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R Longnecker

Showing results (41-50 of 64) with videos related to

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Journal of Virology|August 1, 1992
An Epstein-Barr virus transformation-associated membrane protein interacts with src family tyrosine kinasesA L Burkhardt, J B Bolen, E Kieff, et al.
Journal of Virology|February 9, 2000
Epstein-Barr virus entry utilizing HLA-DP or HLA-DQ as a coreceptorK M Haan, W W Kwok, R Longnecker, et al.
Journal of Virology|December 1, 1993
Epstein-Barr virus recombinants from overlapping cosmid fragmentsB Tomkinson, E Robertson, R Yalamanchili, et al.
Immunity|October 13, 1998
Epstein-Barr virus LMP2A drives B cell development and survival in the absence of normal B cell receptor signalsR G Caldwell, J B Wilson, S J Anderson, et al.
ACS Omega|December 20, 2021
Probing Liquid-Liquid Phase Separation in Secondary Organic Aerosol Mimicking Solutions Using Articulated StrawsEmmaline R Longnecker, Lucy Metz, Rebecca S Miller, et al.
Journal of Virology|September 12, 1998
Tyrosine 112 of latent membrane protein 2A is essential for protein tyrosine kinase loading and regulation of Epstein-Barr virus latencyS Fruehling, R Swart, K M Dolwick, et al.
Journal of Virology|April 1, 1993
The last seven transmembrane and carboxy-terminal cytoplasmic domains of Epstein-Barr virus latent membrane protein 2 (LMP2) are dispensable for lymphocyte infection and growth transformation in vitroR Longnecker, C L Miller, X Q Miao, et al.
Journal of Virology|August 1, 1993
Deletion of DNA encoding the first five transmembrane domains of Epstein-Barr virus latent membrane proteins 2A and 2BR Longnecker, C L Miller, B Tomkinson, et al.
Virology|January 1, 1988
Virulence of and establishment of latency by genetically engineered deletion mutants of herpes simplex virus 1B Meignier, R Longnecker, P Mavromara-Nazos, et al.
Journal of Virology|November 1, 1992
The only domain which distinguishes Epstein-Barr virus latent membrane protein 2A (LMP2A) from LMP2B is dispensable for lymphocyte infection and growth transformation in vitro; LMP2A is therefore nonessentialR Longnecker, C L Miller, X Q Miao, et al.
Pageof 7

Showing results (41-50 of 64) with videos related to

Sort By:
Pageof 7
Journal of Virology|August 1, 1992
An Epstein-Barr virus transformation-associated membrane protein interacts with src family tyrosine kinasesA L Burkhardt, J B Bolen, E Kieff, et al.
Journal of Virology|February 9, 2000
Epstein-Barr virus entry utilizing HLA-DP or HLA-DQ as a coreceptorK M Haan, W W Kwok, R Longnecker, et al.
Journal of Virology|December 1, 1993
Epstein-Barr virus recombinants from overlapping cosmid fragmentsB Tomkinson, E Robertson, R Yalamanchili, et al.
Immunity|October 13, 1998
Epstein-Barr virus LMP2A drives B cell development and survival in the absence of normal B cell receptor signalsR G Caldwell, J B Wilson, S J Anderson, et al.
ACS Omega|December 20, 2021
Probing Liquid-Liquid Phase Separation in Secondary Organic Aerosol Mimicking Solutions Using Articulated StrawsEmmaline R Longnecker, Lucy Metz, Rebecca S Miller, et al.
Journal of Virology|September 12, 1998
Tyrosine 112 of latent membrane protein 2A is essential for protein tyrosine kinase loading and regulation of Epstein-Barr virus latencyS Fruehling, R Swart, K M Dolwick, et al.
Journal of Virology|April 1, 1993
The last seven transmembrane and carboxy-terminal cytoplasmic domains of Epstein-Barr virus latent membrane protein 2 (LMP2) are dispensable for lymphocyte infection and growth transformation in vitroR Longnecker, C L Miller, X Q Miao, et al.
Journal of Virology|August 1, 1993
Deletion of DNA encoding the first five transmembrane domains of Epstein-Barr virus latent membrane proteins 2A and 2BR Longnecker, C L Miller, B Tomkinson, et al.
Virology|January 1, 1988
Virulence of and establishment of latency by genetically engineered deletion mutants of herpes simplex virus 1B Meignier, R Longnecker, P Mavromara-Nazos, et al.
Journal of Virology|November 1, 1992
The only domain which distinguishes Epstein-Barr virus latent membrane protein 2A (LMP2A) from LMP2B is dispensable for lymphocyte infection and growth transformation in vitro; LMP2A is therefore nonessentialR Longnecker, C L Miller, X Q Miao, et al.
Pageof 7