[Letters from Doctors to the BRAC Commission - 2005] (open access)

[Letters from Doctors to the BRAC Commission - 2005]

Letters from several pathologists to the Defense Base Closure and Realignment Commission regarding the disestablishment of the AFIP and their opposition to the recommendation to close the facility.
Date: May 17, 2005
Creator: unknown
Object Type: Letter
System: The UNT Digital Library
Exploration of Simple Analytical Approaches for Rapid Detection of Pathogenic Bacteria (open access)

Exploration of Simple Analytical Approaches for Rapid Detection of Pathogenic Bacteria

Many of the current methods for pathogenic bacterial detection require long sample-preparation and analysis time, as well as complex instrumentation. This dissertation explores simple analytical approaches (e.g., flow cytometry and diffuse reflectance spectroscopy) that may be applied towards ideal requirements of a microbial detection system, through method and instrumentation development, and by the creation and characterization of immunosensing platforms. This dissertation is organized into six sections. In the general Introduction section a literature review on several of the key aspects of this work is presented. First, different approaches for detection of pathogenic bacteria will be reviewed, with a comparison of the relative strengths and weaknesses of each approach, A general overview regarding diffuse reflectance spectroscopy is then presented. Next, the structure and function of self-assembled monolayers (SAMs) formed from organosulfur molecules at gold and micrometer and sub-micrometer patterning of biomolecules using SAMs will be discussed. This section is followed by four research chapters, presented as separate manuscripts. Chapter 1 describes the efforts and challenges towards the creation of imunosensing platforms that exploit the flexibility and structural stability of SAMs of thiols at gold. 1H, 1H, 2H, 2H-perfluorodecyl-1-thiol SAM (PFDT) and dithio-bis(succinimidyl propionate)-(DSP)-derived SAMs were used to construct the platform. Chapter …
Date: December 17, 2005
Creator: Rahman, Salma
Object Type: Thesis or Dissertation
System: The UNT Digital Library
ISG 14 Minutes 10 October 2003 (open access)

ISG 14 Minutes 10 October 2003

Disregard Restriction Header and Footer - ISG 14 Minutes 10 October 2003
Date: October 17, 2005
Creator: United States. Department of Defense.
Object Type: Text
System: The UNT Digital Library
Technical Analysis - Ft Pickett (open access)

Technical Analysis - Ft Pickett

Technical Analysis - Ft Pickett
Date: October 17, 2005
Creator: United States. Defense Base Closure and Realignment Commission.
Object Type: Text
System: The UNT Digital Library
New insights into potential functions for the protein 4.1superfamily of proteins in kidney epithelium (open access)

New insights into potential functions for the protein 4.1superfamily of proteins in kidney epithelium

Members of the protein 4.1 family of adapter proteins are expressed in a broad panel of tissues including various epithelia where they likely play an important role in maintenance of cell architecture and polarity and in control of cell proliferation. We have recently characterized the structure and distribution of three members of the protein 4.1 family, 4.1B, 4.1R and 4.1N, in mouse kidney. We describe here binding partners for renal 4.1 proteins, identified through the screening of a rat kidney yeast two-hybrid system cDNA library. The identification of putative protein 4.1-based complexes enables us to envision potential functions for 4.1 proteins in kidney: organization of signaling complexes, response to osmotic stress, protein trafficking, and control of cell proliferation. We discuss the relevance of these protein 4.1-based interactions in kidney physio-pathology in the context of their previously identified functions in other cells and tissues. Specifically, we will focus on renal 4.1 protein interactions with beta amyloid precursor protein (beta-APP), 14-3-3 proteins, and the cell swelling-activated chloride channel pICln. We also discuss the functional relevance of another member of the protein 4.1 superfamily, ezrin, in kidney physiopathology.
Date: June 17, 2005
Creator: Calinisan, Venice; Gravem, Dana; Chen, Ray Ping-Hsu; Brittin,Sachi; Mohandas, Narla; Lecomte, Marie-Christine et al.
Object Type: Article
System: The UNT Digital Library