|
|
||||||||
Reviews |
1 Department of Medicinal Chemistry, Box 357610, University of Washington, Seattle, WA 98195-7610.
aAuthor for correspondence. E-mail daggett{at}u.washington.edu.
Background: Many clinical diagnostic tests depend on the accurate detection and quantification of proteins and peptides and their functions. Alterations of protein structure, and the resulting consequences on dynamics, can affect the outcome of laboratory tests. These changes can be a result of mutations, other in vivo factors, or even the experimental conditions of the diagnostic test.
Approach: The relationship between protein structure and dynamics and experimentally observable properties used in diagnostic assays are discussed in light of transmissible spongiform encephalopathies, or prion diseases.
Content: This review describes current efforts and possible future directions of prion diagnostic development. Recent advances in therapeutic development are also addressed.
Summary: The intent of the review is to highlight the role of protein dynamics and conformational change in protein-based diagnostics and treatments for prion disease.
The following articles in journals at HighWire Press have cited this article:
![]() |
J.-Y. Madec, S. Simon, S. Lezmi, A. Bencsik, J. Grassi, and T. Baron Abnormal prion protein in genetically resistant sheep from a scrapie-infected flock J. Gen. Virol., November 1, 2004; 85(11): 3483 - 3486. [Abstract] [Full Text] [PDF] |
||||
![]() |
A. Lane, C. J. Stanley, S. Dealler, and S. M. Wilson Polymeric Ligands with Specificity for Aggregated Prion Proteins Clin. Chem., October 1, 2003; 49(10): 1774 - 1775. [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |