschel, Matthias, Reiner Thomssen, and Volker Bruss. "Extensive Mutagenesis of the Hepatitis B Virus Core Gene and Mapping of Mutations That Allow Capsid Formation." Journal of Virology 73, no. 3 (March 1, 1999): 2153–60. http://dx.doi.org/10.1128/jvi.73.3.2153-2160.1999.
Повний текст джерелаOstapenko, Denis, and Mark J. Solomon. "Phosphorylation by Cak1 Regulates the C-Terminal Domain Kinase Ctk1 in Saccharomyces cerevisiae." Molecular and Cellular Biology 25, no. 10 (May 15, 2005): 3906–13. http://dx.doi.org/10.1128/mcb.25.10.3906-3913.2005.
Повний текст джерелаLee, Haekyung, Hyukwoo Shin, Eckard Wimmer, and Aniko V. Paul. "cis-Acting RNA Signals in the NS5B C-Terminal Coding Sequence of the Hepatitis C Virus Genome." Journal of Virology 78, no. 20 (October 15, 2004): 10865–77. http://dx.doi.org/10.1128/jvi.78.20.10865-10877.2004.
Повний текст джерелаGul, Mehreen, Ahmad Navid, Muhammad Fakhar, and Sajid Rashid. "SHP-1 tyrosine phosphatase binding to c-Src kinase phosphor-dependent conformations: A comparative structural framework." PLOS ONE 18, no. 1 (January 13, 2023): e0278448. http://dx.doi.org/10.1371/journal.pone.0278448.
Повний текст джерелаEpp, Simone F., Thilo Köhler, Patrick Plésiat, Mehri Michéa-Hamzehpour, Joachim Frey, and Jean-Claude Pechère. "C-Terminal Region of Pseudomonas aeruginosa Outer Membrane Porin OprD Modulates Susceptibility to Meropenem." Antimicrobial Agents and Chemotherapy 45, no. 6 (June 1, 2001): 1780–87. http://dx.doi.org/10.1128/aac.45.6.1780-1787.2001.
Повний текст джерелаSanford, J. C., Y. Pan, and M. Wessling-Resnick. "Properties of Rab5 N-terminal domain dictate prenylation of C-terminal cysteines." Molecular Biology of the Cell 6, no. 1 (January 1995): 71–85. http://dx.doi.org/10.1091/mbc.6.1.71.
Повний текст джерелаOkamoto, Hisayo, Tove Hammarberg, Ying-Yi Zhang, Bengt Persson, Takashi Watanabe, Bengt Samuelsson, and Olof Rådmark. "Mutation analysis of the human 5-lipoxygenase C-terminus: Support for a stabilizing C-terminal loop." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1749, no. 1 (May 2005): 123–31. http://dx.doi.org/10.1016/j.bbapap.2005.03.005.
Повний текст джерелаSierra-Valdez, Francisco, Caleigh M. Azumaya, Luis O. Romero, Terunaga Nakagawa, and Julio F. Cordero-Morales. "Structure–function analyses of the ion channel TRPC3 reveal that its cytoplasmic domain allosterically modulates channel gating." Journal of Biological Chemistry 293, no. 41 (August 23, 2018): 16102–14. http://dx.doi.org/10.1074/jbc.ra118.005066.
Повний текст джерелаVranken, Wim F., Miloš Buděšínský, Franky Fant, Kris Boulez, Hélène Gras-Masse, and Frans A. M. Borremans. "Conformational Features of a Synthetic Cyclic Peptide Corresponding to the Complete V3 Loop of the ELI HIV-1 Strain in Water." Collection of Czechoslovak Chemical Communications 61, no. 5 (1996): 742–50. http://dx.doi.org/10.1135/cccc19960742.
