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1.
Sci Rep ; 4: 4558, 2014 Apr 02.
Article in English | MEDLINE | ID: mdl-24691055

ABSTRACT

We investigate the magneto-transport properties of epitaxial graphene single-layer on 4H-SiC(0001), grown by atmospheric pressure graphitization in Ar, followed by H2 intercalation. We directly demonstrate the importance of saturating the Si dangling bonds at the graphene/SiC(0001) interface to achieve high carrier mobility. Upon successful Si dangling bonds elimination, carrier mobility increases from 3 000 cm(2)V(-1)s(-1) to >11 000 cm(2)V(-1)s(-1) at 0.3 K. Additionally, graphene electron concentration tends to decrease from a few 10(12) cm(-2) to less than 10(12) cm(-2). For a typical large (30 × 280 µm(2)) Hall bar, we report the observation of the integer quantum Hall states at 0.3 K with well developed transversal resistance plateaus at Landau level filling factors of ν = 2, 6, 10, 14... 42 and Shubnikov de Haas oscillation of the longitudinal resistivity observed from about 1 T. In such a device, the Hall state quantization at ν = 2, at 19 T and 0.3 K, can be very robust: the dissipation in electronic transport can stay very low, with the longitudinal resistivity lower than 5 mΩ, for measurement currents as high as 250 µA. This is very promising in the view of an application in metrology.

2.
Minerva Ginecol ; 57(6): 593-609, 2005 Dec.
Article in Italian | MEDLINE | ID: mdl-16306864

ABSTRACT

Urinary incontinence is a common clinical problem in female sex and occurs especially in postmenopausal women; this disease, that represents an economical problem for society, begins in young age, arises in middle age and increases in women more than 65 years old. Studies carried out on etiological factors involved in urinary incontinence show that estrogens enhance the trophism and vascularization of the muscular and fascial support of the pelvic floor, the growth of fibroblasts and the collagen metabolism in the superficial fascia in postmenopausal women. The postmenopausal estrogenic deficit could be related to many urogenital problems, but many researches performed on the effects of estrogens in urogenital postmenopausal homeostasis and of hormonal replacement therapy in postmenopausal incontinent women, did not show conclusive findings; for this reason, even if many authors attributed to menopause a role of major risk factor for incontinence, a direct correlation has never been confirmed. The treatment of postmenopausal female incontinence may be clinical and pharmacological, and includes a first step therapy (bladder training, biofeedback techniques, electrical pelvic floor stimulation) and a second step therapy (pharmacological therapy, bladder devices and surgical operations). In this review the clinical and pharmacological treatments, their efficacy and their application in incontinent postmenopausal women are described.


Subject(s)
Postmenopause , Urinary Incontinence/therapy , Biofeedback, Psychology , Female , Humans , Pelvic Floor , Urinary Incontinence/diagnosis , Urinary Incontinence/drug therapy , Urinary Incontinence/epidemiology , Urinary Incontinence/etiology
3.
J Cell Sci ; 114(Pt 15): 2819-29, 2001 Aug.
Article in English | MEDLINE | ID: mdl-11683415

ABSTRACT

A study was made of the localization and assembly of the VM32E protein, a putative vitelline membrane component of the Drosophila eggshell. The results highlight some unique features of this protein compared with the other proteins of the same gene family. At the time of its synthesis (stage 10), the VM32E protein is not detectable in polar follicle cells. However, it is able to move in the extracellular space around the oocyte and, by stage 11 is uniformly distributed in the vitelline membrane. During the terminal stages of oogenesis the VM32E protein is partially released from the vitelline membrane and becomes localized in the endochorion layer also. By analyzing transgenic flies carrying variously truncated VM32E proteins, we could identify the protein domains required for the proper assembly of the VM32E protein in the eggshell. The highly conserved vitelline membrane domain is implicated in the early interactions with other components and is required for cross-linking VM32E protein in the vitelline membrane. The terminal carboxylic domain is necessary for localization to the endochorion layer. Protein with the C-end domain deleted is localized solely to the vitelline membrane and cross-linked only in laid eggs, as occurs for the other vitelline membrane proteins.


