Pabst Patent Group LLP | David Shore
Our People
David  A. Shore

SERVICES

Patent

EDUCATION

D. Phil., Biochemistry
University of Oxford

B.Sc., Medical Microbiology
University College, London

ADMISSIONS

  • U.S. Patent and Trademark Office
David A. Shore, D. Phil.
Patent Agent
CONTACT INFORMATION
Tel: 404.879.2345
Fax: 404.879.2160
V-Card

David A. Shore, D. Phil., serves as a Patent Agent in the areas of biotechnology and pharmaceuticals.

Dr. Shore drafts patent applications, prosecutes U.S. patent applications (drafts responses, amendments, and appeal and reply briefs), and corresponds with foreign associates to guide the prosecution of foreign applications.

Dr. Shore has more than a decade of research experience in a diverse range of technological areas and is especially accomplished in the field of protein biochemistry.  Dr. Shore studied infectious diseases as an undergraduate and his Ph.D. research focused on characterization of glycoproteins at the surface of immune cells.  As a post-doctoral fellow at The Scripps Research Institute Dr. Shore determined the X-ray structures of proteins that govern activation of cellular immune responses.  Following completion of his post doctoral studies Dr. Shore served as a research fellow with the Influenza Division of the Centers for Disease Control and Prevention (CDC), where he assisted the development of novel influenza vaccines.

Dr. Shore is named as a co-inventor on multiple patent applications and has co-authored numerous journal articles, including "Structural characterization of a protective epitope spanning A(H1N1)pdm09 influenza virus neuraminidase monomers" (Nature Communications, 2015), "Structural stability of influenza A(H1N1)pdm09 virus hemagglutinins" (Journal of Virology, 2014), "Structural and antigenic variation among diverse clade 2 H5N1 viruses" (PLoS One, 2013), "T cell receptors are structures capable of initiating signaling in the absence of large conformational rearrangements”, (Journal of Biological Chemistry, 2012); “The crystal structure of CD8 in complex with YTS156.7.7 Fab and interaction with other CD8 antibodies define the binding mode of CD8 alpha-beta to MHC class I” (Journal of Molecular Biology, 2008), "Crystal structure of the TCR co-receptor CD8alphaalpha in complex with monoclonal antibody YTS 105.18 Fab fragment at 2.88 A resolution" (Journal of Molecular Biology, 2006), and “Glycosylation and the function of the T cell co-receptor CD8” , Advances in Experimental and Medicine and Biology (2005).