Search Results - "Gogol, Edward P."

Dynamic Assembly of MinD on Phospholipid Vesicles Regulated by ATP and MinE by Hu, Zonglin, Gogol, Edward P., Lutkenhaus, Joe

“…Selection of the division site in Escherichia coli is regulated by the min system and requires the rapid oscillation of MinD between the two halves of the cell…”
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Asymmetric Cryo-EM Structure of Anthrax Toxin Protective Antigen Pore with Lethal Factor N-Terminal Domain by Machen, Alexandra J, Akkaladevi, Narahari, Trecazzi, Caleb, O'Neil, Pierce T, Mukherjee, Srayanta, Qi, Yifei, Dillard, Rebecca, Im, Wonpil, Gogol, Edward P, White, Tommi A, Fisher, Mark T

“…The anthrax lethal toxin consists of protective antigen (PA) and lethal factor (LF). Understanding both the PA pore formation and LF translocation through the…”
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Nucleotide‐induced switch in oligomerization of the AAA+ ATPase ClpB by Akoev, Vladimir, Gogol, Edward P., Barnett, Micheal E., Zolkiewski, Michal

“…ClpB is a member of the bacterial protein‐disaggregating chaperone machinery and belongs to the AAA+ superfamily of ATPases associated with various cellular…”
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Calmodulin-induced structural changes in endothelial nitric oxide synthase by Persechini, Anthony, Tran, Quang-Kim, Black, D.J., Gogol, Edward P.

“…► Structures of intact eNOS±CaM have been derived from cryo-electron micrographs. ► The reductase domains appear to be mobile with respect to the oxygenase…”
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GroEL as a molecular scaffold for structural analysis of the anthrax toxin pore by Gogol, Edward P, Katayama, Hiroo, Falke, Scott, Brzozowski, Marek, Fisher, Mark T, Juryck, Jordan, Janowiak, Blythe E, Collier, R John

“…The protective antigen (PA) moiety of anthrax toxin exists as a stable prepore, converting into the pore form under low pH to translocate the enzymatic…”
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Following Natures Lead: On the Construction of Membrane-Inserted Toxins in Lipid Bilayer Nanodiscs by Akkaladevi, Narahari, Mukherjee, Srayanta, Katayama, Hiroo, Janowiak, Blythe, Patel, Deepa, Gogol, Edward P., Pentelute, Bradley L., John Collier, R., Fisher, Mark T.

“…Bacterial toxin or viral entry into the cell often requires cell surface binding and endocytosis. The endosomal acidification induces a limited…”
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A Ca(2+)-dependent global conformational change in the 3D structure of phosphorylase kinase obtained from electron microscopy by Nadeau, Owen W, Carlson, Gerald M, Gogol, Edward P

“…Phosphorylase kinase (PhK), a Ca(2+)-dependent regulatory enzyme of the glycogenolytic cascade in skeletal muscle, is a 1.3 MDa hexadecameric oligomer…”
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The effects of the flavonoid baicalein and osmolytes on the Mg 2+ accelerated aggregation/fibrillation of carboxymethylated bovine 1SS-α-lactalbumin by Bomhoff, Greg, Sloan, Kirk, McLain, Corey, Gogol, Edward P., Fisher, Mark T.

“…Many protein conformational diseases arise when proteins form alternative stable conformations, resulting in aggregation and accumulation of the protein as…”
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The Phage T4-coded DNA Replication Helicase (gp41) Forms a Hexamer upon Activation by Nucleoside Triphosphate (∗) by Dong, Feng, Gogol, Edward P., von Hippel, Peter H.

“…Sedimentation and high performance liquid chromatography studies show that the functional DNA replication helicase of bacteriophage T4 (gp41) exists primarily…”
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Cryoelectron microscopy reveals new features in the three‐dimensional structure of phosphorylase kinase by Nadeau, Owen W., Gogol, Edward P., Carlson, Gerald M.

“…Phosphorylase kinase (PhK), a regulatory enzyme in the cascade activation of glycogenolysis, is a 1.3‐MDa hexadecameric complex, (αβγδ)4. PhK comprises two…”
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Strategies for folding of affinity tagged proteins using GroEL and osmolytes by Katayama, Hiroo, McGill, Mitchell, Kearns, Andrew, Brzozowski, Marek, Degner, Nicholas, Harnett, Bliss, Kornilayev, Boris, Matković-Čalogović, Dubravka, Holyoak, Todd, Calvet, James P, Gogol, Edward P, Seed, John, Fisher, Mark T

“…Obtaining a proper fold of affinity tagged chimera proteins can be difficult. Frequently, the protein of interest aggregates after the chimeric affinity tag is…”
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The 13Å Structure of a Chaperonin GroEL–Protein Substrate Complex by Cryo-electron Microscopy by Falke, Scott, Tama, Florence, Brooks, Charles L., Gogol, Edward P., Fisher, Mark T.

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Formation of Proteasome−PA700 Complexes Directly Correlates with Activation of Peptidase Activity by Adams, George M, Crotchett, Brad, Slaughter, Clive A, DeMartino, George N, Gogol, Edward P

“…The proteolytic activity of the eukaryotic 20S proteasome is stimulated by a multisubunit activator, PA700, which forms both 1:1 and 2:1 complexes with the…”
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Cryoelectron microscopy of Escherichia coli F1 adenosinetriphosphatase decorated with monoclonal antibodies to individual subunits of the complex by Gogol, Edward P, Aggeler, R, Sagermann, M, Capaldi, Roderick A

“…Monoclonal antibodies directed against epitopes on each of the five subunits (alpha, beta, gamma, delta, and epsilon) of the Escherichia coli F1 ATPase (ECF1)…”
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Molecular architecture of Escherichia coli F1 adenosinetriphosphatase by Gogol, Edward P, Luecken, Uwe, Bork, Tracie, Capaldi, Roderick A

“…The structure of the E. coli F1 ATPase (ECF1) has been studied by a novel combination of two specimen preparation and image analysis techniques. The molecular…”
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Structure of the ATP synthase complex (ECF1F0) of Escherichia coli from cryoelectron microscopy by Luecken, Uwe, Gogol, Edward P, Capaldi, Roderick A

“…The structural relationship of the catalytic portion (ECF1) of the Escherichia coli F1F0 ATP synthase (ECF1F0) to the intact, membrane-bound complex has been…”
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The 13 Å Structure of a Chaperonin GroEL–Protein Substrate Complex by Cryo-electron Microscopy by Falke, Scott, Tama, Florence, Brooks, Charles L., Gogol, Edward P., Fisher, Mark T.

“…The 13 Å resolution structures of GroEL bound to a single monomer of the protein substrate glutamine synthetase (GS m), as well as that of unliganded GroEL…”
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Structure of theEscherichia coli ATP synthase and role of the ? and ? subunits in coupling catalytic site and proton channeling functions by Capaldi, Roderick A., Aggeler, Robert, Gogol, Edward P., Wilkens, Stephan

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A Ca2+-Dependent Global Conformational Change in the 3D Structure of Phosphorylase Kinase Obtained from Electron Microscopy by Nadeau, Owen W, Carlson, Gerald M, Gogol, Edward P

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The 13 angstroms structure of a chaperonin GroEL-protein substrate complex by cryo-electron microscopy by Falke, Scott, Tama, Florence, Brooks, 3rd, Charles L, Gogol, Edward P, Fisher, Mark T

“…The 13 angstroms resolution structures of GroEL bound to a single monomer of the protein substrate glutamine synthetase (GS(m)), as well as that of unliganded…”
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