High molecular weight complex analysis of Epstein–Barr virus Latent Membrane Protein 1 (LMP-1): Structural insights into LMP-1's homo-oligomerization and lipid raft association-Reference-Cited by-同舟云学术

High molecular weight complex analysis of Epstein–Barr virus Latent Membrane Protein 1 (LMP-1): Structural insights into LMP-1's homo-oligomerization and lipid raft association

Published:2013-12 Issue:2 Volume:178 Page:314-327
ISSN:0168-1702
Container-title:Virus Research
language:en
Short-container-title:Virus Research

Author:

Wrobel Christopher M.,Geiger Timothy R.,Nix Rebecca N.,Robitaille Aaron M.,Weigand Sandra,Cervantes Alfredo,Gonzalez Miguel,Martin Jennifer M.

Funder

NIH

NIH Training Grant

Publisher

Elsevier BV

Subject

Cancer Research,Infectious Diseases,Virology

Reference78 articles.

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3. Membrane-bound CD154, but not CD40-specific antibody, mediates NF-kappaB-independent IL-6 production in B cells;Baccam;Eur. J. Immunol.,1999

4. Posttranslational processing of an Epstein–Barr virus-encoded membrane protein expressed in cells transformed by Epstein–Barr virus;Baichwal;J. Virol.,1987

5. The multiple membrane-spanning segments of the BNLF-1 oncogene from Epstein–Barr virus are required for transformation;Baichwal;Oncogene,1989

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2. Oligomerization analysis as a tool to elucidate the mechanism of EBV latent membrane protein 1 inhibition by pentamidine;Biochimica et Biophysica Acta (BBA) - Biomembranes;2020-10

3. The Epstein–Barr virus LMP1 interactome: biological implications and therapeutic targets;Future Virology;2018-12