Повний текст джерелаChan, Tung O., Jin Zhang, Brian C. Tiegs, Brian Blumhof, Linda Yan, Nikhil Keny, Morgan Penny, et al. "Akt kinase C-terminal modifications control activation loop dephosphorylation and enhance insulin response." Biochemical Journal 471, no. 1 (September 21, 2015): 37–51. http://dx.doi.org/10.1042/bj20150325.
Повний текст джерелаBarski, Oleg A., Kenneth H. Gabbay, and Kurt M. Bohren. "The C-Terminal Loop of Aldehyde Reductase Determines the Substrate and Inhibitor Specificity†." Biochemistry 35, no. 45 (January 1996): 14276–80. http://dx.doi.org/10.1021/bi9619740.
Повний текст джерелаChen, Yi-Chun, Yao-Tsung Chang, Chiu-Yueh Chen, Jia-Hau Shiu, Chun-Ho Cheng, Chun-Hao Huang, Ju-Fei Chen, and Woei-Jer Chuang. "Structural Insight into Integrin Recognition and Anticancer Activity of Echistatin." Toxins 12, no. 11 (November 9, 2020): 709. http://dx.doi.org/10.3390/toxins12110709.
Повний текст джерелаPeverelli, Erika, Giovanna Mantovani, Davide Calebiro, Andrea Doni, Sara Bondioni, Andrea Lania, Paolo Beck-Peccoz, and Anna Spada. "The Third Intracellular Loop of the Human Somatostatin Receptor 5 Is Crucial for Arrestin Binding and Receptor Internalization after Somatostatin Stimulation." Molecular Endocrinology 22, no. 3 (March 1, 2008): 676–88. http://dx.doi.org/10.1210/me.2007-0068.
Повний текст джерелаLaw, Ruby H. P., Trifina Sofian, Wan-Ting Kan, Anita J. Horvath, Corinne R. Hitchen, Christopher G. Langendorf, Ashley M. Buckle, James C. Whisstock та Paul B. Coughlin. "X-ray crystal structure of the fibrinolysis inhibitor α2-antiplasmin". Blood 111, № 4 (15 лютого 2008): 2049–52. http://dx.doi.org/10.1182/blood-2007-09-114215.
Повний текст джерелаZhou, Zi-Ren, Yu-Hang Zhang, Shuai Liu, Ai-Xin Song, and Hong-Yu Hu. "Length of the active-site crossover loop defines the substrate specificity of ubiquitin C-terminal hydrolases for ubiquitin chains." Biochemical Journal 441, no. 1 (December 14, 2011): 143–49. http://dx.doi.org/10.1042/bj20110699.
Повний текст джерелаWang, Fanghua, Ruixia Wei, Abdelkarim Abousalham, Wuchong Chen, Bo Yang, and Yonghua Wang. "Effect of N- and C-Terminal Amino Acids on the Interfacial Binding Properties of Phospholipase D from Vibrio parahaemolyticus." International Journal of Molecular Sciences 19, no. 8 (August 19, 2018): 2447. http://dx.doi.org/10.3390/ijms19082447.
Повний текст джерелаSADLISH, Heather, Frederick M. R. WILLIAMS, and Wayne F. FLINTOFF. "Cytoplasmic domains of the reduced folate carrier are essential for trafficking, but not function." Biochemical Journal 364, no. 3 (June 15, 2002): 777–86. http://dx.doi.org/10.1042/bj20011361.
Повний текст джерелаSenda, Yoshie, Naoko Murata‐Kamiya, and Masanori Hatakeyama. "C‐terminal Src kinase‐mediated EPIYA phosphorylation of Pragmin creates a feed‐forward C‐terminal Src kinase activation loop that promotes cell motility." Cancer Science 107, no. 7 (June 13, 2016): 972–80. http://dx.doi.org/10.1111/cas.12962.
Повний текст джерелаCarlberg, K., and L. Rohrschneider. "The effect of activating mutations on dimerization, tyrosine phosphorylation and internalization of the macrophage colony stimulating factor receptor." Molecular Biology of the Cell 5, no. 1 (January 1994): 81–95. http://dx.doi.org/10.1091/mbc.5.1.81.
