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Items: 1 to 20 of 98

1.

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.

Wrobel CM, Geiger TR, Nix RN, Robitaille AM, Weigand S, Cervantes A, Gonzalez M, Martin JM.

Virus Res. 2013 Dec 26;178(2):314-27. doi: 10.1016/j.virusres.2013.09.025.

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Characterization of LMP-1's association with TRAF1, TRAF2, and TRAF3.

Sandberg M, Hammerschmidt W, Sugden B.

J Virol. 1997 Jun;71(6):4649-56.

6.

Matrix metalloproteinase 9 expression is induced by Epstein-Barr virus latent membrane protein 1 C-terminal activation regions 1 and 2.

Takeshita H, Yoshizaki T, Miller WE, Sato H, Furukawa M, Pagano JS, Raab-Traub N.

J Virol. 1999 Jul;73(7):5548-55.

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Repositioning antimicrobial agent pentamidine as a disruptor of the lateral interactions of transmembrane domain 5 of EBV latent membrane protein 1.

Wang X, Fiorini Z, Smith C, Zhang Y, Li J, Watkins LR, Yin H.

PLoS One. 2012;7(10):e47703. doi: 10.1371/journal.pone.0047703.

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Localization of the major NF-kappaB-activating site and the sole TRAF3 binding site of LMP-1 defines two distinct signaling motifs.

Brodeur SR, Cheng G, Baltimore D, Thorley-Lawson DA.

J Biol Chem. 1997 Aug 8;272(32):19777-84.

17.

EBV latent membrane protein-1 protects B cells from apoptosis by inhibition of BAX.

Grimm T, Schneider S, Naschberger E, Huber J, Guenzi E, Kieser A, Reitmeir P, Schulz TF, Morris CA, Stürzl M.

Blood. 2005 Apr 15;105(8):3263-9.

18.

Simultaneous detection of the two main proliferation driving EBV encoded proteins, EBNA-2 and LMP-1 in single B cells.

Rasul AE, Nagy N, Sohlberg E, Ádori M, Claesson HE, Klein G, Klein E.

J Immunol Methods. 2012 Nov 30;385(1-2):60-70. doi: 10.1016/j.jim.2012.08.008.

PMID:
22921685
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Transmembrane peptides used to investigate the homo-oligomeric interface and binding hotspot of latent membrane protein 1.

Sammond DW, Joce C, Takeshita R, McQuate SE, Ghosh N, Martin JM, Yin H.

Biopolymers. 2011 Nov;95(11):772-84. doi: 10.1002/bip.21672.

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