Search Results - "BOOY, FRANK P."

3D structure of EspA filaments from enteropathogenic Escherichia coli by Daniell, Sarah J., Kocsis, Eva, Morris, Edward, Knutton, Stuart, Booy, Frank P., Frankel, Gad

“…Summary The type III secretion system (TTSS) is a modular apparatus assembled by many pathogenic Gram‐negative bacteria and is designed to translocate proteins…”
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Encapsidated Conformation of Bacteriophage T7 DNA by Cerritelli, Mario E, Cheng, Naiqian, Rosenberg, Alan H, McPherson, Catherine E, Booy, Frank P, Steven, Alasdair C

“…The structural organization of encapsidated T7 DNA was investigated by cryo-electron microscopy and image processing. A tail-deletion mutant was found to…”
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Visualization of Dendrimer Molecules by Transmission Electron Microscopy (TEM):  Staining Methods and Cryo-TEM of Vitrified Solutions by Jackson, Catheryn L, Chanzy, Henri D, Booy, Frank P, Drake, Bartholomew J, Tomalia, Donald A, Bauer, Barry J, Amis, Eric J

“…Individual dendrimer molecules of poly(amidoamine) (PAMAM) from generation 10 (G10) to G5 were imaged by conventional transmission electron microscopy (TEM)…”
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Novel structural features of bovine papillomavirus capsid revealed by a three-dimensional reconstruction to 9 Å resolution by Trus, Benes L, Roden, Richard B.S, Greenstone, Heather L, Vrhel, Michael, Schiller, John T, Booy, Frank P

“…The three-dimensional structure of bovine papillomavirus has been determined to 9 A resolution by reconstruction of high resolution, low dose cryo-electron…”
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Structure of L-A virus: a specialized compartment for the transcription and replication of double-stranded RNA by Caston, J.R. (NIH, Bethesda, MD.), Trus, B.L, Booy, F.P, Wickner, R.B, Wall, J.S, Steven, A.C

“…The genomes of double-stranded (ds)RNA viruses are never exposed to the cytoplasm but are confined to and replicated from a specialized protein-bound…”
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Molecular characterization of a partitivirus from Ophiostoma himal-ulmi by Crawford, Lauren J, Osman, Toba A M, Booy, Frank P, Coutts, Robert H A, Brasier, Clive M, Buck, Kenneth W

“…The complete nucleotide sequences of two double-stranded (ds) RNA molecules, S1 (1,744 bp) and S2 (1,567 bp), isolated from an isolate HP62 of the Himalayan…”
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Uncoating the Herpes Simplex Virus Genome by Newcomb, William W., Booy, Frank P., Brown, Jay C.

“…Initiation of infection by herpes simplex virus (HSV-1) involves a step in which the parental virus capsid docks at a nuclear pore and injects its DNA into the…”
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Molecular Tectonic Model of Virus Structural Transitions: the Putative Cell Entry States of Poliovirus by Belnap, D M, Filman, D J, Trus, B L, Cheng, N, Booy, F P, Conway, J F, Curry, S, Hiremath, C N, Tsang, S K, Steven, A C, Hogle, J M

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The filamentous type III secretion translocon of enteropathogenic Escherichia coli by Daniell, Sarah J., Takahashi, Noriko, Wilson, Rebecca, Friedberg, Devorah, Rosenshine, Ilan, Booy, Frank P., Shaw, Robert K., Knutton, Stuart, Frankel, Gad, Aizawa, Shin‐Ichi

“…Enteropathogenic Escherichia coli (EPEC) uses a type III secretion system (TTSS) to inject effector proteins into the plasma membrane and cytosol of infected…”
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Assembly of the Herpes Simplex Virus Capsid: Characterization of Intermediates Observed During Cell-free Capsid Formation by Newcomb, William W., Homa, Fred L., Thomsen, Darrell R., Booy, Frank P., Trus, Benes L., Steven, Alasdair C., Spencer, Juliet V., Brown, Jay C.

