Search results for "Structural Biology."

Photoaffinity cross-linking of F1ATPase from spinach chloroplasts by 3'-arylazido-beta-alanyl-8-azido ATP.

1994

UV irradiation of the ATPase (CF1) from spinach chloroplasts in the presence of 3'-arylazido-beta-alanyl-8-azido ATP (8,3'-DiN3ATP) results in a nucleotide-dependent inactivation of the enzyme and in a nucleotide-dependent formation of alpha-beta cross-links. The results demonstrate an interfacial localization of the nucleotide binding sites on CF1.

Enhanced susceptibility of cholesteryl sulfate-enriched low density lipoproteins to copper-mediated oxidation

1995

AbstractCholesteryl sulfate (CS) is a minor component of cell membranes, also present in lipoproteins, and its exact function is unknown. Since oxidation of low density lipoproteins (LDL) is thought to be an important determinant of atherogenesis, we investigated the influence of CS enrichment on copper-mediated oxidation of LDL. CS was found to act as a pro-oxidant, as measured by lipid oxidation parameters. The results also suggest that these effects were dependent on the sulfate group since pure cholesterol or cholesteryl acetate did not promote Cu2+-mediated oxidation. Our findings imply that CS may affect the oxidizability and hence the potential atherogenicity of LDL.

Pro-oxidant effects of 7-hydroperoxycholest-5-en-3β-ol on the copper-initiated oxidation of low density lipoprotein

1995

AbstractIn low density lipoproteins (LDL) supplemented with aged cholesterol and oxidized in the presence of Cu2+, an increase of the lipid oxidation parameters was observed compared with pure cholesterol-enriched LDL. A compound, identified as 7-hydroperoxycholesterol (7HPC), isolated from aged cholesterol and added to LDL, reproduced the above effects. The results indicate that the pro-oxidant effect of 7HPC is dependent on the hydroperoxy group since the corresponding alcohol derivative, 7α-hydroxycholesterol, had no such effect. These data suggest that among the LDL-associated lipid peroxides, cholesterol peroxides may have important implications in the susceptibility of this lipoprotei…

Scanning electron microscopy of Antarctophthirus microchir (Phthiraptera: Anoplura: Echinophthiriidae): Studying morphological adaptations to aquatic…

2012

The members of the Family Echinophthiriidae (Phthiraptera: Anoplura) are unique among insects because they infest hosts with an amphibious lifestyle. During their evolution they developed morphological traits that are reflected in unique features. The SEM is a helpful tool to analyze them. Knowing in detail the external structure of these lice is the first step to understand the whole process that derived from the co-adaptation of lice and pinnipeds to the marine environment. For the first time, we studied the external structure of all stages of an echinophthiriid louse. The results are discussed in the light of their evolutionary, functional, and ecological implications. Fil: Leonardi, Mar…

Desipramine induces disorder in cholesterol-rich membranes:implications for viral trafficking

2009

In this study, the effect of desipramine (DMI) on phospholipid bilayers and parvoviral entry was elucidated. In atomistic molecular dynamics simulations, DMI was found to introduce disorder in cholesterol-rich phospholipid bilayers. This was manifested by a decrease in the deuterium order parameter S(CD) as well as an increase in the membrane area. Disordering of the membrane suggested DMI to destabilize cholesterol-rich membrane domains (rafts) in cellular conditions. To relate the raft disrupting ability of DMI with novel biological relevance, we studied the intracellular effect of DMI using canine parvovirus (CPV), a virus known to interact with endosomal membranes and sphingomyelin, as …

Expression and subcellular targeting of canine parvovirus capsid proteins in baculovirus-transduced NLFK cells

2004

AbstractA mammalian baculovirus delivery system was developed to study targeting in Norden Laboratories feline kidney (NLFK) cells of the capsid proteins of canine parvovirus (CPV), VP1 and VP2, or corresponding counterparts fused to EGFP. VP1 and VP2, when expressed alone, both had equal nuclear and cytoplasmic distribution. However, assembled form of VP2 had a predominantly cytoplasmic localization. When VP1 and VP2 were simultaneously present in cells, their nuclear localization increased. Thus, confocal immunofluorescence analysis of cells transduced with the different baculovirus constructs or combinations thereof in the absence or presence of infecting CPV revealed that the VP1 protei…

Unusual Intranuclear Inclusions in Malignant Fibrous Histiocytoma: Presence in Primary Tumor

1982

We describe previously unreported intranuclear inclusions in 2 cases of malignant fibrous histiocytoma. The inclusions were found in 2-10% of the tumor cells removed from the patients and in 2-10% of the cells examined in tumor tissue xenotransplanted in nude mice. By stereo electron microscopy the inclusions are closely packed undulating fibrils 18-23 nm in diameter. They are sometimes associated with fibrillary bodies. They closely resemble the inclusions reported in some animals inoculated with serum from patients with non-A non-B hepatitis; however, their nature at present is unknown.

2005

2007

Topology of the 10 subunits within the decamer of KLH, the hemocyanin of the marine gastropod Megathura crenulata.

2002

Immunoelectron microscopy has been performed using negatively stained immune complexes of keyhole limpet hemocyanin isoform 1 (KLH1) decamers and a functional unit-specific monoclonal antibody anti-KLH1-c1. The antibody links hemocyanin molecules at both the collar and the collarless edge of the decamer, indicating a peripheral localization of functional units c. In isoform 2 (KLH2) the positions of functional units c have been identified with the peanut agglutinin (PNA), which has previously been shown to exclusively bind to KLH2-c. Ferritin linked to PNA was used to visualize labeled molecules electron microscopically. The pattern of labeling also indicates a peripheral localization of th…