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Your Environment. Your Health.

Paula Scarborough Juras, Ph.D.

Chronic Disease Epidemiology Group

Paula Juras
Paula S. Juras, Ph.D.
Leader, Scientific Program Support Team
Tel 984-287-3728
Fax 301-480-3290
P.O. Box 12233
Mail Drop A3-05
Durham, N.C. 27709

Research Summary

Paula S. Juras, Ph.D., is the project officer for the Sister Study, a national effort to learn how the environment and genes affect breast cancer risk. It is a long-term study of 50,000 American women, from diverse backgrounds, whose sisters had breast cancer. Because of shared environment, genes and experiences, sisters of women with breast cancer have, on average, twice the risk of developing breast cancer themselves. By studying these sisters, researchers have a greater chance of identifying risk factors and discovering ways to prevent breast cancer.

Juras' dissertation research centered on an indicator of breast cancer prognosis, and her graduate research, as a whole, contributed directly to the development of protease inhibitor therapeutics for persons living with HIV. As a fellow at NIEHS, she studied lung disorders associated with some breast cancer treatments. She also serves as the project officer for the Division's DNA Isolation and Molecular Analysis contract.


  • The Sister Study
    ("/Rhythmyx/assembler/render?sys_contentid=36268&sys_revision=2&sys_variantid=639&sys_context=0&sys_authtype=0&sys_siteid=&sys_folderid=" sys_dependentvariantid="639" sys_dependentid="36268" inlinetype="rxhyperlink" rxinlineslot="103" sys_dependentid="36268" sys_siteid="" sys_folderid="")The Sister Study will prospectively examine environmental and familial risk factors for breast cancer and other diseases in a cohort of 50,000 sisters of women who have had breast cancer. The study should enhance researchers’ ability to understand the interplay of genes and environment in breast cancer risk and to identify potentially preventable risk factors.

Selected Publications

  1. Richards AD, Phylip LH, Farmerie WG, Scarborough PE, Alvarez A, Dunn BM, Hirel Ph-H, Konvalinka J, Strop P, Pavlickova L, Kostka, Kay J. Sensitive, soluble chromogenic substrates for HIV-1 Proteinase. J. Biol. Chem. 265, 7733-7736, 1990. [Abstract] [PDF]
  2. Scarborough PE, Guruprasad K, Topham C, Richo GR, Conner GE, Blundell TL, Dunn BM. Exploration of subsite binding specificity of human cathepsin D through kinetics and knowledge-based molecular modeling. Prot. Sci. 2, 264-276, 1993. [Abstract] [PDF]
  3. Sawyer TK, Fisher JF, Hester JB, Smith CW, Tomasselli AG, Tarpley WG, Burton PS, Hui JO, McQuade TJ, Conradi RA, Bradford VS, Lui L, Kinner JH, Tustin J, Alexander DL, Harrison AW, Emmert DE, Staples DJ, Maggiora LL, Zhang YZ, Poorman RA, Dunn BM, Rao C, Scarborough PE, Lowther WT, Craik C, DeCamp D, Moon J, Howe WJ, Heinrikson, RL. Peptidomimetic inhibitors of human immunodeficiency virus protease (HIV-PR): Design, enzyme binding and selectivity, antiviral efficacy, and cell permeability properties. Bioorganic & Medicainal Chemistry Letters 3, 819-824, 1993. [Abstract]
  4. Scarborough PE, Dunn BM. Redesign of the substrate specificity of human cathepsin D: The dominant role of position 287 in the S2 subsite. Protein Engineering 7, 495-502, 1994. [Abstract]
  5. Scarborough PE, Ma J, Qu W, Zeldin DC. P450 subfamily CYP2J and their role in the bioactivation of arachidonic acid in extrahepatic tissues. Drug Metabolism Reviews 31, 203-232, 1999. [Abstract]
  6. Zeldin DC, Wohlford-Lenane C, Chulada P, Bradbury JA, Scarborough PE, Roggli V, Langenbach R and Schwartz DA. (2001) Airway inflammation and responsiveness in prostaglandin H synthase-deficient mice exposed to bacterial lipopolysaccharide. Am J Respir Cell Mol Biol, 25, 457-65. [Abstract]
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