Статті в журналах з теми "Peptide loading"
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Liu, Bai, Lijing You, Kaiping Han, Hyung-il Lee, Peter Rhode, Sarah Henrickson, Ulrich H. von Andrian, and Hing C. Wong. "Peptide-loading enhancement for antigen presenting cells (93.6)." Journal of Immunology 178, no. 1_Supplement (April 1, 2007): S167. http://dx.doi.org/10.4049/jimmunol.178.supp.93.6.
Повний текст джерелаZernich, Danielle, Anthony W. Purcell, Whitney A. Macdonald, Lars Kjer-Nielsen, Lauren K. Ely, Nihay Laham, Tanya Crockford, et al. "Natural HLA Class I Polymorphism Controls the Pathway of Antigen Presentation and Susceptibility to Viral Evasion." Journal of Experimental Medicine 200, no. 1 (June 28, 2004): 13–24. http://dx.doi.org/10.1084/jem.20031680.
Повний текст джерелаMorozov, Giora I., Huaying Zhao, Michael G. Mage, Lisa F. Boyd, Jiansheng Jiang, Michael A. Dolan, Ramesh Venna, et al. "Interaction of TAPBPR, a tapasin homolog, with MHC-I molecules promotes peptide editing." Proceedings of the National Academy of Sciences 113, no. 8 (February 11, 2016): E1006—E1015. http://dx.doi.org/10.1073/pnas.1519894113.
Повний текст джерелаVatner, Ralph Eric, and Pramod K. Srivastava. "The TCP-1 Ring Complex (TRiC) binds antigenic peptides and facilitates their cross-presentation by APCs (93.5)." Journal of Immunology 178, no. 1_Supplement (April 1, 2007): S166. http://dx.doi.org/10.4049/jimmunol.178.supp.93.5.
Повний текст джерелаHafstrand, Ida, Ece Canan Sayitoglu, Anca Apavaloaei, Benjamin John Josey, Renhua Sun, Xiao Han, Sara Pellegrino, et al. "Successive crystal structure snapshots suggest the basis for MHC class I peptide loading and editing by tapasin." Proceedings of the National Academy of Sciences 116, no. 11 (February 26, 2019): 5055–60. http://dx.doi.org/10.1073/pnas.1807656116.
Повний текст джерелаBadrinath, Soumya, Heike Kunze-Schumacher, Rainer Blasczyk, Trevor Huyton, and Christina Bade-Doeding. "A Micropolymorphism Altering the Residue Triad 97/114/156 Determines the Relative Levels of Tapasin Independence and Distinct Peptide Profiles for HLA-A*24 Allotypes." Journal of Immunology Research 2014 (2014): 1–12. http://dx.doi.org/10.1155/2014/298145.
Повний текст джерелаYuan, Xin, Yingzhou Qin, Qingmei Tian, Cuijuan Liu, Xiangzhou Meng, Bo Qie, Fan Gao, et al. "Smart delivery of poly-peptide composite for effective cancer therapy." Biomedical Materials 17, no. 2 (January 24, 2022): 024103. http://dx.doi.org/10.1088/1748-605x/ac494c.
Повний текст джерелаIlca, F. Tudor, Andreas Neerincx, Mark R. Wills, Maike de la Roche, and Louise H. Boyle. "Utilizing TAPBPR to promote exogenous peptide loading onto cell surface MHC I molecules." Proceedings of the National Academy of Sciences 115, no. 40 (September 13, 2018): E9353—E9361. http://dx.doi.org/10.1073/pnas.1809465115.
Повний текст джерелаSette, A., S. Southwood, J. Miller, and E. Appella. "Binding of major histocompatibility complex class II to the invariant chain-derived peptide, CLIP, is regulated by allelic polymorphism in class II." Journal of Experimental Medicine 181, no. 2 (February 1, 1995): 677–83. http://dx.doi.org/10.1084/jem.181.2.677.
Повний текст джерелаBednarek, M. A., S. Y. Sauma, M. C. Gammon, G. Porter, S. Tamhankar, A. R. Williamson, and H. J. Zweerink. "The minimum peptide epitope from the influenza virus matrix protein. Extra and intracellular loading of HLA-A2." Journal of Immunology 147, no. 12 (December 15, 1991): 4047–53. http://dx.doi.org/10.4049/jimmunol.147.12.4047.
