Zeitschriftenartikel zum Thema „Glycoproteins“
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Garbutt, Michael, Ryan Liebscher, Victoria Wahl-Jensen, Steven Jones, Peggy Möller, Ralf Wagner, Viktor Volchkov, Hans-Dieter Klenk, Heinz Feldmann und Ute Ströher. „Properties of Replication-Competent Vesicular Stomatitis Virus Vectors Expressing Glycoproteins of Filoviruses and Arenaviruses“. Journal of Virology 78, Nr. 10 (15.05.2004): 5458–65. http://dx.doi.org/10.1128/jvi.78.10.5458-5465.2004.
Jorgenson, Rebecca L., Volker M. Vogt und Marc C. Johnson. „Foreign Glycoproteins Can Be Actively Recruited to Virus Assembly Sites during Pseudotyping“. Journal of Virology 83, Nr. 9 (18.02.2009): 4060–67. http://dx.doi.org/10.1128/jvi.02425-08.
Quinn, Derek J., Neil V. McFerran, John Nelson und W. Paul Duprex. „Live-cell visualization of transmembrane protein oligomerization and membrane fusion using two-fragment haptoEGFP methodology“. Bioscience Reports 32, Nr. 3 (29.03.2012): 333–43. http://dx.doi.org/10.1042/bsr20110100.
Lay Mendoza, Maria Fernanda, Marissa Danielle Acciani, Courtney Nina Levit, Christopher Santa Maria und Melinda Ann Brindley. „Monitoring Viral Entry in Real-Time Using a Luciferase Recombinant Vesicular Stomatitis Virus Producing SARS-CoV-2, EBOV, LASV, CHIKV, and VSV Glycoproteins“. Viruses 12, Nr. 12 (17.12.2020): 1457. http://dx.doi.org/10.3390/v12121457.
Joshua, G. W. P., L. J. S. Harrison und M. M. H. Sewell. „Developmental changes in proteins and glycoproteins revealed by direct radio-iodination of viable Taenia saginata larvae“. Parasitology 99, Nr. 2 (Oktober 1989): 265–74. http://dx.doi.org/10.1017/s0031182000058728.
Zhang, Libo, Yanhong Li, Riyao Li, Xiaohong Yang, Zimin Zheng, Jingxin Fu, Hai Yu und Xi Chen. „Glycoprotein In Vitro N-Glycan Processing Using Enzymes Expressed in E. coli“. Molecules 28, Nr. 6 (18.03.2023): 2753. http://dx.doi.org/10.3390/molecules28062753.
Si, Zhihai, Mark Cayabyab und Joseph Sodroski. „Envelope Glycoprotein Determinants of Neutralization Resistance in a Simian-Human Immunodeficiency Virus (SHIV-HXBc2P 3.2) Derived by Passage in Monkeys“. Journal of Virology 75, Nr. 9 (01.05.2001): 4208–18. http://dx.doi.org/10.1128/jvi.75.9.4208-4218.2001.
Calvete, J. J., J. L. McGregor, G. Rivas und J. González-Rodríguez. „Identification of a Glycoprotein III a Dimer in Polyacrylamide Gel Separations of Human Platelet Membranes“. Thrombosis and Haemostasis 58, Nr. 02 (1987): 694–97. http://dx.doi.org/10.1055/s-0038-1645957.
LaBonte, Jason A., Navid Madani und Joseph Sodroski. „Cytolysis by CCR5-Using Human Immunodeficiency Virus Type 1 Envelope Glycoproteins Is Dependent on Membrane Fusion and Can Be Inhibited by High Levels of CD4 Expression“. Journal of Virology 77, Nr. 12 (15.06.2003): 6645–59. http://dx.doi.org/10.1128/jvi.77.12.6645-6659.2003.
Shammala, Farid Abu. „Mass spectrometry-based analysis of glycoproteins and its clinical applications in cancer biomarker discovery“. Brazilian Journal of Biological Sciences 4, Nr. 7 (2017): 203–15. http://dx.doi.org/10.21472/bjbs.040720.
Yang, Xinzhen, Juliette Lee, Erin M. Mahony, Peter D. Kwong, Richard Wyatt und Joseph Sodroski. „Highly Stable Trimers Formed by Human Immunodeficiency Virus Type 1 Envelope Glycoproteins Fused with the Trimeric Motif of T4 Bacteriophage Fibritin“. Journal of Virology 76, Nr. 9 (01.05.2002): 4634–42. http://dx.doi.org/10.1128/jvi.76.9.4634-4642.2002.
