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Scalp-sparing total skin electron therapy in mycosis fungoides: Case report featuring a technique without lead.
Patel CG, Ding G, Kirschner A
(2017) Pract Radiat Oncol 7: 400-402
MeSH Terms: Electrons, Humans, Male, Middle Aged, Mycosis Fungoides, Scalp, Skin Neoplasms, Treatment Outcome
Added April 2, 2019
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MeSH Terms
Predicting near-UV electronic circular dichroism in nucleosomal DNA by means of DFT response theory.
Norman P, Parello J, Polavarapu PL, Linares M
(2015) Phys Chem Chem Phys 17: 21866-79
MeSH Terms: Base Pairing, Circular Dichroism, DNA, B-Form, Electrons, Models, Molecular, Nucleosides, Nucleosomes, Quantum Theory, Spectrophotometry, Ultraviolet, Thermodynamics
Show Abstract · Added April 10, 2018
It is demonstrated that time-dependent density functional theory (DFT) calculations can accurately predict changes in near-UV electronic circular dichroism (ECD) spectra of DNA as the structure is altered from the linear (free) B-DNA form to the supercoiled N-DNA form found in nucleosome core particles. At the DFT/B3LYP level of theory, the ECD signal response is reduced by a factor of 6.7 in going from the B-DNA to the N-DNA form, and it is illustrated how more than 90% of the individual base-pair dimers contribute to this strong hypochromic effect. Of the several inter-base pair parameters, an increase in twist angles is identified as to strongly contribute to a reduced ellipticity. The present work provides first evidence that first-principles calculations can elucidate changes in DNA dichroism due to the supramolecular organization of the nucleoprotein particle and associates these changes with the local structural features of nucleosomal DNA.
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The signaling phospholipid PIP3 creates a new interaction surface on the nuclear receptor SF-1.
Blind RD, Sablin EP, Kuchenbecker KM, Chiu HJ, Deacon AM, Das D, Fletterick RJ, Ingraham HA
(2014) Proc Natl Acad Sci U S A 111: 15054-9
MeSH Terms: Amino Acids, Animals, Biological Transport, Cell Nucleus, Chromatography, Computer Simulation, Crystallography, X-Ray, Electrons, Humans, Ligands, Lipids, Mice, Models, Molecular, Molecular Conformation, Mutation, Mutation, Missense, Peptides, Phosphatidylinositols, Signal Transduction, Solvents, Steroidogenic Factor 1, Surface Plasmon Resonance, Surface Properties, Temperature, Water
Show Abstract · Added August 18, 2015
The signaling phosphatidylinositol lipids PI(4,5)P2 (PIP2) and PI(3,4,5)P3 (PIP3) bind nuclear receptor 5A family (NR5As), but their regulatory mechanisms remain unknown. Here, the crystal structures of human NR5A1 (steroidogenic factor-1, SF-1) ligand binding domain (LBD) bound to PIP2 and PIP3 show the lipid hydrophobic tails sequestered in the hormone pocket, as predicted. However, unlike classic nuclear receptor hormones, the phosphoinositide head groups are fully solvent-exposed and complete the LBD fold by organizing the receptor architecture at the hormone pocket entrance. The highest affinity phosphoinositide ligand PIP3 stabilizes the coactivator binding groove and increases coactivator peptide recruitment. This receptor-ligand topology defines a previously unidentified regulatory protein-lipid surface on SF-1 with the phosphoinositide head group at its nexus and poised to interact with other proteins. This surface on SF-1 coincides with the predicted binding site of the corepressor DAX-1 (dosage-sensitive sex reversal, adrenal hypoplasia critical region on chromosome X), and importantly harbors missense mutations associated with human endocrine disorders. Our data provide the structural basis for this poorly understood cluster of human SF-1 mutations and demonstrates how signaling phosphoinositides function as regulatory ligands for NR5As.
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25 MeSH Terms
Alkylation damage by lipid electrophiles targets functional protein systems.
Codreanu SG, Ullery JC, Zhu J, Tallman KA, Beavers WN, Porter NA, Marnett LJ, Zhang B, Liebler DC
(2014) Mol Cell Proteomics 13: 849-59
MeSH Terms: Aldehydes, Alkylation, Cell Line, Electrons, Glutathione, Humans, Lipids, Protein Interaction Maps, Proteins, Proteome
Show Abstract · Added March 20, 2014
Protein alkylation by reactive electrophiles contributes to chemical toxicities and oxidative stress, but the functional impact of alkylation damage across proteomes is poorly understood. We used Click chemistry and shotgun proteomics to profile the accumulation of proteome damage in human cells treated with lipid electrophile probes. Protein target profiles revealed three damage susceptibility classes, as well as proteins that were highly resistant to alkylation. Damage occurred selectively across functional protein interaction networks, with the most highly alkylation-susceptible proteins mapping to networks involved in cytoskeletal regulation. Proteins with lower damage susceptibility mapped to networks involved in protein synthesis and turnover and were alkylated only at electrophile concentrations that caused significant toxicity. Hierarchical susceptibility of proteome systems to alkylation may allow cells to survive sublethal damage while protecting critical cell functions.