Повний текст джерелаSilva-Flannery, Luciana M., Monica Cabrera-Mora, Megan Dickherber, and Alberto Moreno. "Polymeric Linear Peptide Chimeric Vaccine-Induced Antimalaria Immunity Is Associated with Enhanced In Vitro Antigen Loading." Infection and Immunity 77, no. 5 (February 23, 2009): 1798–806. http://dx.doi.org/10.1128/iai.00470-08.
Повний текст джерелаShi, Guo-Ping, Rebecca A. R. Bryant, Richard Riese, Steven Verhelst, Christoph Driessen, Zhenqiang Li, Dieter Bromme, Hidde L. Ploegh, and Harold A. Chapman. "Role for Cathepsin F in Invariant Chain Processing and Major Histocompatibility Complex Class II Peptide Loading by Macrophages." Journal of Experimental Medicine 191, no. 7 (April 3, 2000): 1177–86. http://dx.doi.org/10.1084/jem.191.7.1177.
Повний текст джерелаNatarajan, Kannan, Jiansheng Jiang, Lisa F. Boyd, Giora I. Morozov, Michael G. Mage, and David H. Margulies. "Insights into MHC-I peptide loading obtained from the structure of a TAPBPR/MHC-I complex." Journal of Immunology 198, no. 1_Supplement (May 1, 2017): 146.25. http://dx.doi.org/10.4049/jimmunol.198.supp.146.25.
Повний текст джерелаMorozov, Giora, Huaying Zhao, Michael Mage, Lisa Boyd, Ramesh Venna, Michael Norcross, Curtis McMurtrey, et al. "Direct interaction of recombinant TAPBPR with MHC-I molecules: stabilization of peptide-free MHC-I promotes high affinity peptide loading (APP5P.102)." Journal of Immunology 194, no. 1_Supplement (May 1, 2015): 183.4. http://dx.doi.org/10.4049/jimmunol.194.supp.183.4.
Повний текст джерелаObuobi, Sybil, Venkatesh Mayandi, Nurul Azlyn Mohd Nor, Benedict Jiasheng Lee, Rajamani Lakshminarayanan, and Pui Lai Rachel Ee. "Nucleic acid peptide nanogels for the treatment of bacterial keratitis." Nanoscale 12, no. 33 (2020): 17411–25. http://dx.doi.org/10.1039/d0nr03095c.
Повний текст джерелаSuh, Woong-Kyung, Michael A. Derby, Myrna F. Cohen-Doyle, Gary J. Schoenhals, Klaus Früh, Jay A. Berzofsky та David B. Williams. "Interaction of Murine MHC Class I Molecules with Tapasin and TAP Enhances Peptide Loading and Involves the Heavy Chain α3 Domain". Journal of Immunology 162, № 3 (1 лютого 1999): 1530–40. http://dx.doi.org/10.4049/jimmunol.162.3.1530.
Повний текст джерелаSgourakis, Nikolaos, Andrew C. McShan, Kannan Natarajan, Vlad K. Kumirov, David Flores-Solis, Jiansheng Jiang, Mareike Badstuebner, Evgenii L. Kovrigin, and David H. Margulies. "Chaperone-assisted peptide exchange on MHC-I is driven by a negative allostery release cycle: Implications for a role of peptide-editing Molecular Chaperones in scrutinizing the peptide repertoire." Journal of Immunology 200, no. 1_Supplement (May 1, 2018): 99.23. http://dx.doi.org/10.4049/jimmunol.200.supp.99.23.
Повний текст джерелаStang, Espen, Carolyn B. Guerra, Miguel Amaya, Yvonne Paterson, Oddmund Bakke, and Elizabeth D. Mellins. "DR/CLIP (Class II-Associated Invariant Chain Peptides) and DR/Peptide Complexes Colocalize in Prelysosomes in Human B Lymphoblastoid Cells." Journal of Immunology 160, no. 10 (May 15, 1998): 4696–707. http://dx.doi.org/10.4049/jimmunol.160.10.4696.