Ji, Xin, Gene G. Olinger, Sheena Aris, Ying Chen, Henry Gewurz und Gregory T. Spear. „Mannose-binding lectin binds to Ebola and Marburg envelope glycoproteins, resulting in blocking of virus interaction with DC-SIGN and complement-mediated virus neutralization“. Journal of General Virology 86, Nr. 9 (01.09.2005): 2535–42. http://dx.doi.org/10.1099/vir.0.81199-0.
Ninagawa, Satoshi, Tetsuya Okada, Yoshiki Sumitomo, Satoshi Horimoto, Takehiro Sugimoto, Tokiro Ishikawa, Shunichi Takeda et al. „Forcible destruction of severely misfolded mammalian glycoproteins by the non-glycoprotein ERAD pathway“. Journal of Cell Biology 211, Nr. 4 (16.11.2015): 775–84. http://dx.doi.org/10.1083/jcb.201504109.
Choukhi, Amélie, André Pillez, Hervé Drobecq, Christian Sergheraert, Czeslaw Wychowski und Jean Dubuisson. „Characterization of aggregates of hepatitis C virus glycoproteins“. Journal of General Virology 80, Nr. 12 (01.12.1999): 3099–107. http://dx.doi.org/10.1099/0022-1317-80-12-3099.
Snyder, Aleksandra, Todd W. Wisner und David C. Johnson. „Herpes Simplex Virus Capsids Are Transported in Neuronal Axons without an Envelope Containing the Viral Glycoproteins“. Journal of Virology 80, Nr. 22 (13.09.2006): 11165–77. http://dx.doi.org/10.1128/jvi.01107-06.
Sandrin, Virginie, Delphine Muriaux, Jean-Luc Darlix und François-Loïc Cosset. „Intracellular Trafficking of Gag and Env Proteins and Their Interactions Modulate Pseudotyping of Retroviruses“. Journal of Virology 78, Nr. 13 (01.07.2004): 7153–64. http://dx.doi.org/10.1128/jvi.78.13.7153-7164.2004.
Yang, Xinzhen, Svetla Kurteva, Xinping Ren, Sandra Lee und Joseph Sodroski. „Subunit Stoichiometry of Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Trimers during Virus Entry into Host Cells“. Journal of Virology 80, Nr. 9 (01.05.2006): 4388–95. http://dx.doi.org/10.1128/jvi.80.9.4388-4395.2006.
Rosenberg, Arielle R., Lélia Delamarre, Anna Preira und Marie-Christine Dokhélar. „Analysis of Functional Conservation in the Surface and Transmembrane Glycoprotein Subunits of Human T-Cell Leukemia Virus Type 1 (HTLV-1) and HTLV-2“. Journal of Virology 72, Nr. 9 (01.09.1998): 7609–14. http://dx.doi.org/10.1128/jvi.72.9.7609-7614.1998.
Karger, Axel, Ulrike Schmidt und Ursula J. Buchholz. „Recombinant bovine respiratory syncytial virus with deletions of the G or SH genes: G and F proteins bind heparin“. Journal of General Virology 82, Nr. 3 (01.03.2001): 631–40. http://dx.doi.org/10.1099/0022-1317-82-3-631.
Børsum, Tone. „Immunoelectrophoretic Analysis of Membrane Glycoproteins in Cultured Human Endothelial Cells“. Thrombosis and Haemostasis 63, Nr. 02 (1990): 303–11. http://dx.doi.org/10.1055/s-0038-1645214.
Bloodgood, R. A., und N. L. Salomonsky. „The transmembrane signaling pathway involved in directed movements of Chlamydomonas flagellar membrane glycoproteins involves the dephosphorylation of a 60-kD phosphoprotein that binds to the major flagellar membrane glycoprotein.“ Journal of Cell Biology 127, Nr. 3 (01.11.1994): 803–11. http://dx.doi.org/10.1083/jcb.127.3.803.
Weaver, T. E., J. A. Whitsett, W. M. Hull und G. Ross. „Identification of canine pulmonary surfactant-associated glycoprotein A precursors“. Journal of Applied Physiology 58, Nr. 6 (01.06.1985): 2091–95. http://dx.doi.org/10.1152/jappl.1985.58.6.2091.
Batonick, Melissa, und Gail W. Wertz. „Requirements for Human Respiratory Syncytial Virus Glycoproteins in Assembly and Egress from Infected Cells“. Advances in Virology 2011 (2011): 1–11. http://dx.doi.org/10.1155/2011/343408.
Bieńkowska-Szewczyk, K., und B. Szewczyk. „Expression of genes coding for animal virus glycoproteins in heterologous systems.“ Acta Biochimica Polonica 46, Nr. 2 (30.06.1999): 325–39. http://dx.doi.org/10.18388/abp.1999_4166.
