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292 Aktuelle Fachpublikationen zum Thema Addition

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Systematic Perturbations of Binuclear Non-heme Iron Sites: Structure and Dioxygen Reactivity of de Novo Due Ferri Proteins

24.07.2015 | Rae Ana Snyder; Justine Betzu; Susan E. Butch; Amanda J. Reig; William F. DeGrado; Edward I. Solomon, Biochemistry, 2015

DFsc (single-chain due ferri) proteins allow for modeling binuclear non-heme iron enzymes with a similar fold. Three 4A → 4G variants of DFsc were studied to investigate the effects of (1) increasing the size of the substrate/solvent access channel (G4DFsc), (2) including an additional His ...

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Decoding the Matrix: Instructive Roles of Proteoglycan Receptors

22.07.2015 | Thomas Neill; Liliana Schaefer; Renato V. Iozzo, Biochemistry, 2015

The extracellular matrix is a dynamic repository harboring instructive cues that embody substantial regulatory dominance over many evolutionarily conserved intracellular activities, including proliferation, apoptosis, migration, motility, and autophagy. The matrix also coordinates and parses ...

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Neural Zinc Finger Factor/Myelin Transcription Factor Proteins: Metal Binding, Fold, and Function

16.07.2015 | Angelique N. Besold; Sarah L. J. Michel, Biochemistry, 2015

Zinc finger (ZF) proteins make up a large family of metalloproteins that contain discrete domains with amino acid ligands (cysteine and histidine) that serve to coordinate zinc in a tetrahedral geometry. Upon zinc coordination, the domains adopt three-dimensional structure. The most well-studied ...

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Chemically Induced Changes to Membrane Permeability in Living Cells Probed with Nonlinear Light Scattering

15.07.2015 | Michael J. Wilhelm; Mohammad Sharifian Gh.; Hai-Lung Dai, Biochemistry, 2015

Second-harmonic light scattering (SHS) permits characterization of membrane-specific molecular transport in living cells. Herein, we demonstrate the use of time-resolved SHS for quantifying chemically induced enhancements in membrane permeability. As proof of concept, we examine the enhanced ...

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G Protein-Coupled Receptor Kinase 2 (GRK2) and 5 (GRK5) Exhibit Selective Phosphorylation of the Neurotensin Receptor in Vitro

08.07.2015 | Sayaka Inagaki; Rodolfo Ghirlando; Sergey A. Vishnivetskiy; Kristoff T. Homan; Jim F. White; John J. G. Tesmer; Vsev ..., Biochemistry, 2015

G protein-coupled receptor kinases (GRKs) play an important role in the desensitization of G protein-mediated signaling of G protein-coupled receptors (GPCRs). The level of interest in mapping their phosphorylation sites has increased because recent studies suggest that the differential pattern ...

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Investigating the in Vitro Thermal Stability and Conformational Flexibility of Estrogen Receptors as Potential Key Factors of Their in Vivo Activity

18.06.2015 | Adélaïde Le Grand; Gwenaëlle André-Leroux; Gaëlle Marteil; Hélène Duval; Olivier Sire; Véronique Le Tilly, Biochemistry, 2015

Among hormone-inducible transcription factors, estrogen receptors (ERs) play important roles in tissue growth and differentiation, via either direct or indirect binding, in the nucleus, to specific DNA targets called estrogen responsive elements (EREs), or through nongenomic pathways. In humans, ...

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Cation-Specific Conformations in a Dual-Function Ion-Pumping Microbial Rhodopsin

17.06.2015 | Giordano F. Z. da Silva; Brandon R. Goblirsch; Ah-Lim Tsai; John L. Spudich, Biochemistry, 2015

A recently discovered rhodopsin ion pump (DeNaR, also known as KR2) in the marine bacterium Dokdonia eikasta uses light to pump protons or sodium ions from the cell depending on the ionic composition of the medium. In cells suspended in a KCl solution, DeNaR functions as a light-driven proton ...

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The Human Iron–Sulfur Assembly Complex Catalyzes the Synthesis of [2Fe-2S] Clusters on ISCU2 That Can Be Transferred to Acceptor Molecules

12.06.2015 | Nicholas G. Fox; Mrinmoy Chakrabarti; Sean P. McCormick; Paul A. Lindahl; David P. Barondeau, Biochemistry, 2015

Iron–sulfur (Fe–S) clusters are essential protein cofactors for most life forms. In human mitochondria, the core Fe–S biosynthetic enzymatic complex (called SDUF) consists of NFS1, ISD11, ISCU2, and frataxin (FXN) protein components. Few mechanistic details about how this complex synthesizes Fe–S ...

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Correlations between the Electronic Properties of Shewanella oneidensis Cytochrome c Nitrite Reductase (ccNiR) and Its Structure: Effects of Heme Oxidation State and Active Site Ligation

12.06.2015 | Natalia Stein; Daniel Love; Evan T. Judd; Sean J. Elliott; Brian Bennett; A. Andrew Pacheco, Biochemistry, 2015

The electrochemical properties of Shewanella oneidensis cytochrome c nitrite reductase (ccNiR), a homodimer that contains five hemes per protomer, were investigated by UV–visible and electron paramagnetic resonance (EPR) spectropotentiometries. Global analysis of the UV–vis spectropotentiometric ...

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HYSCORE Analysis of the Effects of Substrates on Coordination of Water to the Active Site Iron in Tyrosine Hydroxylase

09.06.2015 | John McCracken; Bekir E. Eser; Donald Mannikko; Matthew D. Krzyaniak; Paul F. Fitzpatrick, Biochemistry, 2015

Tyrosine hydroxylase is a mononuclear non-heme iron monooxygenase found in the central nervous system that catalyzes the hydroxylation of tyrosine to yield l-3,4-dihydroxyphenylalanine, the rate-limiting step in the biosynthesis of catecholamine neurotransmitters. Catalysis requires the binding ...

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