Membrane Proteins Structure Determination
Mostrando 13-24 de 25 artigos, teses e dissertações.
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13. Determination of transmembrane protein structure by disulfide cross-linking: the Escherichia coli Tar receptor.
We have devised a generally applicable strategy for analysis of protein structure and have applied it to examine the structure of the transmembrane portion of the Tar receptor of Escherichia coli. The basis of our approach is the use of disulfide cross-linking to identify residues that are within close proximity. To generate and test large numbers of cystein
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14. A PH domain within OCRL bridges clathrin-mediated membrane trafficking to phosphoinositide metabolism
OCRL, whose mutations are responsible for Lowe syndrome and Dent disease, and INPP5B are two similar proteins comprising a central inositol 5-phosphatase domain followed by an ASH and a RhoGAP-like domain. Their divergent NH2-terminal portions remain uncharacterized. We show that the NH2-terminal region of OCRL, but not of INPP5B, binds clathrin heavy chain.
Nature Publishing Group.
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15. Cell Envelope and Shape of Escherichia coli K12. Crosslinking with Dimethyl Imidoesters of the Whole Cell Wall
E. coli cells treated with the bifunctional crosslinking reagents dimethyl malonimidate, succinimidate, adipimidate, suberimidate, and sebacinimidate served for the isolation of rod-shaped “ghosts.” These ghosts proved to be crosslinked over their entire surface; i.e., a macromolecule (resistant to boiling 1% Na dodecyl sulfate) the size of the cell had
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16. Role of the Rous Sarcoma Virus p10 Domain in Shape Determination of Gag Virus-Like Particles Assembled In Vitro and within Escherichia coli
Purified retrovirus Gag proteins can assemble in vitro into virus-like particles (VLPs) in the presence of RNA. It was shown previously that a Rous sarcoma virus Gag protein missing only the protease domain forms spherical particles resembling immature virions lacking a membrane but that a similar protein missing the p10 domain forms tubular particles. Thus,
American Society for Microbiology.
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17. Vascular patterning defects associated with expression of activated Notch4 in embryonic endothelium
Notch proteins function as receptors for membrane-bound ligands (Jagged and Delta-like) to regulate cell-fate determination. We have investigated the role of Notch signaling in embryonic endothelium of the mouse by expressing an activated form of the Notch4 protein in vasculature under the regulation of the Flk1 (VEGFR) locus. Expression of activated No
The National Academy of Sciences.
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18. Oligomeric structure of virion-associated and soluble forms of the simian immunodeficiency virus envelope protein in the prefusion activated conformation
The envelope proteins (env) of simian immunodeficiency virus (SIV) and HIV type 1 assemble to form noncovalently associated oligomers in the endoplasmic reticulum. After cleavage in a Golgi compartment, oligomeric env complexes are transported to the surface of infected cells, where incorporation into budding virions can occur. Difficulties in obtaining
The National Academy of Sciences.
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19. Molecular analysis of the serotyping antigens of Neisseria meningitidis.
Molecular approaches to the rapid analysis of the serotyping antigens of Neisseria meningitidis, the class 2 and 3 outer membrane proteins (OMPs), were developed, evaluated, and used to study 12 antigenic variants of these proteins. A primer set for the polymerase chain reaction (PCR) amplification of the genes encoding these antigens was devised. Low-string
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20. Identification of a Dichelobacter nodosus Ferric Uptake Regulator and Determination of Its Regulatory Targets
The expression of iron regulated genes in bacteria is typically controlled by the ferric uptake regulator (Fur) protein, a global transcriptional repressor that regulates functions as diverse as iron acquisition, oxidative stress, and virulence. We have identified a fur homologue in Dichelobacter nodosus, the causative agent of ovine footrot, and shown that
American Society for Microbiology.
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21. Genomic Interspecies Microarray Hybridization: Rapid Discovery of Three Thousand Genes in the Maize Endophyte, Klebsiella pneumoniae 342, by Microarray Hybridization with Escherichia coli K-12 Open Reading Frames
In an effort to efficiently discover genes in the diazotrophic endophyte of maize, Klebsiella pneumoniae 342, DNA from strain 342 was hybridized to a microarray containing 96% (n = 4,098) of the annotated open reading frames from Escherichia coli K-12. Using a criterion of 55% identity or greater, 3,000 (70%) of the E. coli K-12 open reading frames were also
American Society for Microbiology.
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22. Amino acid sequence of the NH2-terminal extra piece segments of the precursors of mouse immunoglobulin lambda1-type and kappa-type light chains.
The mRNA molecules coding for mouse immunoglobulin light (L) chains direct the cell-free synthesis of precursors in which extra peptide segments precede the amino termini of the mature proteins. The results of amino acid sequence analyses of two precursors labeled with 20 radioactive amino acids enabled unambiguous determination of the complete primary struc
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23. An ab Initio Structural Model of a Nucleoside Permease Predicts Functionally Important Residues*
Permeases belonging to the equilibrative nucleoside transporter family promote uptake of nucleosides and/or nucleobases into a wide range of eukaryotes and mediate the uptake of a variety of drugs used in the treatment of cancer, heart disease, AIDS, and parasitic infections. No experimental three-dimensional structure exists for any of these permeases, and
American Society for Biochemistry and Molecular Biology.
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24. ElNémo: a normal mode web server for protein movement analysis and the generation of templates for molecular replacement
Normal mode analysis (NMA) is a powerful tool for predicting the possible movements of a given macromolecule. It has been shown recently that half of the known protein movements can be modelled by using at most two low-frequency normal modes. Applications of NMA cover wide areas of structural biology, such as the study of protein conformational changes upon
Oxford University Press.