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30 results on '"Song Langzhou"'

6. Superior efficacy of a recombinant flagellin:H5N1 HA globular head vaccine is determined by the placement of the globular head within flagellin

Author

Song, Langzhou, Zhang, Yi, Yun, Nadezhda E., Poussard, Allison L., Smith, Jeanon N., Smith, Jennifer K., Borisevich, Viktoriya, Linde, Jenna J., Zacks, Michele A., Li, Hong, Kavita, Uma, Reiserova, Lucia, Liu, Xiangyu, Dumuren, Kunmi, Balasubramanian, Bhuvaneswari, Weaver, Bruce, Parent, Jason, Umlauf, Scott, Liu, Ge, Huleatt, Jim, Tussey, Lynda, and Paessler, Slobodan

Published
2009
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10. Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex

Author

Zheng, Ning, Schulman, Brenda A., Song, Langzhou, Miller, Julie J., Jeffrey, Philip D., Wang, Ping, Chu, Claire, Koepp, Deanna M., Elledge, Stephen J., Pagano, Michele, Conaway, Ronald C., Conaway, Joan W., Harper, J. Wade, and Pavletich, Nikola P.

Abstract

Author(s): Ning Zheng [1, 2]; Brenda A. Schulman [1, 3]; Langzhou Song [1, 2]; Julie J. Miller [1, 2]; Philip D. Jeffrey [1]; Ping Wang [1, 2]; Claire Chu [3]; [...]

Published
2002
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11. Structure of a staphylococcal alpha-hemolysin, a heptameric transmembrane pore

Author

Song, Langzhou, Hobaugh, Michael R., Shustak, Christopher, Cheley, Stephen, Bayley, Hagan, and Gouaux, J. Eric

Subjects
Hemolysis and hemolysins -- Research, Bilayer lipid membranes -- Physiological aspects, Membranes (Biology) -- Physiological aspects, Biological transport -- Physiological aspects
Published
1996

12. Subunit stoichiometry of staphylococcal alpha-hemolysin in crystals and on membranes: a heptameric transmembrane pore

Author

Gouaux, J. Eric, Braha, Orit, Hobaugh, Michael R., Song, Langzhou, Cheley, Stephen, Shustak, Christopher, and Bayley, Hagan

Subjects
Staphylococcus -- Research, Toxins -- Analysis, Proteins -- Conformation, Science and technology
Abstract

Examination of the data from chemical modification experiments and X-ray diffraction studies of alpha-hemolysin (alpha-HL) oligomeric toxin in staphylococcus reveals that alpha-HL is heptameric in nature and has a sevenfold rotational symmetry axis. Electrophoretic separation helps identify the alpha-HL pore on rabbit erythrocyte membranes as a heptamer. Thus, alpha-HL has a definite heptameric oligomerization state in a biological membrane and in three-dimensional crystals.

Published
1994

16. Immunogenicity and Efficacy of Flagellin-Envelope Fusion Dengue Vaccines in Mice and Monkeys

Author

Liu, Ge, primary, Song, Langzhou, additional, Beasley, David W. C., additional, Putnak, Robert, additional, Parent, Jason, additional, Misczak, John, additional, Li, Hong, additional, Reiserova, Lucia, additional, Liu, Xiangyu, additional, Tian, Haijun, additional, Liu, Wenzhe, additional, Labonte, Darlene, additional, Duan, Lihua, additional, Kim, Youngsun, additional, Travalent, Linda, additional, Wigington, Devin, additional, Weaver, Bruce, additional, and Tussey, Lynda, additional

Published
2015
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21. Efficacious Recombinant Influenza Vaccines Produced by High Yield Bacterial Expression: A Solution to Global Pandemic and Seasonal Needs

Author

Song, Langzhou, primary, Nakaar, Valerian, additional, Kavita, Uma, additional, Price, Albert, additional, Huleatt, Jim, additional, Tang, Jie, additional, Jacobs, Andrea, additional, Liu, Ge, additional, Huang, Yan, additional, Desai, Priyanka, additional, Maksymiuk, Gail, additional, Takahashi, Virginia, additional, Umlauf, Scott, additional, Reiserova, Lucia, additional, Bell, Rodney, additional, Li, Hong, additional, Zhang, Yi, additional, McDonald, William F., additional, Powell, T. J., additional, and Tussey, Lynda, additional

Published
2008
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25. Structure of the Cul1?Rbx1?Skp1?F boxSkp2 SCF ubiquitin ligase complex.

Author

Zheng, Ning, Schulman, Brenda A., Song, Langzhou, Miller, Julie J., Jeffrey, Philip D., Wang, Ping, Chu, Claire, Koepp, Deanna M., Elledge, Stephen J., Pagano, Michele, Conaway, Ronald C., Conaway, Joan W., Harper, J. Wade, and Pavletich, Nikola P.

Subjects
CRYSTALS, CATALYSIS, UBIQUITIN
Abstract

SCF complexes are the largest family of E3 ubiquitin?protein ligases and mediate the ubiquitination of diverse regulatory and signalling proteins. Here we present the crystal structure of the Cul1?Rbx1?Skp1?F boxSkp2 SCF complex, which shows that Cul1 is an elongated protein that consists of a long stalk and a globular domain. The globular domain binds the RING finger protein Rbx1 through an intermolecular β-sheet, forming a two-subunit catalytic core that recruits the ubiquitin-conjugating enzyme. The long stalk, which consists of three repeats of a novel five-helix motif, binds the Skp1?F boxSkp2 protein substrate-recognition complex at its tip. Cul1 serves as a rigid scaffold that organizes the Skp1?F boxSkp2 and Rbx1 subunits, holding them over 100 Å apart. The structure suggests that Cul1 may contribute to catalysis through the positioning of the substrate and the ubiquitin-conjugating enzyme, and this model is supported by Cul1 mutations designed to eliminate the rigidity of the scaffold. [ABSTRACT FROM AUTHOR]

Published
2002
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26. α-Hemolysin, γ-hemolysin, and leukocidin from Staphylococcus aureus: Distant in sequence but similar in structure.

Author

Gouaux, Eric, Hobaugh, Michael, and Song, Langzhou

Abstract

α-Hemolysin from Staphylococcus aureus assembles from a water-soluble, monomeric species to a membrane-bound heptamer on the surface of target cells, creating water-filled channels that lead to cell death and lysis. Staphylococcus aureus also produces the γ-hemolysin and leukocidin toxins, which function as two component toxins in the disruption and lysis of erythrocytes and leukocytes. Analysis of the aligned sequences of α-hemolysin, γ-hemolysin, and leukocidin in the context of the α-hemolysin heptamer structure supports the conclusion that even though the level of sequence identity between α-hemolysin and the γ-hemolysin and leukocidin toxins is in the so-called twilight zone, the three-dimensional structures of the protomers are probably conserved. By analogy with α-hemolysin, γ-hemolysin and leukocidin may also form oligomeric, transmembrane channels in which an anti-parallel β-barrel constitutes the primary membrane-embedded domain. [ABSTRACT FROM AUTHOR]

Published
1997
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