Subject(s)
Egg Proteins/genetics , Oogenesis/physiology , Vitelline Membrane/chemistry , Vitelline Membrane/metabolism , Amino Acid Sequence , Animals , Animals, Genetically Modified , Blotting, Western , Drosophila melanogaster , Epitopes/genetics , Female , Microscopy, Immunoelectron , Molecular Sequence Data , Mutation/physiology , Protein Structure, Tertiary , Vitelline Membrane/ultrastructure
4.
Proc Natl Acad Sci U S A ; 98(6): 3074-9, 2001 Mar 13.
Article in English | MEDLINE | ID: mdl-11248034

ABSTRACT

The energy of DNA deformation plays a crucial and active role in its packaging and its function in the cell. Considerable effort has gone into developing methodologies capable of evaluating the local sequence-directed curvature and flexibility of a DNA chain. These studies thus far have focused on DNA constructs expressly tailored either with anomalous flexibility or curvature tracts. Here we demonstrate that these two structural properties can be mapped also along the chain of a "natural" DNA with any sequence on the basis of its scanning force microscope (SFM) images. To know the orientation of the sequence of the investigated DNA molecules in their SFM images, we prepared a palindromic dimer of the long DNA molecule under study. The palindromic symmetry also acted as an internal gauge of the statistical significance of the analysis carried out on the SFM images of the dimer molecules. It was found that although the curvature modulus is not efficient in separating static and dynamic contributions to the curvature of the population of molecules, the curvature taken with its direction (its sign in two dimensions) permits the direct separation of the intrinsic curvature from the flexibility contributions. The sequence-dependent flexibility seems to vary monotonically with the chain's intrinsic curvature; the chain rigidity was found to modulate as its local thermodynamic stability and does not correlate with the dinucleotide chain rigidities evaluation made from x-ray data by other authors.


Subject(s)
DNA, Bacterial/chemistry , Nucleic Acid Conformation , Plasmids/chemistry , Microscopy, Atomic Force/methods
5.
Dev Dyn ; 218(3): 499-506, 2000 Jul.
Article in English | MEDLINE | ID: mdl-10878615

ABSTRACT

The VM32E gene is differently expressed in the distinct cell domains composing the follicular epithelium. Our previous work on the VM32E gene defined the promoter regions required for the control of gene expression in the ventral and dorsal follicle domains. In this report, we present data from a finer dissection of each upstream regulatory region, allowing to draw the functional interactions among different regulatory elements. A 73-bp proximal region (-112/-39) contains regulatory element(s) to dictate the activation of the gene in the follicular epithelium. This region interacts with two other cis-regulatory elements and is absolutely required for their output. The first element (-206/ -113), individually unable to raise reporter expression, elicits gene activity in the ventral domain when joined to the proximal fragment; a second element (-348/-254) joined to the same proximal fragment sustains the full dorsal and ventral activity. Moreover, the ectopic expression driven by some promoter fragments in border or posterior cells uncovers the existence of specific negative regulatory elements. So, the follicular domain specificity of VM32E gene expression is achieved through the combined activities of cell-type specific positive and negative elements.


Subject(s)
Drosophila/embryology , Drosophila/genetics , Gene Expression Regulation, Developmental , Oogenesis/physiology , Regulatory Sequences, Nucleic Acid , Vitelline Membrane/physiology , Animals , Body Patterning , DNA Probes , Genes, Insect , Genes, Reporter , In Situ Hybridization , Models, Genetic , Recombinant Fusion Proteins , Transformation, Genetic , beta-Galactosidase/metabolism
6.
Dev Genes Evol ; 208(2): 106-12, 1998 Apr.
Article in English | MEDLINE | ID: mdl-9569352

ABSTRACT

In Drosophila a remarkable feature of oogenesis is the regression of the nurse cells after dumping their cytoplasmic contents into the oocyte. We have studied the nature of this process at the late stages of egg chamber development. In egg chambers DAPI staining shows highly condensed chromatin from stage 12 and TUNEL labelling shows DNA fragmentation up to stage 14. Gel electrophoresis of the end-labelled DNA, extracted from isolated egg chambers at the same stages of development, shows a ladder typical of apoptotic nuclei. This provides evidence that, during Drosophila oogenesis, the nurse cells undergo apoptosis. Apoptotic nuclei have also been detected in dumping-defective egg chambers, indicating that the cytoplasmic depletion of nurse cells is concurrent with but apparently not the cause of the process.