Повний текст джерелаBraun, Katharina, Christina M. Stürzel, Frank Kirchhoff, and Mika Lindén. "In Vitro Evaluation of a Peptide-Mesoporous Silica Nanoparticle Drug Release System against HIV-1." Inorganics 8, no. 7 (July 13, 2020): 42. http://dx.doi.org/10.3390/inorganics8070042.
Повний текст джерелаWearsch, Pamela, Wei Zhang, and Peter Cresswell. "Essential glycan-dependent interactions optimize MHC class I peptide loading (100.51)." Journal of Immunology 186, no. 1_Supplement (April 1, 2011): 100.51. http://dx.doi.org/10.4049/jimmunol.186.supp.100.51.
Повний текст джерелаBrumeanu, T. D., W. J. Swiggard, R. M. Steinman, C. A. Bona, and H. Zaghouani. "Efficient loading of identical viral peptide onto class II molecules by antigenized immunoglobulin and influenza virus." Journal of Experimental Medicine 178, no. 5 (November 1, 1993): 1795–99. http://dx.doi.org/10.1084/jem.178.5.1795.
Повний текст джерелаMorozov, Giora, Huaying Zhao, Michael Mage, Lisa Boyd, Peter Schuck, Kannan Natarajan та David Margulies. "Tapasin-related protein TAPBPR interacts directly with peptide-free MHC-I/β2-microgolbulin complexes (APP3P.101)". Journal of Immunology 192, № 1_Supplement (1 травня 2014): 111.2. http://dx.doi.org/10.4049/jimmunol.192.supp.111.2.
Повний текст джерелаMcCully, Mark, Macarena Sanchez-Navarro, Meritxell Teixido, and Ernest Giralt. "Peptide Mediated Brain Delivery of Nano- and Submicroparticles: A Synergistic Approach." Current Pharmaceutical Design 24, no. 13 (July 11, 2018): 1366–76. http://dx.doi.org/10.2174/1381612824666171201115126.
Повний текст джерелаBenham, A. M., and J. J. Neefjes. "Proteasome activity limits the assembly of MHC class I molecules after IFN-gamma stimulation." Journal of Immunology 159, no. 12 (December 15, 1997): 5896–904. http://dx.doi.org/10.4049/jimmunol.159.12.5896.
Повний текст джерелаJiang, Jiansheng, Kannan Natarajan, Ellen Kim, Javeed A. Dhobi, Michael G. Mage, Lisa F. Boyd, and David H. Margulies. "Structural Insights into the Mechanism(s) of Peptide Loading in MHC-I dependent Antigen Presentation." Journal of Immunology 204, no. 1_Supplement (May 1, 2020): 140.9. http://dx.doi.org/10.4049/jimmunol.204.supp.140.9.
Повний текст джерелаDe Luca, Maria, Rosa Gaglione, Bartolomeo Della Ventura, Angela Cesaro, Rocco Di Girolamo, Raffaele Velotta, and Angela Arciello. "Loading of Polydimethylsiloxane with a Human ApoB-Derived Antimicrobial Peptide to Prevent Bacterial Infections." International Journal of Molecular Sciences 23, no. 9 (May 7, 2022): 5219. http://dx.doi.org/10.3390/ijms23095219.
Повний текст джерелаMage, Michael, Rui Wang, Lisa Boyd, Maria Revilleza, Kannan Natarajan, Ted Hansen, and David Margulies. "Conformation and solvent-accessibility of an MHC-I alpha-1 domain segment provide insight into the peptide receptive transition state (100.6)." Journal of Immunology 186, no. 1_Supplement (April 1, 2011): 100.6. http://dx.doi.org/10.4049/jimmunol.186.supp.100.6.
Повний текст джерелаFelt, V. "C-Peptide during Glucose Loading in Myxedema." Hormone and Metabolic Research 20, no. 06 (June 1988): 375. http://dx.doi.org/10.1055/s-2007-1010839.
Повний текст джерелаUlbrecht, Matthias, Susanne Modrow, Rakesh Srivastava, Per A. Peterson, and Elisabeth H. Weiss. "Interaction of HLA-E with Peptides and the Peptide Transporter In Vitro: Implications for its Function in Antigen Presentation." Journal of Immunology 160, no. 9 (May 1, 1998): 4375–85. http://dx.doi.org/10.4049/jimmunol.160.9.4375.