Повний текст джерелаMaerz, Anne L., Heidi E. Drummer, Kirilee A. Wilson, and Pantelis Poumbourios. "Functional Analysis of the Disulfide-Bonded Loop/Chain Reversal Region of Human Immunodeficiency Virus Type 1 gp41 Reveals a Critical Role in gp120-gp41 Association." Journal of Virology 75, no. 14 (July 15, 2001): 6635–44. http://dx.doi.org/10.1128/jvi.75.14.6635-6644.2001.
Повний текст джерелаPearson, Adam J., Paul Fullwood, Gabriela Toro Tapia, Ian Prise, Michael P. Smith, Qiuping Xu, Allan Jordan, et al. "Discovery of a Gatekeeper Residue in the C-Terminal Tail of the Extracellular Signal-Regulated Protein Kinase 5 (ERK5)." International Journal of Molecular Sciences 21, no. 3 (January 31, 2020): 929. http://dx.doi.org/10.3390/ijms21030929.
Повний текст джерелаIshii, K., H. Hayashi, M. Todaka, S. Kamohara, F. Kanai, H. Jinnouchi, L. Wang, and Y. Ebina. "Possible domains responsible for intracellular targeting and insulin-dependent translocation of glucose transporter type 4." Biochemical Journal 309, no. 3 (August 1, 1995): 813–23. http://dx.doi.org/10.1042/bj3090813.
Повний текст джерелаLabrosse, Béatrice, Carole Treboute, Anne Brelot, and Marc Alizon. "Cooperation of the V1/V2 and V3 Domains of Human Immunodeficiency Virus Type 1 gp120 for Interaction with the CXCR4 Receptor." Journal of Virology 75, no. 12 (June 15, 2001): 5457–64. http://dx.doi.org/10.1128/jvi.75.12.5457-5464.2001.
Повний текст джерелаTerasawa, Kazuya, Katsuhiko Yoshimatsu, Shun-ichiro Iemura, Tohru Natsume, Keiji Tanaka, and Yasufumi Minami. "Cdc37 Interacts with the Glycine-Rich Loop of Hsp90 Client Kinases." Molecular and Cellular Biology 26, no. 9 (May 1, 2006): 3378–89. http://dx.doi.org/10.1128/mcb.26.9.3378-3389.2006.
Повний текст джерелаAlmond, David, Chavdar Krachmarov, James Swetnam, Susan Zolla-Pazner, and Timothy Cardozo. "Resistance of Subtype C HIV-1 Strains to Anti-V3 Loop Antibodies." Advances in Virology 2012 (2012): 1–8. http://dx.doi.org/10.1155/2012/803535.
Повний текст джерелаRubenstein, Eric M., Rhonda R. McCartney, and Martin C. Schmidt. "Regulatory Domains of Snf1-Activating Kinases Determine Pathway Specificity." Eukaryotic Cell 5, no. 4 (April 2006): 620–27. http://dx.doi.org/10.1128/ec.5.4.620-627.2006.
Повний текст джерелаGuimaraes, Carla P., Martin D. Witte, Christopher S. Theile, Gunes Bozkurt, Lenka Kundrat, Annet E. M. Blom, and Hidde L. Ploegh. "Site-specific C-terminal and internal loop labeling of proteins using sortase-mediated reactions." Nature Protocols 8, no. 9 (August 29, 2013): 1787–99. http://dx.doi.org/10.1038/nprot.2013.101.
Повний текст джерелаRaja, M. Mobeen, and Rolf K. H. Kinne. "Interaction of C-Terminal Loop 13 of Sodium-Glucose Cotransporter SGLT1 with Lipid Bilayers†." Biochemistry 44, no. 25 (June 2005): 9123–29. http://dx.doi.org/10.1021/bi050323d.
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