Статті в журналах з теми "Homodimers"
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Krause, Jean-Michel, Peter Berger, Jordi Roig, Vinod Singh та Wolfgang E. Merz. "Rapid Maturation of Glycoprotein Hormone Free α-Subunit (GPHα) and GPHαα Homodimers". Molecular Endocrinology 21, № 10 (1 жовтня 2007): 2551–64. http://dx.doi.org/10.1210/me.2007-0051.
Повний текст джерелаHadarovich, A. Y., A. A. Kalinouski, and A. V. Tuzikov. "Protein homodimers structure prediction based on deep neural network." Informatics 17, no. 2 (June 26, 2020): 44–53. http://dx.doi.org/10.37661/1816-0301-2020-17-2-44-53.
Повний текст джерелаGeng, Jie, та Malini Raghavan. "CD8αα homodimers function as a coreceptor for KIR3DL1". Proceedings of the National Academy of Sciences 116, № 36 (16 серпня 2019): 17951–56. http://dx.doi.org/10.1073/pnas.1905943116.
Повний текст джерелаTajer, Benjamin, James A. Dutko, Shawn C. Little, and Mary C. Mullins. "BMP heterodimers signal via distinct type I receptor class functions." Proceedings of the National Academy of Sciences 118, no. 15 (April 7, 2021): e2017952118. http://dx.doi.org/10.1073/pnas.2017952118.
Повний текст джерелаPeng, K.-C., D. Puett, and J. M. Brewer. "Homodimer formation by the individual subunits of bovine lutropin as determined by sedimentation equilibrium." Journal of Molecular Endocrinology 18, no. 3 (June 1997): 259–65. http://dx.doi.org/10.1677/jme.0.0180259.
Повний текст джерелаGarton, Michael, Stephen S. MacKinnon, Anatoly Malevanets, and Shoshana J. Wodak. "Interplay of self-association and conformational flexibility in regulating protein function." Philosophical Transactions of the Royal Society B: Biological Sciences 373, no. 1749 (May 7, 2018): 20170190. http://dx.doi.org/10.1098/rstb.2017.0190.
Повний текст джерелаCampbell, Brandon, Marharyta Petukh, Emil Alexov, and Chuan Li. "On the electrostatic properties of homodimeric proteins." Journal of Theoretical and Computational Chemistry 13, no. 03 (May 2014): 1440007. http://dx.doi.org/10.1142/s0219633614400070.
Повний текст джерелаIbrahim, Mahmoud A. A., Rehab R. A. Saeed, Mohammed N. I. Shehata, Muhammad Naeem Ahmed, Ahmed M. Shawky, Manal M. Khowdiary, Eslam B. Elkaeed, Mahmoud E. S. Soliman, and Nayra A. M. Moussa. "Type I–IV Halogen⋯Halogen Interactions: A Comparative Theoretical Study in Halobenzene⋯Halobenzene Homodimers." International Journal of Molecular Sciences 23, no. 6 (March 14, 2022): 3114. http://dx.doi.org/10.3390/ijms23063114.
Повний текст джерелаBonsor, Daniel A., Sebastian Günther, Robert Beadenkopf, Dorothy Beckett, and Eric J. Sundberg. "Diverse oligomeric states of CEACAM IgV domains." Proceedings of the National Academy of Sciences 112, no. 44 (October 19, 2015): 13561–66. http://dx.doi.org/10.1073/pnas.1509511112.
Повний текст джерелаMou, Yun, Po-Ssu Huang, Fang-Ciao Hsu, Shing-Jong Huang, and Stephen L. Mayo. "Computational design and experimental verification of a symmetric protein homodimer." Proceedings of the National Academy of Sciences 112, no. 34 (August 12, 2015): 10714–19. http://dx.doi.org/10.1073/pnas.1505072112.
Повний текст джерелаHwang, Eunha, Hae-Kap Cheong, Ameeq Ul Mushtaq, Hye-Yeon Kim, Kwon Joo Yeo, Eunhee Kim, Woo Cheol Lee, Kwang Yeon Hwang, Chaejoon Cheong, and Young Ho Jeon. "Structural basis of the heterodimerization of the MST and RASSF SARAH domains in the Hippo signalling pathway." Acta Crystallographica Section D Biological Crystallography 70, no. 7 (June 29, 2014): 1944–53. http://dx.doi.org/10.1107/s139900471400947x.
Повний текст джерелаNeugebauer, Judith M., Sunjong Kwon, Hyung-Seok Kim, Nathan Donley, Anup Tilak, Shailaja Sopory, and Jan L. Christian. "The prodomain of BMP4 is necessary and sufficient to generate stable BMP4/7 heterodimers with enhanced bioactivity in vivo." Proceedings of the National Academy of Sciences 112, no. 18 (April 20, 2015): E2307—E2316. http://dx.doi.org/10.1073/pnas.1501449112.
