Search Results - "Faber, Rick"

Biochemical and Crystallographic Characterization of Ferredoxin−NADP+ Reductase from Nonphotosynthetic Tissues by Aliverti, Alessandro, Faber, Rick, Finnerty, Casey M, Ferioli, Cristian, Pandini, Vittorio, Negri, Armando, Karplus, P. Andrew, Zanetti, Giuliana

“…Distinct forms of ferredoxin−NADP+ reductase are expressed in photosynthetic and nonphotosynthetic plant tissues. Both enzymes catalyze electron transfer…”
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Altered Domain Closure and Iron Binding in Transferrins: The Crystal Structure of the Asp60Ser Mutant of the Amino-terminal Half-molecule of Human Lactoferrin by Faber, Rick H., Bland, Tony, Day, Catherine L., Norris, Gillian E., Tweedie, John W., Baker, Edward N.

“…The crystal structure of a site-specific mutant of the N-terminal half-molecule of human lactoferrin, Lf N, in which the iron ligand Asp60 has been mutated to…”
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High‐resolution studies of hydride transfer in the ferredoxin:NADP+ reductase superfamily by Kean, Kelsey M., Carpenter, Russell A., Pandini, Vittorio, Zanetti, Giuliana, Hall, Andrea R., Faber, Rick, Aliverti, Alessandro, Karplus, P. Andrew

“…Ferredoxin: NADP+ reductase (FNR) is an FAD‐containing enzyme best known for catalysing the transfer of electrons from ferredoxin (Fd) to NADP+ to make NADPH…”
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Evolutionary analysis of the multigene pregnancy-specific β1-Glycoprotein family: Separation of historical and nonhistorical signals by McLenachan, Patricia A., Lockhart, Peter J., Rick Faber, H., Mansfield, Brian C.

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Mutation of Arginine 121 in Lactoferrin Destabilizes Iron Binding by Disruption of Anion Binding:  Crystal Structures of R121S and R121E Mutants by Faber, H. Rick, Baker, Christina J, Day, Catherine L, Tweedie, John W, Baker, Edward N

“…A conserved arginine residue helps to form the synergistic anion binding site in transferrins. To probe the importance of this residue for anion binding and…”
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Glycerol kinase from Escherichia coli and an Ala65→Thr mutant: the crystal structures reveal conformational changes with implications for allosteric regulation by Feese, Michael D, Faber, H Rick, Bystrom, Cory E, Pettigrew, Donald W, Remington, S James

“…Background: Glycerol kinase (GK) from Escherichia coli is a velocity-modulated (V system) enzyme that has three allosteric effectors with independent…”
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Escherichia coli Glycerol Kinase: Role of a Tetramer Interface in Regulation by Fructose 1,6-Bisphosphate and Phosphotransferase System Regulatory Protein IIIglc by Liu, Wei Zhang, Faber, Rick, Feese, Michael, Remington, S. James, Pettigrew, Donald W

“…Escherichia coli glycerol kinase (EC 2.7.1.30; ATP:glycerol 3-phosphotransferase) is a key element in a signal transduction pathway that couples expression of…”
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Structure of the Regulatory Complex of Escherichia coli III$^{Glc}$ with Glycerol Kinase by Hurley, James H., Faber, H. Rick, Worthylake, David, Meadow, Norman D., Roseman, Saul, Pettigrew, Donald W., Remington, S. James

“…The phosphocarrier protein III$^{Glc}$ is an integral component of the bacterial phosphotransferase (PTS) system. Unphosphorylated III$^{Glc}$ inhibits non-PTS…”
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A Lifting Theorem for Locally Convex Subspaces of Lo by Faber, Rick G

“…We prove that for every closed locally convex subspace $E$ of $L_0$ and for any continuous linear operator $T$ from $L_0$ to $L_0/E$ there is a continuous…”
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1.8 å crystal structure of the C-terminal domain of rabbit serum haemopexin by Faber, H.Rick, Groom, Colin R, Baker, Heather M, Morgan, William T, Smith, Ann, Baker, Edward N

“…Background: Haemopexin is a serum glycoprotein that binds haem reversibly and delivers it to the liver where it is taken up by receptor-mediated endocytosis…”
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Structure of the regulatory complex of Escherichia coli IIIGlc with glycerol kinase by Hurley, J H, Faber, H R, Worthylake, D, Meadow, N D, Roseman, S, Pettigrew, D W, Remington, S J

“…The phosphocarrier protein IIIGlc is an integral component of the bacterial phosphotransferase (PTS) system. Unphosphorylated IIIGlc inhibits non-PTS…”
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