Citations

We report a method to improve image quality in the nondestructive investigation and visualization of defects using vibroacoustography (VA). Vibroacoustography is an ultrasound-based imaging technique that uses the dynamic (oscillatory) radiation force of low-frequency excitation (within kilohertz range) to remotely vibrate objects and detect the ensuing acoustic emission. This technique is nondestructive and noncontact and has shown numerous capabilities to produce high-resolution images of different types of materials. However, for reflective materials, ultrasound reflects back and forth between the object and transducer, thus establishing standing waves. This phenomenon produces an artifact in the shape of false contours in the VA images. The goal of this study is to investigate the formation of the standing wave artifacts and develop a process called chirp imaging to improve defect visibility and flaw detection capability. Chirp VA experiments are performed on a flawed fiber-reinforced ceramic composite plate and on an electronic chip. To assess the efficacy of the chirp imaging process in removing the standing-wave artifact, the resulting chirp images are compared to “fixed frequency” VA images. Results show that the false contour can be significantly reduced in the image, thus remarkably improving image quality and flaw detection.

ABSTRACT The human immunodeficiency virus type 1 (HIV-1) protein Vpr (viral protein R) arrests cells in the G 2 phase of the cell cycle, a process that requires activation of the ATR (ataxia-telangiectasia and Rad3-related) pathway. In this study we demonstrate that the expression of Vpr does not cause DNA double-strand breaks but rather induces ATR activation, as indicated by induction of Chk1 phosphorylation and the formation of γ-H2AX and 53BP1 nuclear foci. We define a C-terminal domain containing repeated H(F/S)RIG sequences required for Vpr-induced activation of ATR. Further investigation of the mechanism by which Vpr activates the ATR pathway reveals an increase in chromatin binding of replication protein A (RPA) upon Vpr expression. Immunostaining shows that RPA localizes to nuclear foci in Vpr-expressing cells. Furthermore, we demonstrate direct binding of Vpr to chromatin in vivo, whereas Vpr C-terminal domain mutants lose this chromatin-binding activity. These data support a mechanism whereby HIV-1 Vpr induces ATR activation by targeting the host cell DNA and probably interfering with normal DNA replication.