Kukushkin, Nikolay V., Dominic S. Alonzi, Raymond A. Dwek und Terry D. Butters. „Demonstration that endoplasmic reticulum-associated degradation of glycoproteins can occur downstream of processing by endomannosidase“. Biochemical Journal 438, Nr. 1 (27.07.2011): 133–42. http://dx.doi.org/10.1042/bj20110186.
Lisanti, M. P., A. Le Bivic, M. Sargiacomo und E. Rodriguez-Boulan. „Steady-state distribution and biogenesis of endogenous Madin-Darby canine kidney glycoproteins: evidence for intracellular sorting and polarized cell surface delivery.“ Journal of Cell Biology 109, Nr. 5 (01.11.1989): 2117–27. http://dx.doi.org/10.1083/jcb.109.5.2117.
Wang, Qiong, und Michael J. Betenbaugh. „Metabolic engineering of CHO cells to prepare glycoproteins“. Emerging Topics in Life Sciences 2, Nr. 3 (18.10.2018): 433–42. http://dx.doi.org/10.1042/etls20180056.
Bloodgood, R. A., und N. L. Salomonsky. „Calcium influx regulates antibody-induced glycoprotein movements within the Chlamydomonas flagellar membrane“. Journal of Cell Science 96, Nr. 1 (01.05.1990): 27–33. http://dx.doi.org/10.1242/jcs.96.1.27.
Hulswit, Ruben J. G., Guido C. Paesen, Thomas A. Bowden und Xiaohong Shi. „Recent Advances in Bunyavirus Glycoprotein Research: Precursor Processing, Receptor Binding and Structure“. Viruses 13, Nr. 2 (23.02.2021): 353. http://dx.doi.org/10.3390/v13020353.
Srivastav, Archana, Balvir Singh, Abhishek Chandra, Farrukh Jamal, Mohammad Y. Khan und Sunil R. Chowdhury. „Partial characterization, sperm association and significance of N- and O-linked glycoproteins in epididymal fluid of rhesus monkeys (Macaca mulatta)“. Reproduction 127, Nr. 3 (März 2004): 343–57. http://dx.doi.org/10.1530/rep.1.00119.
Horvat, B., H. A. Multhaupt und I. Damjanov. „Glycoproteins of mouse vaginal epithelium: differential expression related to estrous cyclicity.“ Journal of Histochemistry & Cytochemistry 41, Nr. 9 (September 1993): 1351–57. http://dx.doi.org/10.1177/41.9.8354876.
Zimmer, Gert, Klaus-Peter Zimmer, Ina Trotz und Georg Herrler. „Vesicular Stomatitis Virus Glycoprotein Does Not Determine the Site of Virus Release in Polarized Epithelial Cells“. Journal of Virology 76, Nr. 8 (15.04.2002): 4103–7. http://dx.doi.org/10.1128/jvi.76.8.4103-4107.2002.
Vollenweider, Florence, Felix Kappeler, Christian Itin und Hans-Peter Hauri. „Mistargeting of the Lectin ERGIC-53 to the Endoplasmic Reticulum of HeLa Cells Impairs the Secretion of a Lysosomal Enzyme“. Journal of Cell Biology 142, Nr. 2 (27.07.1998): 377–89. http://dx.doi.org/10.1083/jcb.142.2.377.
Rosenberg, Arielle R., Lélia Delamarre, Claudine Pique, Isabelle Le Blanc, Graziella Griffith und Marie-Christine Dokhélar. „Early Assembly Step of a Retroviral Envelope Glycoprotein: Analysis Using a Dominant Negative Assay“. Journal of Cell Biology 145, Nr. 1 (05.04.1999): 57–68. http://dx.doi.org/10.1083/jcb.145.1.57.
Culp, D. J., L. R. Latchney, M. W. Frampton, M. R. Jahnke, P. E. Morrow und M. J. Utell. „Composition of human airway mucins and effects after inhalation of acid aerosol“. American Journal of Physiology-Lung Cellular and Molecular Physiology 269, Nr. 3 (01.09.1995): L358—L370. http://dx.doi.org/10.1152/ajplung.1995.269.3.l358.
Wu, R., C. G. Plopper und P. W. Cheng. „Mucin-like glycoprotein secreted by cultured hamster tracheal epithelial cells. Biochemical and immunological characterization“. Biochemical Journal 277, Nr. 3 (01.08.1991): 713–18. http://dx.doi.org/10.1042/bj2770713.
Garry, Courtney E., und Robert F. Garry. „Proteomics Computational Analyses Suggest that the Antennavirus Glycoprotein Complex Includes a Class I Viral Fusion Protein (α-Penetrene) with an Internal Zinc-Binding Domain and a Stable Signal Peptide“. Viruses 11, Nr. 8 (14.08.2019): 750. http://dx.doi.org/10.3390/v11080750.