Повний текст джерелаLee, Sungwook, Boyoun Park, Kwonyoon Kang, and Kwangseog Ahn. "Redox-regulated Export of the Major Histocompatibility Complex Class I-Peptide Complexes from the Endoplasmic Reticulum." Molecular Biology of the Cell 20, no. 14 (July 15, 2009): 3285–94. http://dx.doi.org/10.1091/mbc.e09-03-0238.
Повний текст джерелаEggensperger, Sabine, and Robert Tampé. "The transporter associated with antigen processing: a key player in adaptive immunity." Biological Chemistry 396, no. 9-10 (September 1, 2015): 1059–72. http://dx.doi.org/10.1515/hsz-2014-0320.
Повний текст джерелаArshad, Najla, Nathalie Vigneron, Cansu Cimen Bozkus, Vincent Stroobant, Stefan Naulaerts, Nina Bhardwaj, Benoît Van den Eynde, and Peter Cresswell. "Abstract 1379: Discovery of tumor-associated, immunogenic peptides presented in a patient-derived, mutant calreticulin-driven myeloproliferative neoplasm cell line." Cancer Research 82, no. 12_Supplement (June 15, 2022): 1379. http://dx.doi.org/10.1158/1538-7445.am2022-1379.
Повний текст джерелаFerrari, Giorgio, Andrew M. Knight, Colin Watts, and Jean Pieters. "Distinct Intracellular Compartments Involved in Invariant Chain Degradation and Antigenic Peptide Loading of Major Histocompatibility Complex (MHC) Class II Molecules." Journal of Cell Biology 139, no. 6 (December 15, 1997): 1433–46. http://dx.doi.org/10.1083/jcb.139.6.1433.
Повний текст джерелаGeng, Jie, Irina Pogozheva, and Malini Raghavan. "Use of functional polymorphisms to elucidate the peptide binding site of the transporter associated with antigen processing (TAP) complexes (APP5P.101)." Journal of Immunology 194, no. 1_Supplement (May 1, 2015): 183.3. http://dx.doi.org/10.4049/jimmunol.194.supp.183.3.
Повний текст джерелаMaharani, Rani, Dessy Yulyani Kurnia, Ace Tatang Hidayat, Jamaludin Al-Anshori, Dadan Sumiarsa, Desi Harneti, and Nurlelasari Nurlelasari. "Upaya Optimasi Sintesis Pentapeptida Leu-Ala-Asn-Ala-Lys dengan Pengurangan Nilai Loading Resin." Chimica et Natura Acta 8, no. 1 (April 15, 2020): 26. http://dx.doi.org/10.24198/cna.v8.n1.28671.
Повний текст джерелаWu, Ivy, Ryan Park, and Andrew M. Herring. "Combined Electrodialysis and Peptide-Directed Struvite Recovery System." ECS Meeting Abstracts MA2022-02, no. 27 (October 9, 2022): 1041. http://dx.doi.org/10.1149/ma2022-02271041mtgabs.
Повний текст джерелаBenham, Adam M., Monique Grommé, and Jacques Neefjes. "Allelic Differences in the Relationship Between Proteasome Activity and MHC Class I Peptide Loading." Journal of Immunology 161, no. 1 (July 1, 1998): 83–89. http://dx.doi.org/10.4049/jimmunol.161.1.83.
Повний текст джерелаNatarajan, Kannan, Giora Morozov, Jiansheng Jiang, Lisa F. Boyd, Michael G. Mage, and David H. Margulies. "TAPBPR, a Peptide Editor – interactions with MHC complexes and SAXS structural studies." Journal of Immunology 196, no. 1_Supplement (May 1, 2016): 116.5. http://dx.doi.org/10.4049/jimmunol.196.supp.116.5.
Повний текст джерелаKirschmann, D. A., K. L. Duffin, C. E. Smith, J. K. Welply, S. C. Howard, B. D. Schwartz, and S. L. Woulfe. "Naturally processed peptides from rheumatoid arthritis associated and non-associated HLA-DR alleles." Journal of Immunology 155, no. 12 (December 15, 1995): 5655–62. http://dx.doi.org/10.4049/jimmunol.155.12.5655.
