Search Results - "Protasevich, I"

A gene optimization strategy that enhances production of fully functional P-glycoprotein in Pichia pastoris by Bai, Jiangping, Swartz, Douglas J, Protasevich, Irina I, Brouillette, Christie G, Harrell, Patina M, Hildebrandt, Ellen, Gasser, Brigitte, Mattanovich, Diethard, Ward, Andrew, Chang, Geoffrey, Urbatsch, Ina L

“…Structural and biochemical studies of mammalian membrane proteins remain hampered by inefficient production of pure protein. We explored codon optimization…”
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Structures of a minimal human CFTR first nucleotide-binding domain as a monomer, head-to-tail homodimer, and pathogenic mutant by Atwell, Shane, Brouillette, Christie G., Conners, Kris, Emtage, Spencer, Gheyi, Tarun, Guggino, William B., Hendle, Jorg, Hunt, John F., Lewis, Hal A., Lu, Frances, Protasevich, Irina I., Rodgers, Logan A., Romero, Rich, Wasserman, Stephen R., Weber, Patricia C., Wetmore, Diana, Zhang, Feiyu F., Zhao, Xun

“…Upon removal of the regulatory insert (RI), the first nucleotide binding domain (NBD1) of human cystic fibrosis transmembrane conductance regulator (CFTR) can…”
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Structure of a Complex of Human Lactoferrin N-lobe with Pneumococcal Surface Protein A Provides Insight into Microbial Defense Mechanism by Senkovich, Olga, Cook, William J., Mirza, Shaper, Hollingshead, Susan K., Protasevich, Irina I., Briles, David E., Chattopadhyay, Debasish

“…Human lactoferrin, a component of the innate immune system, kills a wide variety of microorganisms including the Gram positive bacteria Streptococcus…”
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Conformational Changes Relevant to Channel Activity and Folding within the first Nucleotide Binding Domain of the Cystic Fibrosis Transmembrane Conductance Regulator by Hudson, Rhea P., Chong, P.Andrew, Protasevich, Irina I., Vernon, Robert, Noy, Efrat, Bihler, Hermann, An, Jian Li, Kalid, Ori, Sela-Culang, Inbal, Mense, Martin, Senderowitz, Hanoch, Brouillette, Christie G., Forman-Kay, Julie D.

“…Deletion of Phe-508 (F508del) in the first nucleotide binding domain (NBD1) of the cystic fibrosis transmembrane conductance regulator (CFTR) leads to defects…”
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Role of Inhibitor Aliphatic Chain in the Thermodynamics of Inhibitor Binding to Escherichia coli Enoyl-ACP Reductase and the Phe203Leu Mutant:  A Proposed Mechanism for Drug Resistance by Protasevich, Irina I, Brouillette, Christie G, Snow, Mark E, Dunham, Steve, Rubin, J. Ronald, Gogliotti, Rocco, Siegel, Karen

“…The antibacterial target enoyl-acyl carrier protein (ACP) reductase is a homotetrameric enzyme that catalyzes the last reductive step of fatty acid…”
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Apocalmodulin Binds to the Myosin Light Chain Kinase Calmodulin Target Site by Tsvetkov, P O, Protasevich, I I, Gilli, R, Lafitte, D, Lobachov, V M, Haiech, J, Briand, C, Makarov, A A

“…The interaction of a 20-residue-long peptide derived from the calmodulin-binding domain of the smooth muscle myosin light chain kinase with calcium-free…”
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Comparative study of binase and barnase: experience in chimeric ribonucleases by Schulga, A, Kurbanov, F, Kirpichnikov, M, Protasevich, I, Lobachov, V, Ranjbar, B, Chekhov, V, Polyakov, K, Engelborghs, Y, Makarov, A

“…Chimeric enzymes were constructed to elucidate the differences in physicochemical properties of two related bacterial RNases, barnase and binase. Chimeras…”
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Valine 108, a Chain-Folding Initiation Site-Belonging Residue, Crucial for the Ribonuclease A Stability by Coll, M.G., Protasevich, I.I., Torrent, J., Ribó, M., Lobachov, V.M., Makarov, A.A., Vilanova, M.

“…Thermal denaturation of bovine pancreatic ribonuclease A and a set of its single variants, carrying replacements of hydrophobic residues in the postulated…”
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Key Role of Phenylalanine 20 in Cytochrome c3:  Structure, Stability, and Function Studies by Dolla, Alain, Arnoux, Pascal, Protasevich, Irina, Lobachov, Vladimir, Brugna, Marianne, Giudici-Orticoni, Marie Thérèse, Haser, Richard, Czjzek, Mirjam, Makarov, Alexander, Bruschi, M

“…Aromatic residues in c-type cytochromes might have an important function in the folding and/or electron transferring properties of the molecule. In the…”
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Thermal stability of the polyheme cytochrome c3 superfamily by Florens, L., Bianco, P., Haladjian, J., Bruschi, M., Protasevich, I., Makarov, A.

