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24 results on '"Suloway, Christian"'

1. Influenza Research Database: An integrated bioinformatics resource for influenza virus research

Author

Zhang, Yun, Aevermann, Brian D, Anderson, Tavis K, Burke, David F, Dauphin, Gwenaelle, Gu, Zhiping, He, Sherry, Kumar, Sanjeev, Larsen, Christopher N, Lee, Alexandra J, Li, Xiaomei, Macken, Catherine, Mahaffey, Colin, Pickett, Brett E, Reardon, Brian, Smith, Thomas, Stewart, Lucy, Suloway, Christian, Sun, Guangyu, Tong, Lei, Vincent, Amy L, Walters, Bryan, Zaremba, Sam, Zhao, Hongtao, Zhou, Liwei, Zmasek, Christian, Klem, Edward B, and Scheuermann, Richard H

Subjects
Emerging Infectious Diseases, Pneumonia & Influenza, Vaccine Related, Networking and Information Technology R&D (NITRD), Prevention, Biodefense, Infectious Diseases, Influenza, Infection, Good Health and Well Being, Computational Biology, Databases, Factual, Influenza A virus, Molecular Typing, Phenotype, Phylogeny, Research, Software, Viral Proteins, Virulence, Environmental Sciences, Biological Sciences, Information and Computing Sciences, Developmental Biology
Abstract

The Influenza Research Database (IRD) is a U.S. National Institute of Allergy and Infectious Diseases (NIAID)-sponsored Bioinformatics Resource Center dedicated to providing bioinformatics support for influenza virus research. IRD facilitates the research and development of vaccines, diagnostics and therapeutics against influenza virus by providing a comprehensive collection of influenza-related data integrated from various sources, a growing suite of analysis and visualization tools for data mining and hypothesis generation, personal workbench spaces for data storage and sharing, and active user community support. Here, we describe the recent improvements in IRD including the use of cloud and high performance computing resources, analysis and visualization of user-provided sequence data with associated metadata, predictions of novel variant proteins, annotations of phenotype-associated sequence markers and their predicted phenotypic effects, hemagglutinin (HA) clade classifications, an automated tool for HA subtype numbering conversion, linkouts to disease event data and the addition of host factor and antiviral drug components. All data and tools are freely available without restriction from the IRD website at https://www.fludb.org.

Published
2017

15. Structural Insights into Tail-Anchored Protein Targeting by Get3

Author

Suloway, Christian J. M., Suloway, Christian J. M., Suloway, Christian J. M., and Suloway, Christian J. M.

Abstract

Translocation of membrane proteins from the point of synthesis to their integration in the membrane is critical to the function of the cell. Tail-anchored (TA) proteins are an important class of membrane proteins with a single transmembrane domain (TMD) close to the carboxyl-terminus. They are defined topologically by having their amino-terminus in the cytosol and their carboxyl-terminus on the exterior side of the membrane. Since the TMD is sequestered by the ribosome during translation, co-translational translocation of TA proteins by the SRP-dependent pathway is not possible. The Guided Entry of Tail-anchored proteins (GET) pathway post-translationally targets TA proteins to the endoplasmic reticulum (ER) membrane. The conserved nucleotide hydrolase Get3 is the central protein in the pathway that specifically binds the TMD of TA proteins to chaperone them from a sorting complex of Get4, Get5, Sgt2 and other chaperones to an ER membrane receptor formed by Get1 and Get2. We have created a model for the mechanism of Get3 TA protein binding coupled to nucleotide state using X-ray crystallography, structural modeling and mutagenesis experiments. We then demonstrate expression, purification and crystallization of complexes of Get3 with TA proteins for structural studies. Finally, we present a crystal structure of a tetrameric archaeal Get3 homologue that forms a central hydrophobic chamber and is capable of binding TA proteins. Using small-angle X-ray scattering, the structure is comparable to a tetrameric fungal Get3 complex with TA protein, which is capable of TA protein membrane integration in vitro. This suggests a model in which a tetramer of Get3 binds TA proteins for delivery to the membrane.

Published
2012

16. Influenza Research Database: An integrated bioinformatics resource for influenza virus research

Author

Zhang, Yun, primary, Aevermann, Brian D., additional, Anderson, Tavis K., additional, Burke, David F., additional, Dauphin, Gwenaelle, additional, Gu, Zhiping, additional, He, Sherry, additional, Kumar, Sanjeev, additional, Larsen, Christopher N., additional, Lee, Alexandra J., additional, Li, Xiaomei, additional, Macken, Catherine, additional, Mahaffey, Colin, additional, Pickett, Brett E., additional, Reardon, Brian, additional, Smith, Thomas, additional, Stewart, Lucy, additional, Suloway, Christian, additional, Sun, Guangyu, additional, Tong, Lei, additional, Vincent, Amy L., additional, Walters, Bryan, additional, Zaremba, Sam, additional, Zhao, Hongtao, additional, Zhou, Liwei, additional, Zmasek, Christian, additional, Klem, Edward B., additional, and Scheuermann, Richard H., additional

Published
2016
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17. Tail-anchor targeting by a Get3 tetramer: the structure of an archaeal homologue

Author

Suloway, Christian J. M., Rome, Michael E., and Clemons, William M., Jr.

Subjects
Adenosine Triphosphatases, Models, Molecular, Saccharomyces cerevisiae Proteins, Protein Conformation, Molecular Sequence Data, Guanine Nucleotide Exchange Factors, Amino Acid Sequence, Archaea, Article, Protein Binding
Abstract

Efficient delivery of membrane proteins is a critical cellular process. The recently elucidated GET (Guided Entry of TA proteins) pathway is responsible for the targeted delivery of tail-anchored (TA) membrane proteins to the endoplasmic reticulum. The central player is the ATPase Get3, which in its free form exists as a dimer. Biochemical evidence suggests a role for a tetramer of Get3. Here, we present the first crystal structure of an archaeal Get3 homologue that exists as a tetramer and is capable of TA protein binding. The tetramer generates a hydrophobic chamber that we propose binds the TA protein. We use small-angle X-ray scattering to provide the first structural information of a fungal Get3/TA protein complex showing that the overall molecular envelope is consistent with the archaeal tetramer structure. Moreover, we show that this fungal tetramer complex is capable of TA insertion. This allows us to suggest a model where a tetramer of Get3 sequesters a TA protein during targeting to the membrane.

Published
2011

23. Rapid routine structure determination of macromolecular assemblies using electron microscopy: current progress and further challenges

Author

Carragher, Bridget, primary, Fellmann, Denis, additional, Guerra, Francisco, additional, Milligan, Ronald A., additional, Mouche, Fabrice, additional, Pulokas, James, additional, Sheehan, Brian, additional, Quispe, Joel, additional, Suloway, Christian, additional, Zhu, Yuanxin, additional, and Potter, Clinton S., additional

Published
2003
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24. Rapid, routine structure determination of macromolecular assemblies using electron microscopy: current progress and further challenges.

Author

Carragher, Bridget, Fellmann, Denis, Guerra, Francisco, Milligan, Ronald A., Mouche, Fabrice, Pulokas, James, Sheehan, Brian, Quispe, Joel, Suloway, Christian, Yuanxin Zhu, and Potter, Clinton S.

Subjects
MACROMOLECULES, ELECTRON microscopy, MOLECULES, ELECTRON distribution, ELECTRONS, DENSITY matrices
Abstract

Discusses the rapid, routine structure determination of macromolecular assemblies using electron microscopy. Techniques required to produce a three-dimensional electron density map of a macromolecular structure; Development of systems to automate the process of data acquisition from an electron microscope.

Published
2004
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