Статті в журналах з теми "N-terminal domain (NTD)"
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Makarov, Valentin V., Ekaterina N. Rybakova, Alexander V. Efimov, Eugene N. Dobrov, Marina V. Serebryakova, Andrey G. Solovyev, Igor V. Yaminsky, Michael E. Taliansky, Sergey Yu Morozov, and Natalia O. Kalinina. "Domain organization of the N-terminal portion of hordeivirus movement protein TGBp1." Journal of General Virology 90, no. 12 (December 1, 2009): 3022–32. http://dx.doi.org/10.1099/vir.0.013862-0.
Повний текст джерелаIino, Hitoshi, Kwang Kim, Atsuhiro Shimada, Ryoji Masui, Seiki Kuramitsu, and Kenji Fukui. "Characterization of C- and N-terminal domains of Aquifex aeolicus MutL endonuclease: N-terminal domain stimulates the endonuclease activity of C-terminal domain in a zinc-dependent manner." Bioscience Reports 31, no. 5 (April 21, 2011): 309–22. http://dx.doi.org/10.1042/bsr20100116.
Повний текст джерелаKumar, Raj, and E. Brad Thompson. "Transactivation Functions of the N-Terminal Domains of Nuclear Hormone Receptors: Protein Folding and Coactivator Interactions." Molecular Endocrinology 17, no. 1 (January 1, 2003): 1–10. http://dx.doi.org/10.1210/me.2002-0258.
Повний текст джерелаRosenzweig, Rina, Patrick Farber, Algirdas Velyvis, Enrico Rennella, Michael P. Latham, and Lewis E. Kay. "ClpB N-terminal domain plays a regulatory role in protein disaggregation." Proceedings of the National Academy of Sciences 112, no. 50 (November 30, 2015): E6872—E6881. http://dx.doi.org/10.1073/pnas.1512783112.
Повний текст джерелаCohn, Marianne T., Peter Kjelgaard, Dorte Frees, José R. Penadés, and Hanne Ingmer. "Clp-dependent proteolysis of the LexA N-terminal domain in Staphylococcus aureus." Microbiology 157, no. 3 (March 1, 2011): 677–84. http://dx.doi.org/10.1099/mic.0.043794-0.
Повний текст джерелаRowley, Paul A., та Margaret C. M. Smith. "Role of the N-Terminal Domain of φC31 Integrase in attB-attP Synapsis". Journal of Bacteriology 190, № 20 (8 серпня 2008): 6918–21. http://dx.doi.org/10.1128/jb.00612-08.
Повний текст джерелаHu, Tiancen, Jennifer E. Yeh, Luca Pinello, Jaison Jacob, Srinivas Chakravarthy, Guo-Cheng Yuan, Rajiv Chopra, and David A. Frank. "Impact of the N-Terminal Domain of STAT3 in STAT3-Dependent Transcriptional Activity." Molecular and Cellular Biology 35, no. 19 (July 13, 2015): 3284–300. http://dx.doi.org/10.1128/mcb.00060-15.
Повний текст джерелаMarcianò, G., and D. T. Huang. "Structure of the human histone chaperone FACT Spt16 N-terminal domain." Acta Crystallographica Section F Structural Biology Communications 72, no. 2 (January 22, 2016): 121–28. http://dx.doi.org/10.1107/s2053230x15024565.
Повний текст джерелаWang, Yong-Sheng, Chung-ke Chang, and Ming-Hon Hou. "Crystallographic analysis of the N-terminal domain ofMiddle East respiratory syndrome coronavirusnucleocapsid protein." Acta Crystallographica Section F Structural Biology Communications 71, no. 8 (July 28, 2015): 977–80. http://dx.doi.org/10.1107/s2053230x15010146.
Повний текст джерелаGalaz-Davison, Pablo, Ernesto A. Román, and César A. Ramírez-Sarmiento. "The N-terminal domain of RfaH plays an active role in protein fold-switching." PLOS Computational Biology 17, no. 9 (September 3, 2021): e1008882. http://dx.doi.org/10.1371/journal.pcbi.1008882.