Hortin, G., E. D. Green, J. U. Baenziger und A. W. Strauss. „Sulphation of proteins secreted by a human hepatoma-derived cell line. Sulphation of N-linked oligosaccharides on α2HS-glycoprotein“. Biochemical Journal 235, Nr. 2 (15.04.1986): 407–14. http://dx.doi.org/10.1042/bj2350407.
Kassa, Aemro, Andrés Finzi, Marie Pancera, Joel R. Courter, Amos B. Smith und Joseph Sodroski. „Identification of a Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Variant Resistant to Cold Inactivation“. Journal of Virology 83, Nr. 9 (11.02.2009): 4476–88. http://dx.doi.org/10.1128/jvi.02110-08.
Snyder, Aleksandra, Katarina Polcicova und David C. Johnson. „Herpes Simplex Virus gE/gI and US9 Proteins Promote Transport of both Capsids and Virion Glycoproteins in Neuronal Axons“. Journal of Virology 82, Nr. 21 (27.08.2008): 10613–24. http://dx.doi.org/10.1128/jvi.01241-08.
Lamers, Susanna L., Ruchi M. Newman, Oliver Laeyendecker, Aaron A. R. Tobian, Robert C. Colgrove, Stuart C. Ray, David M. Koelle, Jeffrey Cohen, David M. Knipe und Thomas C. Quinn. „Global Diversity within and between Human Herpesvirus 1 and 2 Glycoproteins“. Journal of Virology 89, Nr. 16 (27.05.2015): 8206–18. http://dx.doi.org/10.1128/jvi.01302-15.
Stein, W. D. „Kinetics of the multidrug transporter (P-glycoprotein) and its reversal“. Physiological Reviews 77, Nr. 2 (01.04.1997): 545–90. http://dx.doi.org/10.1152/physrev.1997.77.2.545.
Lin, Borong, Xue Qing, Jinling Liao und Kan Zhuo. „Role of Protein Glycosylation in Host-Pathogen Interaction“. Cells 9, Nr. 4 (20.04.2020): 1022. http://dx.doi.org/10.3390/cells9041022.
Bowden, Thomas A., Max Crispin, Stephen C. Graham, David J. Harvey, Jonathan M. Grimes, E. Yvonne Jones und David I. Stuart. „Unusual Molecular Architecture of the Machupo Virus Attachment Glycoprotein“. Journal of Virology 83, Nr. 16 (03.06.2009): 8259–65. http://dx.doi.org/10.1128/jvi.00761-09.
Jiang, Lingdong, Rui Lu und Lei Ye. „Towards Detection of Glycoproteins Using Molecularly Imprinted Nanoparticles and Boronic Acid-Modified Fluorescent Probe“. Polymers 11, Nr. 1 (18.01.2019): 173. http://dx.doi.org/10.3390/polym11010173.
KONRAD, Zvia, und Jerry EICHLER. „Lipid modification of proteins in Archaea: attachment of a mevalonic acid-based lipid moiety to the surface-layer glycoprotein of Haloferax volcanii follows protein translocation“. Biochemical Journal 366, Nr. 3 (15.09.2002): 959–64. http://dx.doi.org/10.1042/bj20020757.
Batonick, Melissa, Antonius G. P. Oomens und Gail W. Wertz. „Human Respiratory Syncytial Virus Glycoproteins Are Not Required for Apical Targeting and Release from Polarized Epithelial Cells“. Journal of Virology 82, Nr. 17 (18.06.2008): 8664–72. http://dx.doi.org/10.1128/jvi.00827-08.
Santos, Joy Ramielle L., Weijie Sun, Tarana A. Mangukia, Eduardo Reyes-Serratos und Marcelo Marcet-Palacios. „Challenging the Existing Model of the Hexameric HIV-1 Gag Lattice and MA Shell Superstructure: Implications for Viral Entry“. Viruses 13, Nr. 8 (31.07.2021): 1515. http://dx.doi.org/10.3390/v13081515.
Wahl-Jensen, Victoria, Sabine K. Kurz, Paul R. Hazelton, Hans-Joachim Schnittler, Ute Ströher, Dennis R. Burton und Heinz Feldmann. „Role of Ebola Virus Secreted Glycoproteins and Virus-Like Particles in Activation of Human Macrophages“. Journal of Virology 79, Nr. 4 (15.02.2005): 2413–19. http://dx.doi.org/10.1128/jvi.79.4.2413-2419.2005.
Roberts, G. P. R., und J. Brunt. „Differentiation-related changes in glycoprotein synthesis by human keratinocytes“. Biochemical Journal 237, Nr. 2 (15.07.1986): 519–25. http://dx.doi.org/10.1042/bj2370519.