Повний текст джерелаKovats, Susan, Catherine E. Grubin, Susan Eastman, Paul deRoos, Ashok Dongre, Luc Van Kaer, and Alexander Y. Rudensky. "Invariant Chain–independent Function of H-2M in the Formation of Endogenous Peptide–Major Histocompatibility Complex Class II Complexes In Vivo." Journal of Experimental Medicine 187, no. 2 (January 19, 1998): 245–51. http://dx.doi.org/10.1084/jem.187.2.245.
Повний текст джерелаSgourakis, Nikolaos, Andrew C. McShan, Christine A. Devlin, Giora Morozov, and Erik Procko. "Illuminating the Mechanism of MHC-I Folding and Antigen Repertoire Selection Using Deep Mutational Scanning and Biophysical Studies." Journal of Immunology 204, no. 1_Supplement (May 1, 2020): 140.21. http://dx.doi.org/10.4049/jimmunol.204.supp.140.21.
Повний текст джерелаAmigorena, S., P. Webster, J. Drake, J. Newcomb, P. Cresswell, and I. Mellman. "Invariant chain cleavage and peptide loading in major histocompatibility complex class II vesicles." Journal of Experimental Medicine 181, no. 5 (May 1, 1995): 1729–41. http://dx.doi.org/10.1084/jem.181.5.1729.
Повний текст джерелаBatista, Patrícia, Pedro M. Castro, Ana Raquel Madureira, Bruno Sarmento, and Manuela Pintado. "Preparation, Characterization and Evaluation of Guar Films Impregnated with Relaxing Peptide Loaded into Chitosan Microparticles." Applied Sciences 11, no. 21 (October 21, 2021): 9849. http://dx.doi.org/10.3390/app11219849.
Повний текст джерелаKARATAŞ, Şule, and Fatma SAVRAN OĞUZ. "MHC Sınıf I ve MHC Sınıf II Gen Düzenlenmesi." Turkish Journal of Immunology 8, no. 3 (December 2020): 144–56. http://dx.doi.org/10.25002/tji.2020.1364.
Повний текст джерелаFan, Taotao, Xiaoyan Yu, Bing Shen, and Leming Sun. "Peptide Self-Assembled Nanostructures for Drug Delivery Applications." Journal of Nanomaterials 2017 (2017): 1–16. http://dx.doi.org/10.1155/2017/4562474.
Повний текст джерелаRizvi, Syed, and Malini Raghavan. "Tapasin-assisted peptide loading and the nature of the HLA-A2(T134K) assembly defect (106.36)." Journal of Immunology 188, no. 1_Supplement (May 1, 2012): 106.36. http://dx.doi.org/10.4049/jimmunol.188.supp.106.36.
Повний текст джерелаNie, Kun, Xiang Yu, Navnita Kumar, and Yihe Zhang. "Versatile Layer-By-Layer Highly Stable Multilayer Films: Study of the Loading and Release of FITC-Labeled Short Peptide in the Drug Delivery Field." Materials 12, no. 8 (April 12, 2019): 1206. http://dx.doi.org/10.3390/ma12081206.
Повний текст джерелаBakker, Jeroen, and Jacques Neefjes. "Identifying MHC class II peptide loading control mechanisms." Molecular Immunology 51, no. 1 (May 2012): 7. http://dx.doi.org/10.1016/j.molimm.2012.02.013.
Повний текст джерелаBusch, Robert, Robert C. Doebele, Namrata S. Patil, Achal Pashine, and Elizabeth D. Mellins. "Accessory molecules for MHC class II peptide loading." Current Opinion in Immunology 12, no. 1 (February 2000): 99–106. http://dx.doi.org/10.1016/s0952-7915(99)00057-6.
Повний текст джерелаBryant, Paula, and Hidde Ploegh. "Class II MHC peptide loading by the professionals." Current Opinion in Immunology 16, no. 1 (February 2004): 96–102. http://dx.doi.org/10.1016/j.coi.2003.11.011.
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