Повний текст джерелаFischer, Katharina, Sharon M. Kelly, Kate Watt, Nicholas C. Price, and Iain J. McEwan. "Conformation of the Mineralocorticoid Receptor N-terminal Domain: Evidence for Induced and Stable Structure." Molecular Endocrinology 24, no. 10 (October 1, 2010): 1935–48. http://dx.doi.org/10.1210/me.2010-0005.
Повний текст джерелаPark, Su, Il-Geun Park, Hyunkyung Kim та Ji Lee. "N-Terminal Domain Mediated Regulation of RORα1 Inhibits Invasive Growth in Prostate Cancer". International Journal of Molecular Sciences 20, № 7 (4 квітня 2019): 1684. http://dx.doi.org/10.3390/ijms20071684.
Повний текст джерелаZhang, Yiguo, Dorothy H. Crouch, Masayuki Yamamoto, and John D. Hayes. "Negative regulation of the Nrf1 transcription factor by its N-terminal domain is independent of Keap1: Nrf1, but not Nrf2, is targeted to the endoplasmic reticulum." Biochemical Journal 399, no. 3 (October 13, 2006): 373–85. http://dx.doi.org/10.1042/bj20060725.
Повний текст джерелаPapageorgiou, Nicolas, Julie Lichière, Amal Baklouti, François Ferron, Marion Sévajol, Bruno Canard, and Bruno Coutard. "Structural characterization of the N-terminal part of the MERS-CoV nucleocapsid by X-ray diffraction and small-angle X-ray scattering." Acta Crystallographica Section D Structural Biology 72, no. 2 (January 22, 2016): 192–202. http://dx.doi.org/10.1107/s2059798315024328.
Повний текст джерелаParatkar, Swaroopa, Aishwarya P. Deshpande, Guo-Qing Tang, and Smita S. Patel. "The N-terminal Domain of the Yeast Mitochondrial RNA Polymerase Regulates Multiple Steps of Transcription." Journal of Biological Chemistry 286, no. 18 (March 18, 2011): 16109–20. http://dx.doi.org/10.1074/jbc.m111.228023.
Повний текст джерелаYuan, Hanna, Pan-Hsien Kuo, Chien-Hao Chiang, and Woei Chyn Chu. "TDP-43 domain assembly and RNA binding specificity." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C217. http://dx.doi.org/10.1107/s2053273314097824.
Повний текст джерелаXie, Wei, Ivica Sowemimo, Rippei Hayashi, Juncheng Wang, Thomas R. Burkard, Julius Brennecke, Stefan L. Ameres, and Dinshaw J. Patel. "Structure-function analysis of microRNA 3′-end trimming by Nibbler." Proceedings of the National Academy of Sciences 117, no. 48 (November 16, 2020): 30370–79. http://dx.doi.org/10.1073/pnas.2018156117.
Повний текст джерелаWoo, Tai-Ting, Chi-Ning Chuang, Mika Higashide, Akira Shinohara, and Ting-Fang Wang. "Dual roles of yeast Rad51 N-terminal domain in repairing DNA double-strand breaks." Nucleic Acids Research 48, no. 15 (July 11, 2020): 8474–89. http://dx.doi.org/10.1093/nar/gkaa587.
Повний текст джерелаWinkelmann, A., M. Semtner, and J. C. Meier. "Chloride transporter KCC2-dependent neuroprotection depends on the N-terminal protein domain." Cell Death & Disease 6, no. 6 (June 2015): e1776-e1776. http://dx.doi.org/10.1038/cddis.2015.127.
Повний текст джерелаWang, Yuanyuan, Zemao Gong, Han Fang, Dongming Zhi, and Hu Tao. "The N-terminal 1–55 residues domain of pyruvate dehydrogenase from Escherichia coli assembles as a dimer in solution." Protein Engineering, Design and Selection 32, no. 6 (June 2019): 271–76. http://dx.doi.org/10.1093/protein/gzz044.
Повний текст джерелаBrodie, Jacqueline, and Iain J. McEwan. "Intra-domain communication between the N-terminal and DNA-binding domains of the androgen receptor: modulation of androgen response element DNA binding." Journal of Molecular Endocrinology 34, no. 3 (June 2005): 603–15. http://dx.doi.org/10.1677/jme.1.01723.