“…The herpes simplex virus-1 (HSV-1) capsid is an icosahedral shell approximately 15 nm thick and 125 nm in diameter. Three of its primary structural components…”
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Conformational Intermediates and Fusion Activity of Influenza Virus Hemagglutinin by Korte, T, Ludwig, K, Booy, F P, Blumenthal, R, Herrmann, A

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At Sixes and Sevens: Characterization of the Symmetry Mismatch of the ClpAP Chaperone-Assisted Protease by Beuron, Fabienne, Maurizi, Michael R., Belnap, David M., Kocsis, Eva, Booy, Frank P., Kessel, Martin, Steven, Alasdair C.

“…ClpAP, a typical energy-dependent protease, consists of a proteolytic component (ClpP) and a chaperone-like ATPase (ClpA). ClpP is composed of two apposed…”
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L1 Interaction Domains of Papillomavirus L2 Necessary for Viral Genome Encapsidation by Okun, M M, Day, P M, Greenstone, H L, Booy, F P, Lowy, D R, Schiller, J T, Roden, R B

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Structure of the herpes simplex virus capsid. Molecular composition of the pentons and the triplexes by Newcomb, W W, Trus, B L, Booy, F P, Steven, A C, Wall, J S, Brown, J C

“…The molecular anatomy of the herpes simplex virus (HSV-1) capsid has been examined by conventional electron microscopy, cryoelectron microscopy combined with…”
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Two antibodies that neutralize papillomavirus by different mechanisms show distinct binding patterns at 13 Å resolution by Booy, Frank P, Roden, Richard B.S, Greenstone, Heather L, Schiller, John T, Trus, Benes L

“…Complexes between bovine papillomavirus type 1 (BPV1) and examples of two sets of neutralizing, monoclonal antibodies (mAb) to the major capsid protein (L1)…”
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Voltage-gated K+ channel from mammalian brain: 3D structure at 18A of the complete (alpha)4(beta)4 complex by Orlova, Elena V, Papakosta, Marianthi, Booy, Frank P, van Heel, Marin, Dolly, J Oliver

“…Voltage-sensitive K(+) channels (Kv) serve numerous important roles, e.g. in the control of neuron excitability and the patterns of synaptic activity. Here, we…”
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The making and breaking of symmetry in virus capsid assembly: glimpses of capsid biology from cryoelectron microscopy by Steven, Alasdair C., Trus, Benes L., Booy, Frank P., Cheng, Naiqian, Zlotnick, Adam, Caston, Jose R., Conway, James F.

“…Virus capsids constitute a diverse and versatile family of protein‐bound containers and compartments ranging in diameter from ~200 Å (mass~1 MDa) to >1500 Å…”
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Structure of the Herpes Simplex Virus Capsid: Peptide A862-H880 of the Major Capsid Protein Is Displayed on the Rim of the Capsomer Protrusions by Spencer, Juliet V, Trus, Benes L, Booy, Frank P, Steven, Alasdair C, Newcomb, William W, Brown, Jay C

“…The herpes simplex virus-1 (HSV-1) capsid shell has 162 capsomers arranged on aT= 16 icosahedral lattice. The major capsid protein, VP5 (MW = 149,075) is the…”
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Cryo-crinkling: what happens to carbon films on copper grids at low temperature by Booy, F P, Pawley, J B

“…A study of the surface flatness of carbon films on copper grids used for cryo-electron microscopy has been carried out using a Hitachi S-900 low-voltage SEM…”
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Voltage-gated K + Channel from Mammalian Brain: 3D Structure at 18 Å of the Complete (α) 4(β) 4 Complex by Orlova, Elena V., Papakosta, Marianthi, Booy, Frank P., van Heel, Marin, Dolly, J.Oliver

“…Voltage-sensitive K + channels (Kv) serve numerous important roles, e.g. in the control of neuron excitability and the patterns of synaptic activity. Here, we…”
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