Subject(s)
Apoptosis , Drosophila melanogaster/physiology , Oogenesis , Ovary/cytology , Animals , Drosophila melanogaster/cytology , Female , Mutation
7.
Mol Gen Genet ; 254(3): 231-7, 1997 Apr 16.
Article in English | MEDLINE | ID: mdl-9150256

ABSTRACT

The Drosophila vitelline membrane protein gene VM32E is expressed according to a precise temporal and spatial program in the follicle cells. Results from germ line transformation experiments using different fragments of the -465/-39 VM32E region fused to the hsp/lacZ reporter gene revealed that the region -348/-39 is sufficient to confer the wild-type expression pattern. Within this segment, distinct cis-regulatory elements control VM32E expression in ventral and dorsal follicle cells. The region between -135/-113 is essential for expression of the VM32E gene in the ventral columnar follicle cells. Expression in the dorsal domain requires the two regions -348/-254 and -118/-39. Furthermore, the region -253/-119 appears to contain a negative element that represses gene activity in anterior centripetal cells. We suggest that the expression of the VM32E gene throughout the follicular epithelium is controlled by specific cis-regulatory elements acting in distinct spatial domains and following a precise developmental program.


Subject(s)
Drosophila melanogaster/genetics , Egg Proteins/genetics , Genes, Insect , Membrane Proteins/genetics , Vitelline Membrane , Animals , Gene Expression Regulation , Genes, Regulator , Promoter Regions, Genetic
8.
Dev Biol ; 159(2): 450-61, 1993 Oct.
Article in English | MEDLINE | ID: mdl-8104831

ABSTRACT

A putative membrane form of guanylate cyclase gene was identified in region 32 of the second chromosome of Drosophila melanogaster. The Drosophila protein has a single hydrophobic sequence that divides the protein into a putative extracellular region and a cytoplasmic catalytic region which contains tyrosine kinase and cyclase domains showing varying degrees of conservation with other guanylate and adenylate cyclases. The gene shows a very interrupted organization with small exons separated by small introns and a low level of expression. Transcripts have been localized in situ during oogenesis in the germarium and later in stages 10-14 of egg chamber development. The putative maternal transcript can be seen in very early embryos and reappears later as a product of zygotic gene expression.


Subject(s)
Drosophila melanogaster/genetics , Guanylate Cyclase/genetics , Zygote/metabolism , Amino Acid Sequence , Animals , Base Sequence , Cell Membrane/enzymology , Chromosome Mapping , DNA, Complementary/isolation & purification , Gene Expression , Guanylate Cyclase/analysis , Guanylate Cyclase/chemistry , Molecular Sequence Data , Organ Specificity
9.
Mol Gen Genet ; 230(3): 433-41, 1991 Dec.
Article in English | MEDLINE | ID: mdl-1662765

ABSTRACT

The abnormal oocyte phenotype is characterized by instability, as shown by the loss and reappearance of the abo maternal effect under specific genetic conditions. Our previous finding that a correlation exists between the abo phenotype and the presence of a blood transposon in region 32E, led us to perform an extensive genetic and molecular analysis of the most significant aspects of the abo phenotype in different genetic backgrounds. The results of these experiments can be summarized as follows: Complete reversion occurs only when the blood trnasposon is lost, thus definitively demonstrating that the insertion of the blood transposon in region 32E is the molecular event that causes the pleiotropic abo phenotype. Partial reversion can also occur without loss of the transposon indicating that different molecular pathways may be involved in the loss of the abo phenotype. Reappearance of the full abo phenotype can occur only in heterozygous lines constructed from partially revertant abo homozygous lines that have not lost the blood transposon.


Subject(s)
DNA Transposable Elements , Drosophila melanogaster/genetics , Animals , Drosophila melanogaster/physiology , Female , Heterozygote , Homozygote , Male , Mutation , Oocytes/physiology , Phenotype
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