Повний текст джерелаLee, Jungwoon, Ja Young Kim, In Young Kang, Hye Kyoung Kim, Yong-Mahn Han, and Jungho Kim. "The EWS–Oct-4 fusion gene encodes a transforming gene." Biochemical Journal 406, no. 3 (August 29, 2007): 519–26. http://dx.doi.org/10.1042/bj20070243.
Повний текст джерелаYu, Xinzhe, and Ping Yi. "Structural Insights of Transcriptionally Active, Full-Length Androgen Receptor Coactivator Complexes." Journal of the Endocrine Society 5, Supplement_1 (May 1, 2021): A817. http://dx.doi.org/10.1210/jendso/bvab048.1665.
Повний текст джерелаNickens, Sausen, and Bochman. "The Biochemical Activities of the Saccharomyces cerevisiae Pif1 Helicase Are Regulated by Its N-Terminal Domain." Genes 10, no. 6 (May 28, 2019): 411. http://dx.doi.org/10.3390/genes10060411.
Повний текст джерелаBaker-LePain, Julie C., Marcella Sarzotti, Timothy A. Fields, Chuan-Yuan Li, and Christopher V. Nicchitta. "GRP94 (gp96) and GRP94 N-Terminal Geldanamycin Binding Domain Elicit Tissue Nonrestricted Tumor Suppression." Journal of Experimental Medicine 196, no. 11 (December 2, 2002): 1447–59. http://dx.doi.org/10.1084/jem.20020436.
Повний текст джерелаSharma, Dhakaram Pangeni, Ramachandran Vijayan, Syed Arif Abdul Rehman, and Samudrala Gourinath. "Structural insights into the interaction of helicase and primase in Mycobacterium tuberculosis." Biochemical Journal 475, no. 21 (November 15, 2018): 3493–509. http://dx.doi.org/10.1042/bcj20180673.
Повний текст джерелаLavery, Derek N., and Iain J. Mcewan. "Structure and function of steroid receptor AF1 transactivation domains: induction of active conformations." Biochemical Journal 391, no. 3 (October 25, 2005): 449–64. http://dx.doi.org/10.1042/bj20050872.
Повний текст джерелаVivoli-Vega, Mirella, Prandvera Guri, Fabrizio Chiti, and Francesco Bemporad. "Insight into the Folding and Dimerization Mechanisms of the N-Terminal Domain from Human TDP-43." International Journal of Molecular Sciences 21, no. 17 (August 29, 2020): 6259. http://dx.doi.org/10.3390/ijms21176259.
Повний текст джерелаRaman, Swetha, and Kaza Suguna. "Functional characterization of heat-shock protein 90 fromOryza sativaand crystal structure of its N-terminal domain." Acta Crystallographica Section F Structural Biology Communications 71, no. 6 (May 20, 2015): 688–96. http://dx.doi.org/10.1107/s2053230x15006639.
Повний текст джерелаUllah, M. Obayed, Thomas Ve, Matthew Mangan, Mohammed Alaidarous, Matthew J. Sweet, Ashley Mansell, and Bostjan Kobe. "The TLR signalling adaptor TRIF/TICAM-1 has an N-terminal helical domain with structural similarity to IFIT proteins." Acta Crystallographica Section D Biological Crystallography 69, no. 12 (November 19, 2013): 2420–30. http://dx.doi.org/10.1107/s0907444913022385.
Повний текст джерелаHussain, Mushtaq, Anusha Amanullah, Ayesha Aslam, Fozia Raza, Shabana Arzoo, Iffat Waqar Qureshi, Humera Waheed, et al. "Design and Immunoinformatic Assessment of Candidate Multivariant mRNA Vaccine Construct against Immune Escape Variants of SARS-CoV-2." Polymers 14, no. 16 (August 10, 2022): 3263. http://dx.doi.org/10.3390/polym14163263.
Повний текст джерелаHanamshet, Kritika, and Alexander V. Mazin. "The function of RAD52 N-terminal domain is essential for viability of BRCA-deficient cells." Nucleic Acids Research 48, no. 22 (December 4, 2020): 12778–91. http://dx.doi.org/10.1093/nar/gkaa1145.