Повний текст джерелаThompson, PD, LS Remus, JC Hsieh, PW Jurutka, GK Whitfield, MA Galligan, C. Encinas Dominguez, CA Haussler, and MR Haussler. "Distinct retinoid X receptor activation function-2 residues mediate transactivation in homodimeric and vitamin D receptor heterodimeric contexts." Journal of Molecular Endocrinology 27, no. 2 (October 1, 2001): 211–27. http://dx.doi.org/10.1677/jme.0.0270211.
Повний текст джерелаLiss, Andrew S., and Henry R. Bose,. "Mutational Analysis of the v-Rel Dimerization Interface Reveals a Critical Role for v-Rel Homodimers in Transformation." Journal of Virology 76, no. 10 (May 15, 2002): 4928–39. http://dx.doi.org/10.1128/jvi.76.10.4928-4939.2002.
Повний текст джерелаPeckys, Diana B., Ulrike Korf, and Niels de Jonge. "Local variations of HER2 dimerization in breast cancer cells discovered by correlative fluorescence and liquid electron microscopy." Science Advances 1, no. 6 (July 2015): e1500165. http://dx.doi.org/10.1126/sciadv.1500165.
Повний текст джерелаZhang, X. K., G. Salbert, M. O. Lee, and M. Pfahl. "Mutations that alter ligand-induced switches and dimerization activities in the retinoid X receptor." Molecular and Cellular Biology 14, no. 6 (June 1994): 4311–23. http://dx.doi.org/10.1128/mcb.14.6.4311-4323.1994.
Повний текст джерелаZhang, X. K., G. Salbert, M. O. Lee, and M. Pfahl. "Mutations that alter ligand-induced switches and dimerization activities in the retinoid X receptor." Molecular and Cellular Biology 14, no. 6 (June 1994): 4311–23. http://dx.doi.org/10.1128/mcb.14.6.4311.
Повний текст джерелаKrouwels, Anita, Juvita D. Iljas, Angela H. M. Kragten, Wouter J. A. Dhert, F. Cumhur Öner, Marianna A. Tryfonidou, and Laura B. Creemers. "Bone Morphogenetic Proteins for Nucleus Pulposus Regeneration." International Journal of Molecular Sciences 21, no. 8 (April 14, 2020): 2720. http://dx.doi.org/10.3390/ijms21082720.
Повний текст джерелаVidilaseris, Keni, Alexandros Kiriazis, Ainoleena Turku, Ayman Khattab, Niklas G. Johansson, Teppo O. Leino, Paula S. Kiuru, et al. "Asymmetry in catalysis by Thermotoga maritima membrane-bound pyrophosphatase demonstrated by a nonphosphorus allosteric inhibitor." Science Advances 5, no. 5 (May 2019): eaav7574. http://dx.doi.org/10.1126/sciadv.aav7574.
Повний текст джерелаIvanov, Yuri D., Amir Taldaev, Andrey V. Lisitsa, Elena A. Ponomarenko, and Alexander I. Archakov. "Prediction of Monomeric and Dimeric Structures of CYP102A1 Using AlphaFold2 and AlphaFold Multimer and Assessment of Point Mutation Effect on the Efficiency of Intra- and Interprotein Electron Transfer." Molecules 27, no. 4 (February 18, 2022): 1386. http://dx.doi.org/10.3390/molecules27041386.
Повний текст джерелаGanchi, P. A., S. C. Sun, W. C. Greene, and D. W. Ballard. "A novel NF-kappa B complex containing p65 homodimers: implications for transcriptional control at the level of subunit dimerization." Molecular and Cellular Biology 13, no. 12 (December 1993): 7826–35. http://dx.doi.org/10.1128/mcb.13.12.7826-7835.1993.
Повний текст джерелаGanchi, P. A., S. C. Sun, W. C. Greene, and D. W. Ballard. "A novel NF-kappa B complex containing p65 homodimers: implications for transcriptional control at the level of subunit dimerization." Molecular and Cellular Biology 13, no. 12 (December 1993): 7826–35. http://dx.doi.org/10.1128/mcb.13.12.7826.
Повний текст джерелаGresock, Michael G., Kyle A. Kastead, and Kathleen Postle. "From Homodimer to Heterodimer and Back: Elucidating the TonB Energy Transduction Cycle." Journal of Bacteriology 197, no. 21 (August 17, 2015): 3433–45. http://dx.doi.org/10.1128/jb.00484-15.
Повний текст джерелаCheskis, B., and L. P. Freedman. "Ligand modulates the conversion of DNA-bound vitamin D3 receptor (VDR) homodimers into VDR-retinoid X receptor heterodimers." Molecular and Cellular Biology 14, no. 5 (May 1994): 3329–38. http://dx.doi.org/10.1128/mcb.14.5.3329-3338.1994.