“…The cytochrome c 3 superfamily includes Desulfovibrio polyheme cytochromes c. We report the characteristic thermal stability parameters of the Desulfovibrio…”
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Förster Resonance Energy Transfer Measurements Are Consistent with a Helical Bundle Model for Lipid-Free Apolipoprotein A-I by Brouillette, Christie G, Dong, Wen-Ji, Yang, Zhengrong W, Ray, Marjorie J, Protasevich, Irina I, Cheung, Herbert C, Engler, Jeffrey A

“…Apolipoprotein (apo) A-I mutants were constructed for FRET studies to distinguish between two possible lipid-free conformers, a globular helix bundle and an…”
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Key role of barstar Cys-40 residue in the mechanism of heat denaturation of bacterial ribonuclease complexes with barstar by Protasevich, I.I, Schulga, A.A, Vasilieva, L.I, Polyakov, K.M, Lobachov, V.M, Hartley, R.W, Kirpichnikov, M.P, Makarov, A.A

“…The mechanism by which barnase and binase are stabilized in their complexes with barstar and the role of the Cys-40 residue of barstar in that stabilization…”
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Dissociation constants and thermal stability of complexes of Bacillus intermedius RNase and the protein inhibitor of Bacillus amyloliquefaciens RNase by Yakovlev, G.I., Moiseyev, G.P., Protasevich, I.I., Ranjbar, B., Bocharov, A.L., Kirpichnikov, M.P., Gilli, R.M., Briand, C.M., Hartley, R.W., Makarov, A.A.

“…Binase, the extracellular ribonuclease of Bacillus intermedius, is inhibited by barstar, the natural protein inhibitor of the homologous RNase, barnase, of B…”
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Structural adaptation of an interacting non-native C-terminal helical extension revealed in the crystal structure of NAD+ synthetase from Bacillus anthracis by McDonald, Heather M., Pruett, Pamela S., Deivanayagam, Champion, Protasevich, Irina I., Carson, W. Michael, DeLucas, Lawrence J., Brouillette, Wayne J., Brouillette, Christie G.

“…The crystal structures of NH3‐dependent NAD+ synthetase from Bacillus anthracis as the apoenzyme (1.9 Å), in complex with the natural catalytic products AMP…”
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Effect of modification of carbohydrate component on properties of glucoamylase by Neustroev, K.N., Golubev, A.M., Firsov, L.M., Ibatullin, F.M., Protasevich, I.I., Makarov, A.A.

“…In this study, we investigated enzymatic deglycosylation of glucoamylase from Aspergillus awamori X 100/D27, a glycoprotein which has two N-linked and about…”
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Deletion of DnaK's Lid Strengthens Binding to the Nucleotide Exchange Factor, GrpE:  A Kinetic and Thermodynamic Analysis by Chesnokova, Liudmila S, Slepenkov, Sergey V, Protasevich, Irina I, Sehorn, Michael G, Brouillette, Christie G, Witt, Stephan N

“…In this study, we have used surface plasmon resonance (SPR) and isothermal microtitration calorimetry (ITC) to study the mechanism of complex formation between…”
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Heat denaturation of pepsinogen in a water-ethanol mixture by Makarov, A.A., Protasevich, I.I., Bazhulina, N.P., Esipova, N.G.

“…The effect of ethanol and pH on thermodynamic parameters and cooperativity of pepsinogen heat denaturation was studied by scanning microcalorimetry. Addition…”
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Comparative study of monoclonal immunoglobulin M and rheumatoid immunoglobulin M by differential scanning microcalorimetry by Protasevich, I I, Ranjbar, B, Varlamova EYu, Cherkasov, I A, Lapuk, V A

“…Thermal denaturation of monoclonal immunoglobulin M (IgM) and rheumatoid immunoglobulin M (IgM-RF) and their Fab- and (Fc)5-fragments was studied by…”
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Thermostability of the barnase—barstar complex by Makarov, A.A., Protasevich, I.I., Lobachov, V.M., Kirpichnikov, M.P., Yakovlev, G.I., Gilli, R.M., Briand, C.M., Hartley, R.W.

“…Scanning microcalorimetry was used to study heat denaturation of barnase in complex with its intracellular inhibitor barstar. The heat denaturation of the…”
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Melting of the left-handed helical conformation of charged poly-L-lysine by Makarov, A A, Adzhubei, I A, Protasevich, I I, Lobachov, V M, Fasman, G D

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