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10 MeSH Terms
Structural refinement from restrained-ensemble simulations based on EPR/DEER data: application to T4 lysozyme.
Islam SM, Stein RA, McHaourab HS, Roux B
(2013) J Phys Chem B 117: 4740-54
MeSH Terms: Bacteriophage T4, Crystallography, X-Ray, Cyclic N-Oxides, Electron Spin Resonance Spectroscopy, Electrons, Mesylates, Molecular Dynamics Simulation, Muramidase, Protein Structure, Tertiary, Spin Labels
Show Abstract · Added February 19, 2015
DEER (double electron-electron resonance) is a powerful pulsed ESR (electron spin resonance) technique allowing the determination of distance histograms between pairs of nitroxide spin-labels linked to a protein in a native-like solution environment. However, exploiting the huge amount of information provided by ESR/DEER histograms to refine structural models is extremely challenging. In this study, a restrained ensemble (RE) molecular dynamics (MD) simulation methodology is developed to address this issue. In RE simulation, the spin-spin distance distribution histograms calculated from a multiple-copy MD simulation are enforced, via a global ensemble-based energy restraint, to match those obtained from ESR/DEER experiments. The RE simulation is applied to 51 ESR/DEER distance histogram data from spin-labels inserted at 37 different positions in T4 lysozyme (T4L). The rotamer population distribution along the five dihedral angles connecting the nitroxide ring to the protein backbone is determined and shown to be consistent with available information from X-ray crystallography. For the purpose of structural refinement, the concept of a simplified nitroxide dummy spin-label is designed and parametrized on the basis of these all-atom RE simulations with explicit solvent. It is demonstrated that RE simulations with the dummy nitroxide spin-labels imposing the ESR/DEER experimental distance distribution data are able to systematically correct and refine a series of distorted T4L structures, while simple harmonic distance restraints are unsuccessful. This computationally efficient approach allows experimental restraints from DEER experiments to be incorporated into RE simulations for efficient structural refinement.
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10 MeSH Terms
Targeted protein capture for analysis of electrophile-protein adducts.
Connor RE, Codreanu SG, Marnett LJ, Liebler DC
(2013) Methods Mol Biol 987: 163-76
MeSH Terms: Affinity Labels, Aldehydes, Benzoquinones, Blotting, Western, Cell Line, Tumor, Databases, Protein, Electrons, HSP90 Heat-Shock Proteins, Humans, Immunoprecipitation, Lactams, Macrocyclic, Mass Spectrometry, Protein Structure, Tertiary, Trypsin
Show Abstract · Added March 20, 2014
Proteomic analyses of protein-electrophile adducts generally employ affinity capture of the adduct moiety, which enables global analyses, but is poorly suited to targeted studies of specific proteins. We describe a targeted molecular probe approach to study modifications of the molecular chaperone heat-shock protein 90 (Hsp90), which regulates diverse client proteins. Noncovalent affinity capture with a biotinyl analog of the HSP90 inhibitor geldanamycin enables detection of the native protein isoforms Hsp90α and Hsp90β and their phosphorylated forms. We applied this probe to map and quantify adducts formed on Hsp90 by 4-hydroxynonenal (HNE) in RKO cells. This approach was also applied to measure the kinetics of site-specific adduction of selected Hsp90 residues. A protein-selective affinity capture approach is broadly applicable for targeted analysis of electrophile adducts and their biological effects.
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14 MeSH Terms
Conformation of receptor-bound visual arrestin.
Kim M, Vishnivetskiy SA, Van Eps N, Alexander NS, Cleghorn WM, Zhan X, Hanson SM, Morizumi T, Ernst OP, Meiler J, Gurevich VV, Hubbell WL
(2012) Proc Natl Acad Sci U S A 109: 18407-12
MeSH Terms: Arrestin, Crystallography, X-Ray, Electrons, Models, Molecular, Mutant Proteins, Phosphorylation, Protein Binding, Protein Multimerization, Protein Stability, Protein Structure, Secondary, Rhodopsin, Sequence Deletion, Solutions, Staining and Labeling, Temperature
Show Abstract · Added January 24, 2015
Arrestin-1 (visual arrestin) binds to light-activated phosphorylated rhodopsin (P-Rh*) to terminate G-protein signaling. To map conformational changes upon binding to the receptor, pairs of spin labels were introduced in arrestin-1 and double electron-electron resonance was used to monitor interspin distance changes upon P-Rh* binding. The results indicate that the relative position of the N and C domains remains largely unchanged, contrary to expectations of a "clam-shell" model. A loop implicated in P-Rh* binding that connects β-strands V and VI (the "finger loop," residues 67-79) moves toward the expected location of P-Rh* in the complex, but does not assume a fully extended conformation. A striking and unexpected movement of a loop containing residue 139 away from the adjacent finger loop is observed, which appears to facilitate P-Rh* binding. This change is accompanied by smaller movements of distal loops containing residues 157 and 344 at the tips of the N and C domains, which correspond to "plastic" regions of arrestin-1 that have distinct conformations in monomers of the crystal tetramer. Remarkably, the loops containing residues 139, 157, and 344 appear to have high flexibility in both free arrestin-1 and the P-Rh*complex.