Повний текст джерелаCheskis, B., and L. P. Freedman. "Ligand modulates the conversion of DNA-bound vitamin D3 receptor (VDR) homodimers into VDR-retinoid X receptor heterodimers." Molecular and Cellular Biology 14, no. 5 (May 1994): 3329–38. http://dx.doi.org/10.1128/mcb.14.5.3329.
Повний текст джерелаLiu, Ying, Yue Zhang, Jing Jiang, Peter E. Lobie, Ramasamy Paulmurugan, John F. Langenheim, Wen Y. Chen, Kurt R. Zinn, and Stuart J. Frank. "GHR/PRLR Heteromultimer Is Composed of GHR Homodimers and PRLR Homodimers." Molecular Endocrinology 30, no. 5 (May 2016): 504–17. http://dx.doi.org/10.1210/me.2015-1319.
Повний текст джерелаBarkalow, Fern J., Kurt L. Barkalow, and Tanya N. Mayadas. "Dimerization of P-selectin in platelets and endothelial cells." Blood 96, no. 9 (November 1, 2000): 3070–77. http://dx.doi.org/10.1182/blood.v96.9.3070.
Повний текст джерелаBarkalow, Fern J., Kurt L. Barkalow, and Tanya N. Mayadas. "Dimerization of P-selectin in platelets and endothelial cells." Blood 96, no. 9 (November 1, 2000): 3070–77. http://dx.doi.org/10.1182/blood.v96.9.3070.h8003070_3070_3077.
Повний текст джерелаNakayama, K., H. Shimizu, K. Mitomo, T. Watanabe, S. Okamoto, and K. Yamamoto. "A lymphoid cell-specific nuclear factor containing c-Rel-like proteins preferentially interacts with interleukin-6 kappa B-related motifs whose activities are repressed in lymphoid cells." Molecular and Cellular Biology 12, no. 4 (April 1992): 1736–46. http://dx.doi.org/10.1128/mcb.12.4.1736-1746.1992.
Повний текст джерелаNakayama, K., H. Shimizu, K. Mitomo, T. Watanabe, S. Okamoto, and K. Yamamoto. "A lymphoid cell-specific nuclear factor containing c-Rel-like proteins preferentially interacts with interleukin-6 kappa B-related motifs whose activities are repressed in lymphoid cells." Molecular and Cellular Biology 12, no. 4 (April 1992): 1736–46. http://dx.doi.org/10.1128/mcb.12.4.1736.
Повний текст джерелаSun, J., and P. B. Kavathas. "Comparison of the roles of CD8 alpha alpha and CD8 alpha beta in interaction with MHC class I." Journal of Immunology 159, no. 12 (December 15, 1997): 6077–82. http://dx.doi.org/10.4049/jimmunol.159.12.6077.
Повний текст джерелаSINHA, Dipali, Mariola MARCINKIEWICZ, David GAILANI, and Peter N. WALSH. "Molecular cloning and biochemical characterization of rabbit factor XI." Biochemical Journal 367, no. 1 (October 1, 2002): 49–56. http://dx.doi.org/10.1042/bj20020232.
Повний текст джерелаTakeshita, Akira, Yasunori Ozawa, and William W. Chin. "Nuclear Receptor Coactivators Facilitate Vitamin D Receptor Homodimer Action on Direct Repeat Hormone Response Elements." Endocrinology 141, no. 3 (March 1, 2000): 1281–84. http://dx.doi.org/10.1210/endo.141.3.7441.
Повний текст джерелаMagyar, Csaba, Anikó Mentes, Erzsébet Fichó, Miklós Cserző, and István Simon. "Physical Background of the Disordered Nature of “Mutual Synergetic Folding” Proteins." International Journal of Molecular Sciences 19, no. 11 (October 26, 2018): 3340. http://dx.doi.org/10.3390/ijms19113340.
Повний текст джерелаHeinzel, F. P., A. M. Hujer, F. N. Ahmed, and R. M. Rerko. "In vivo production and function of IL-12 p40 homodimers." Journal of Immunology 158, no. 9 (May 1, 1997): 4381–88. http://dx.doi.org/10.4049/jimmunol.158.9.4381.
Повний текст джерелаWatowich, S. S., D. J. Hilton, and H. F. Lodish. "Activation and inhibition of erythropoietin receptor function: role of receptor dimerization." Molecular and Cellular Biology 14, no. 6 (June 1994): 3535–49. http://dx.doi.org/10.1128/mcb.14.6.3535-3549.1994.
Повний текст джерелаWatowich, S. S., D. J. Hilton, and H. F. Lodish. "Activation and inhibition of erythropoietin receptor function: role of receptor dimerization." Molecular and Cellular Biology 14, no. 6 (June 1994): 3535–49. http://dx.doi.org/10.1128/mcb.14.6.3535.