Повний текст джерелаEgan, Susan M., Andrew J. Pease, Jeffrey Lang, Xiang Li, Vydehi Rao, William K. Gillette, Raquel Ruiz, Juan L. Ramos, and Richard E. Wolf. "Transcription Activation by a Variety of AraC/XylS Family Activators Does Not Depend on the Class II-Specific Activation Determinant in the N-Terminal Domain of the RNA Polymerase Alpha Subunit." Journal of Bacteriology 182, no. 24 (December 15, 2000): 7075–77. http://dx.doi.org/10.1128/jb.182.24.7075-7077.2000.
Повний текст джерелаSaikatendu, Kumar Singh, Jeremiah S. Joseph, Vanitha Subramanian, Benjamin W. Neuman, Michael J. Buchmeier, Raymond C. Stevens, and Peter Kuhn. "Ribonucleocapsid Formation of Severe Acute Respiratory Syndrome Coronavirus through Molecular Action of the N-Terminal Domain of N Protein." Journal of Virology 81, no. 8 (January 17, 2007): 3913–21. http://dx.doi.org/10.1128/jvi.02236-06.
Повний текст джерелаPrakash, Amresh, Vijay Kumar, Naveen Kumar Meena, and Andrew M. Lynn. "Elucidation of the structural stability and dynamics of heterogeneous intermediate ensembles in unfolding pathway of the N-terminal domain of TDP-43." RSC Advances 8, no. 35 (2018): 19835–45. http://dx.doi.org/10.1039/c8ra03368d.
Повний текст джерелаAuerbach, Marcy R., Kristy R. Brown, and Ila R. Singh. "Mutational Analysis of the N-Terminal Domain of Moloney Murine Leukemia Virus Capsid Protein." Journal of Virology 81, no. 22 (September 12, 2007): 12337–47. http://dx.doi.org/10.1128/jvi.01286-07.
Повний текст джерелаChi, Xiangyang, Renhong Yan, Jun Zhang, Guanying Zhang, Yuanyuan Zhang, Meng Hao, Zhe Zhang, et al. "A neutralizing human antibody binds to the N-terminal domain of the Spike protein of SARS-CoV-2." Science 369, no. 6504 (June 22, 2020): 650–55. http://dx.doi.org/10.1126/science.abc6952.
Повний текст джерелаKroetz, Mary B., Dan Su, and Mark Hochstrasser. "Essential Role of Nuclear Localization for Yeast Ulp2 SUMO Protease Function." Molecular Biology of the Cell 20, no. 8 (April 15, 2009): 2196–206. http://dx.doi.org/10.1091/mbc.e08-10-1090.
Повний текст джерелаChang, Chung-Ke, Yen-Lan Hsu, Yuan-Hsiang Chang, Fa-An Chao, Ming-Chya Wu, Yu-Shan Huang, Chin-Kun Hu, and Tai-Huang Huang. "Multiple Nucleic Acid Binding Sites and Intrinsic Disorder of Severe Acute Respiratory Syndrome Coronavirus Nucleocapsid Protein: Implications for Ribonucleocapsid Protein Packaging." Journal of Virology 83, no. 5 (December 3, 2008): 2255–64. http://dx.doi.org/10.1128/jvi.02001-08.
Повний текст джерелаDavenport, Kristen A., Davin M. Henderson, Candace K. Mathiason, and Edward A. Hoover. "Assessment of the PrP c Amino-Terminal Domain in Prion Species Barriers." Journal of Virology 90, no. 23 (September 21, 2016): 10752–61. http://dx.doi.org/10.1128/jvi.01121-16.
Повний текст джерелаAirola, Michael V., Prajna Shanbhogue, Achraf A. Shamseddine, Kip E. Guja, Can E. Senkal, Rohan Maini, Nana Bartke, et al. "Structure of human nSMase2 reveals an interdomain allosteric activation mechanism for ceramide generation." Proceedings of the National Academy of Sciences 114, no. 28 (June 26, 2017): E5549—E5558. http://dx.doi.org/10.1073/pnas.1705134114.