1 Communities
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15 MeSH Terms
Nanometer-resolution electron microscopy through micrometers-thick water layers.
de Jonge N, Poirier-Demers N, Demers H, Peckys DB, Drouin D
(2010) Ultramicroscopy 110: 1114-9
MeSH Terms: Animals, Electrons, Eukaryotic Cells, Gold, Humans, Microscopy, Electron, Scanning Transmission, Monte Carlo Method, Nanoparticles, Nanotechnology, Water
Show Abstract · Added May 27, 2014
Scanning transmission electron microscopy (STEM) was used to image gold nanoparticles on top of and below saline water layers of several micrometers thickness. The smallest gold nanoparticles studied had diameters of 1.4 nm and were visible for a liquid thickness of up to 3.3 microm. The imaging of gold nanoparticles below several micrometers of liquid was limited by broadening of the electron probe caused by scattering of the electron beam in the liquid. The experimental data corresponded to analytical models of the resolution and of the electron probe broadening as function of the liquid thickness. The results were also compared with Monte Carlo simulations of the STEM imaging on modeled specimens of similar geometry and composition as used for the experiments. Applications of STEM imaging in liquid can be found in cell biology, e.g., to study tagged proteins in whole eukaryotic cells in liquid and in materials science to study the interaction of solid:liquid interfaces at the nanoscale.
Published by Elsevier B.V.
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10 MeSH Terms
Photosystem I - based biohybrid photoelectrochemical cells.
Ciesielski PN, Hijazi FM, Scott AM, Faulkner CJ, Beard L, Emmett K, Rosenthal SJ, Cliffel D, Kane Jennings G
(2010) Bioresour Technol 101: 3047-53
MeSH Terms: Biocatalysis, Bioelectric Energy Sources, Electricity, Electrons, Light, Models, Molecular, Photochemistry, Photosystem I Protein Complex, Plants
Show Abstract · Added May 27, 2014
Photosynthesis is the process by which Nature coordinates a tandem of protein complexes of impressive complexity that function to harness staggering amounts of solar energy on a global scale. Advances in biochemistry and nanotechnology have provided tools to isolate and manipulate the individual components of this process, thus opening a door to a new class of highly functional and vastly abundant biological resources. Here we show how one of these components, Photosystem I (PSI), is incorporated into an electrochemical system to yield a stand-alone biohybrid photoelectrochemical cell that converts light energy into electrical energy. The cells make use of a dense multilayer of PSI complexes assembled on the surface of the cathode to produce a photocatalytic effect that generates photocurrent densities of approximately 2 microA/cm(2) at moderate light intensities. We describe the relationship between the current and voltage production of the cells and the photoinduced interactions of PSI complexes with electrochemical mediators, and show that the performance of the present device is limited by diffusional transport of the electrochemical mediators through the electrolyte. These biohybrid devices display remarkable stability, as they remain active in ambient conditions for at least 280 days. Even at bench-scale production, the materials required to fabricate the cells described in this manuscript cost approximately 10 cents per cm(2) of active electrode area.
Copyright 2009 Elsevier Ltd. All rights reserved.
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9 MeSH Terms
Placement and orientation of individual DNA shapes on lithographically patterned surfaces.
Kershner RJ, Bozano LD, Micheel CM, Hung AM, Fornof AR, Cha JN, Rettner CT, Bersani M, Frommer J, Rothemund PW, Wallraff GM
(2009) Nat Nanotechnol 4: 557-61
MeSH Terms: Biocompatible Materials, Crystallization, DNA, Electrons, Materials Testing, Nanostructures, Nanotechnology, Nucleic Acid Conformation, Oxidation-Reduction, Surface Properties
Show Abstract · Added April 12, 2013
Artificial DNA nanostructures show promise for the organization of functional materials to create nanoelectronic or nano-optical devices. DNA origami, in which a long single strand of DNA is folded into a shape using shorter 'staple strands', can display 6-nm-resolution patterns of binding sites, in principle allowing complex arrangements of carbon nanotubes, silicon nanowires, or quantum dots. However, DNA origami are synthesized in solution and uncontrolled deposition results in random arrangements; this makes it difficult to measure the properties of attached nanodevices or to integrate them with conventionally fabricated microcircuitry. Here we describe the use of electron-beam lithography and dry oxidative etching to create DNA origami-shaped binding sites on technologically useful materials, such as SiO(2) and diamond-like carbon. In buffer with approximately 100 mM MgCl(2), DNA origami bind with high selectivity and good orientation: 70-95% of sites have individual origami aligned with an angular dispersion (+/-1 s.d.) as low as +/-10 degrees (on diamond-like carbon) or +/-20 degrees (on SiO(2)).
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10 MeSH Terms