Повний текст джерелаCaillat, Christophe, Alexander Fish, Dafni-Eleftheria Pefani, Stavros Taraviras, Zoi Lygerou, and Anastassis Perrakis. "The structure of the GemC1 coiled coil and its interaction with the Geminin family of coiled-coil proteins." Acta Crystallographica Section D Biological Crystallography 71, no. 11 (October 31, 2015): 2278–86. http://dx.doi.org/10.1107/s1399004715016892.
Повний текст джерелаKristensen, Kristian K., Katrine Zinck Leth-Espensen, Haydyn D. T. Mertens, Gabriel Birrane, Muthuraman Meiyappan, Gunilla Olivecrona, Thomas J. D. Jørgensen, Stephen G. Young, and Michael Ploug. "Unfolding of monomeric lipoprotein lipase by ANGPTL4: Insight into the regulation of plasma triglyceride metabolism." Proceedings of the National Academy of Sciences 117, no. 8 (February 7, 2020): 4337–46. http://dx.doi.org/10.1073/pnas.1920202117.
Повний текст джерелаMarui, Nobuyuki, Russell M. Medford та Mushtaq Ahmad. "Activation of RelA homodimers by tumour necrosis factor α: a possible transcriptional activator in human vascular endothelial cells". Biochemical Journal 390, № 1 (9 серпня 2005): 317–24. http://dx.doi.org/10.1042/bj20041659.
Повний текст джерелаAllen, Rachel L., Chris A. O’Callaghan, Andrew J. McMichael та Paul Bowness. "Cutting Edge: HLA-B27 Can Form a Novel β2-Microglobulin-Free Heavy Chain Homodimer Structure". Journal of Immunology 162, № 9 (1 травня 1999): 5045–48. http://dx.doi.org/10.4049/jimmunol.162.9.5045.
Повний текст джерелаMuthuswamy, Senthil K., Michael Gilman, and Joan S. Brugge. "Controlled Dimerization of ErbB Receptors Provides Evidence for Differential Signaling by Homo- and Heterodimers." Molecular and Cellular Biology 19, no. 10 (October 1, 1999): 6845–57. http://dx.doi.org/10.1128/mcb.19.10.6845.
Повний текст джерелаInukai, T., T. Inaba, T. Yoshihara, and A. T. Look. "Cell transformation mediated by homodimeric E2A-HLF transcription factors." Molecular and Cellular Biology 17, no. 3 (March 1997): 1417–24. http://dx.doi.org/10.1128/mcb.17.3.1417.
Повний текст джерелаGhetie, Maria-Ana, Helen Bright, and Ellen S. Vitetta. "Homodimers but not monomers of Rituxan (chimeric anti-CD20) induce apoptosis in human B-lymphoma cells and synergize with a chemotherapeutic agent and an immunotoxin." Blood 97, no. 5 (March 1, 2001): 1392–98. http://dx.doi.org/10.1182/blood.v97.5.1392.
Повний текст джерелаStaudt, Ryan P., and Thomas E. Smithgall. "Nef homodimers down-regulate SERINC5 by AP-2–mediated endocytosis to promote HIV-1 infectivity." Journal of Biological Chemistry 295, no. 46 (September 1, 2020): 15540–52. http://dx.doi.org/10.1074/jbc.ra120.014668.
Повний текст джерелаWang, Jun, Marek W. Radomski, Carlos Medina, and John F. Gilmer. "MMP inhibition by barbiturate homodimers." Bioorganic & Medicinal Chemistry Letters 23, no. 2 (January 2013): 444–47. http://dx.doi.org/10.1016/j.bmcl.2012.11.063.
Повний текст джерелаKubo, Ken-ichiro, Katsuhiko Mikoshiba, and Kazunori Nakajima. "Secreted Reelin molecules form homodimers." Neuroscience Research 43, no. 4 (August 2002): 381–88. http://dx.doi.org/10.1016/s0168-0102(02)00068-8.
Повний текст джерелаBardsley, Ben, Younghoon R. Cho, Martin S. Westwell, and Dudley H. Williams. "Induction of asymmetry into homodimers." Chirality 10, no. 12 (1998): 14–23. http://dx.doi.org/10.1002/(sici)1520-636x(1998)10:1/2<14::aid-chir4>3.3.co;2-v.
Повний текст джерелаBardsley, Ben, Younghoon R. Cho, Martin S. Westwell, and Dudley H. Williams. "Induction of asymmetry into homodimers." Chirality 10, no. 1-2 (1998): 14–23. http://dx.doi.org/10.1002/chir.4.
Повний текст джерелаKundrotas, Petras J., Ilya A. Vakser, and Joël Janin. "Structural templates for modeling homodimers." Protein Science 22, no. 11 (September 20, 2013): 1655–63. http://dx.doi.org/10.1002/pro.2361.
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