Search Results - "Gorovits, B M"

The Chaperonin GroEL Is Destabilized by Binding of ADP () by Gorovits, Boris M., Horowitz, Paul M.

“…The urea-induced dissociation and subsequent conformational transitions of the nucleotide-bound form of GroEL were studied by light scattering,…”
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High Hydrostatic Pressure Can Reverse Aggregation of Protein Folding Intermediates and Facilitate Acquisition of Native Structure by Gorovits, Boris M, Horowitz, Paul M

“…The present work demonstrates that high hydrostatic pressure can increase protein folding by reducing nonspecific aggregation. Protein aggregation is one of…”
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New immunoassay technique using antibody immobilized on a membrane and a flow cuvette as reaction vessel by Gorovits, B M, Osipov, A P, Egorov, A M

“…Immunoenzymatic detection systems have been developed using human IgG as a model antigen. A membrane with covalently immobilized specific antibodies was placed…”
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Productive and Nonproductive Intermediates in the Folding of Denatured Rhodanese by Panda, M, Gorovits, B M, Horowitz, P M

“…The competition between protein aggregation and folding has been investigated using rhodanese (thiosulfate:cyanide sulfurtransferase, EC 2.8.1.1 ) as a model…”
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A Visual Membrane Immunoassay for the Detection of Methamphetamine Using an Enzyme-Labeled Tracer Derived from Methamphetamine and Amphetamine by CHOI, Myung Ja, GOROVITS, Boris M., CHOI, Jeongeun, SONG, EunYoung, NAM, Kyung Soo, PARK, Jongsei

“…A visual membrane enzyme immunoassay is described for the measurement of methamphetamine in urine. To increase assay sensitivity, tracers with chemically…”
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Reversible Oligomerization and Denaturation of the Chaperonin GroES by Seale, Jeffrey W., Gorovits, Boris M., Ybarra, Jesse, Horowitz, Paul M.

“…The chaperonin GroEL can assist protein folding and normally acts with the co-chaperonin GroES. These Escherichia coli proteins are encoded on the same operon,…”
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The Molecular Chaperonin cpn60 Displays Local Flexibility That Is Reduced after Binding with an Unfolded Protein by Gorovits, Boris M., Horowitz, Paul M.

“…Steady-state fluorescence polarization was used to examine the chaperonin cpn60 that was covalently labeled with pyrene. Two compounds, 1-pyrenesulfonyl…”
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Residual Structure in Urea-Denatured Chaperonin GroEL by Gorovits, Boris M, Seale, Jeffrey W, Horowitz, Paul M

“…The urea denaturation of the chaperonin GroEL has been studied by circular dichroism, intrinsic tyrosine fluorescence and fluorescence of the hydrophobic…”
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Conditions of Forming Protein Complexes with GroEL Can Influence the Mechanism of Chaperonin-assisted Refolding by Gorovits, B M, Horowitz, P M

“…The interaction of GroEL with urea-unfolded dihydrofolate reductase (DHFR) has been studied in the presence of DHFR substrates by investigating the ability of…”
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Fluorescence anisotropy method for investigation of GroEL-GroES interaction by Gorovits, B M, Horowitz, P M

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ATP Hydrolysis Is Critical for Induction of Conformational Changes in GroEL That Expose Hydrophobic Surfaces by Gorovits, Boris M., Ybarra, Jesse, Horowitz, Paul M.

“…The degree of hydrophobic exposure in the molecular chaperone GroEL during its cycle of ATP hydrolysis was analyzed using…”
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Intrinsic Fluorescence Studies of the Chaperonin GroEL Containing Single Tyr → Trp Replacements Reveal Ligand-induced Conformational Changes by Gibbons, Don L., Hixson, John D., Hay, Nicki, Lund, Peter, Gorovits, Boris M., Ybarra, Jesse, Horowitz, Paul M.

“…Two mutants of GroEL containing the single tyrosine to tryptophan replacement of either residue 203 or 360 in the apical domain have been purified,…”
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Rhodanese folding is controlled by the partitioning of its folding intermediates by Gorovits, Boris M, McGee, William A, Horowitz, Paul M

“…Rhodanese is used widely as a model for protein folding, since the enzyme as usually studied refolds poorly unless the process is assisted. Here, the influence…”
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Conditions for nucleotide-dependent GroES-GroEL interactions. GroEL14(groES7)2 is favored by an asymmetric distribution of nucleotides by Gorovits, B M, Ybarra, J, Seale, J W, Horowitz, P M

“…A still unresolved question regarding the mechanism of chaperonin-assisted protein folding involves the stoichiometry of the GroEL-GroES complex. This is…”
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Conditions for nucleotide-dependent GroES-GroEL interactions. GroEL sub(14)(GroES sub(7)) sub(2) is favored by an asymmetric distribution of nucleotides by Gorovits, B M, Ybarra, J, Seale, J W, Horowitz, P M

“…A still unresolved question regarding the mechanism of chaperonin-assisted protein folding involves the stoichiometry of the GroEL-GroES complex. This is…”
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Intrinsic fluorescence studies of the chaperonin GroEL containing single Tyr arrow right Trp replacements reveal ligand-induced conformational changes by Gibbons, D L, Hixson, J D, Hay, N, Lund, P, Gorovits, B M, Ybarra, J, Horowitz, P M

“…Two mutants of GroEL containing the single tyrosine to tryptophan replacement of either residue 203 or 360 in the apical domain have been purified,…”
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Phytoecdysteroids of plants of the genusSilene by Saatov, Z., Gorovits, M. B., Abubakirov, N. K.

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Triterpene glycosides of Astragalus and their genins XXX. Cycloaraloside A from Astragalus amarus by Isaev, M. I., Gorovits, M. B., Abubakirov, N. K.

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Phytoecdysteroids of the plant Dianthus hoeltzeri by Saatov, Z., Gorovits, M. B., Abubakirov, N. K.

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Progress in the chemistry of the cycloartanes by Isaev, M. I., Gorovits, M. B., Abubakirov, N. K.

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