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Ingrid C. Deckman
Researcher at Bristol-Myers Squibb
Publications - 13
Citations - 738
Ingrid C. Deckman is an academic researcher from Bristol-Myers Squibb. The author has contributed to research in topics: Protease & Peptide sequence. The author has an hindex of 11, co-authored 13 publications receiving 722 citations. Previous affiliations of Ingrid C. Deckman include GlaxoSmithKline.
Papers
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Journal ArticleDOI
The protease of herpes simplex virus type 1 is essential for functional capsid formation and viral growth.
Min Gao,L. Matusick-Kumar,W. Hurlburt,S F DiTusa,W. W. Newcomb,Jay C. Brown,P.J. McCann rd,Ingrid C. Deckman,Richard J. Colonno +8 more
TL;DR: The herpes simplex virus type 1 protease and related proteins are involved in the assembly of viral capsids and the function of Na, at least in part, is to direct the catalytic domain N(o) to the nucleus.
Journal ArticleDOI
Autoproteolysis of herpes simplex virus type 1 protease releases an active catalytic domain found in intermediate capsid particles.
S P Weinheimer,P J McCann,Donald R. O'Boyle,J T Stevens,B A Boyd,D A Drier,Gregory Yamanaka,C.L. DiIanni,Ingrid C. Deckman,M G Cordingley +9 more
TL;DR: At least two protease autoprocessing products, in addition to fully processed I CP35cd (ICP35ef), were associated with intermediate B capsids in the nucleus of infected cells, suggesting a key role for proteolytic maturation of the protease and ICP35cd in HSV-1 capsid assembly.
Journal ArticleDOI
Identification of the herpes simplex virus-1 protease cleavage sites by direct sequence analysis of autoproteolytic cleavage products
C.L. DiIanni,D A Drier,Ingrid C. Deckman,P.J. McCann rd,Fenyong Liu,Bernard Roizman,Richard J. Colonno,M G Cordingley +7 more
TL;DR: Protein sequencing revealed that cleavage occurs between the Ala and Ser residues at amino acids 610/611 and 247/248 of the HSV-1 protease, which are highly conserved in homologous proteases of other herpes viruses.
Journal ArticleDOI
Use of protein unfolding studies to determine the conformational and dimeric stabilities of HIV-1 and SIV proteases.
Stephan K. Grant,Ingrid C. Deckman,Jeffrey S. Culp,Michael D. Minnich,Ian Brooks,Preston Hensley,Christine Debouck,Thomas D. Meek +7 more
TL;DR: HIV-1 PR was more stable to denaturation by chaotropes and extremes of pH and temperature than SIV PR, indicating that the former enzyme has greater conformational stability.
Book ChapterDOI
Physical studies of ribosomal protein-RNA interactions.
TL;DR: The simplicity of the sucrose gradient assays and the unambiguous interpretation of the results should make them a useful complement to filter binding assays for quantitative studies.