Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Filters

W W Hurlburt

Showing results (1-10 of 8) with videos related to

Pageof 1
Sort By:
The Journal of General Virology|April 1, 1997
A functional interaction of ICP8, the herpes simplex virus single-stranded DNA-binding protein, and the helicase-primase complex that is dependent on the presence of the UL8 subunitR K Hamatake, M Bifano, W W Hurlburt, et al.
The Journal of Biological Chemistry|February 18, 1994
The UL8 component of the herpes simplex virus helicase-primase complex stimulates primer synthesis by a subassembly of the UL5 and UL52 componentsD J Tenney, W W Hurlburt, P A Micheletti, et al.
The Journal of Biological Chemistry|April 21, 1995
Sequence-dependent primer synthesis by the herpes simplex virus helicase-primase complexD J Tenney, A K Sheaffer, W W Hurlburt, et al.
The Journal of General Virology|October 1, 1993
The herpes simplex virus type 1 DNA polymerase accessory protein, UL42, contains a functional protease-resistant domainR K Hamatake, M Bifano, D J Tenney, et al.
Journal of Virology|April 1, 1993
Deletions of the carboxy terminus of herpes simplex virus type 1 UL42 define a conserved amino-terminal functional domainD J Tenney, W W Hurlburt, M Bifano, et al.
Virus Research|October 1, 1995
Characterization of monoclonal antibodies recognizing amino- and carboxy-terminal epitopes of the herpes simplex virus UL42 proteinA K Sheaffer, W W Hurlburt, J T Stevens, et al.
Biochemistry|February 15, 2001
Biochemical characterization of osteo-testicular protein tyrosine phosphatase and its functional significance in rat primary osteoblastsM V Chengalvala, A R Bapat, W W Hurlburt, et al.
Journal of Virology|January 1, 1993
Mutations in the C terminus of herpes simplex virus type 1 DNA polymerase can affect binding and stimulation by its accessory protein UL42 without affecting basal polymerase activityD J Tenney, P A Micheletti, J T Stevens, et al.
Pageof 1

Showing results (1-10 of 8) with videos related to

Sort By:
Pageof 1
The Journal of General Virology|April 1, 1997
A functional interaction of ICP8, the herpes simplex virus single-stranded DNA-binding protein, and the helicase-primase complex that is dependent on the presence of the UL8 subunitR K Hamatake, M Bifano, W W Hurlburt, et al.
The Journal of Biological Chemistry|February 18, 1994
The UL8 component of the herpes simplex virus helicase-primase complex stimulates primer synthesis by a subassembly of the UL5 and UL52 componentsD J Tenney, W W Hurlburt, P A Micheletti, et al.
The Journal of Biological Chemistry|April 21, 1995
Sequence-dependent primer synthesis by the herpes simplex virus helicase-primase complexD J Tenney, A K Sheaffer, W W Hurlburt, et al.
The Journal of General Virology|October 1, 1993
The herpes simplex virus type 1 DNA polymerase accessory protein, UL42, contains a functional protease-resistant domainR K Hamatake, M Bifano, D J Tenney, et al.
Journal of Virology|April 1, 1993
Deletions of the carboxy terminus of herpes simplex virus type 1 UL42 define a conserved amino-terminal functional domainD J Tenney, W W Hurlburt, M Bifano, et al.
Virus Research|October 1, 1995
Characterization of monoclonal antibodies recognizing amino- and carboxy-terminal epitopes of the herpes simplex virus UL42 proteinA K Sheaffer, W W Hurlburt, J T Stevens, et al.
Biochemistry|February 15, 2001
Biochemical characterization of osteo-testicular protein tyrosine phosphatase and its functional significance in rat primary osteoblastsM V Chengalvala, A R Bapat, W W Hurlburt, et al.
Journal of Virology|January 1, 1993
Mutations in the C terminus of herpes simplex virus type 1 DNA polymerase can affect binding and stimulation by its accessory protein UL42 without affecting basal polymerase activityD J Tenney, P A Micheletti, J T Stevens, et al.
Pageof 1