Повний текст джерелаVREULS, Christelle, Patrice FILÉE, Hélène VAN MELCKEBEKE, Tony AERTS, Peter DE DEYN, Gabriel LLABRÈS, André MATAGNE, Jean-Pierre SIMORRE, Jean-Marie FRÈRE, and Bernard JORIS. "Guanidinium chloride denaturation of the dimeric Bacillus licheniformis BlaI repressor highlights an independent domain unfolding pathway." Biochemical Journal 384, no. 1 (November 9, 2004): 179–90. http://dx.doi.org/10.1042/bj20040658.
Повний текст джерелаBerkowitz, Reed L., and David A. Ostrov. "The Elusive Coreceptors for the SARS-CoV-2 Spike Protein." Viruses 15, no. 1 (December 25, 2022): 67. http://dx.doi.org/10.3390/v15010067.
Повний текст джерелаMoretti, Matteo, Isabella Marzi, Cristina Cantarutti, Mirella Vivoli Vega, Walter Mandaliti, Maria Chiara Mimmi, Francesco Bemporad, Alessandra Corazza, and Fabrizio Chiti. "Conversion of the Native N-Terminal Domain of TDP-43 into a Monomeric Alternative Fold with Lower Aggregation Propensity." Molecules 27, no. 13 (July 5, 2022): 4309. http://dx.doi.org/10.3390/molecules27134309.
Повний текст джерелаValášek, Leoš, Klaus H. Nielsen, Fan Zhang, Christie A. Fekete, and Alan G. Hinnebusch. "Interactions of Eukaryotic Translation Initiation Factor 3 (eIF3) Subunit NIP1/c with eIF1 and eIF5 Promote Preinitiation Complex Assembly and Regulate Start Codon Selection." Molecular and Cellular Biology 24, no. 21 (November 1, 2004): 9437–55. http://dx.doi.org/10.1128/mcb.24.21.9437-9455.2004.
Повний текст джерелаJi, Xinhua. "RNA Biogenesis: Mechanism and Evolution of RNase III." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C210. http://dx.doi.org/10.1107/s2053273314097897.
Повний текст джерелаWolf, Nina M., Hyun Lee, Daniel Zagal, Joo-Won Nam, Dong-Chan Oh, Hanki Lee, Joo-Won Suh, Guido F. Pauli, Sanghyun Cho, and Celerino Abad-Zapatero. "Structure of the N-terminal domain of ClpC1 in complex with the antituberculosis natural product ecumicin reveals unique binding interactions." Acta Crystallographica Section D Structural Biology 76, no. 5 (April 23, 2020): 458–71. http://dx.doi.org/10.1107/s2059798320004027.
Повний текст джерелаObst, Jon K., Nasrin R. Mawji, Simon J. L. Teskey, Jun Wang, and Marianne D. Sadar. "Differential Gene Expression Profiles between N-Terminal Domain and Ligand-Binding Domain Inhibitors of Androgen Receptor Reveal Ralaniten Induction of Metallothionein by a Mechanism Dependent on MTF1." Cancers 14, no. 2 (January 13, 2022): 386. http://dx.doi.org/10.3390/cancers14020386.
Повний текст джерелаZhou, Fujun, Sarah E. Walker, Sarah F. Mitchell, Jon R. Lorsch, and Alan G. Hinnebusch. "Identification and Characterization of Functionally Critical, Conserved Motifs in the Internal Repeats and N-terminal Domain of Yeast Translation Initiation Factor 4B (yeIF4B)." Journal of Biological Chemistry 289, no. 3 (November 27, 2013): 1704–22. http://dx.doi.org/10.1074/jbc.m113.529370.
Повний текст джерелаKumar, Raj, Jenna F. DuMond, Shagufta H. Khan, E. Brad Thompson, Yi He, Maurice B. Burg, and Joan D. Ferraris. "NFAT5, which protects against hypertonicity, is activated by that stress via structuring of its intrinsically disordered domain." Proceedings of the National Academy of Sciences 117, no. 33 (August 3, 2020): 20292–97. http://dx.doi.org/10.1073/pnas.1911680117.
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