scholarly journals Lamellarin D Bioconjugates II: Synthesis and Cellular Internalization of Dendrimer and Nuclear Location Signal Derivatives

2009 ◽  
Vol 20 (6) ◽  
pp. 1112-1121 ◽  
Author(s):  
Daniel Pla ◽  
Marc Martí ◽  
Josep Farrera-Sinfreu ◽  
Daniel Pulido ◽  
Andrés Francesch ◽  
...  
1992 ◽  
Vol 198 (1) ◽  
pp. 107-114 ◽  
Author(s):  
Mitsuru Kido ◽  
Yoshihiro Yoneda ◽  
Mahito Nakanishi ◽  
Tsuyoshi Uchida ◽  
Yoshio Okada

1991 ◽  
Vol 17 (2) ◽  
pp. 229-234 ◽  
Author(s):  
Michael W. Lassner ◽  
Aubrey Jones ◽  
Steve Daubert ◽  
Luca Comai

Cell ◽  
1987 ◽  
Vol 50 (3) ◽  
pp. 465-475 ◽  
Author(s):  
Bruce L. Roberts ◽  
William D. Richardson ◽  
Alan E. Smith

Cell ◽  
1992 ◽  
Vol 68 (6) ◽  
pp. 1121-1133 ◽  
Author(s):  
Thomas Henkel ◽  
Ulrike Zabel ◽  
Karen van Zee ◽  
Judith M. Müller ◽  
Ellen Fanning ◽  
...  

1986 ◽  
Vol 6 (11) ◽  
pp. 4136-4139
Author(s):  
W H Colledge ◽  
W D Richardson ◽  
M D Edge ◽  
A E Smith

Site-directed mutagenesis was used to change Lys-128 of the simian virus 40 large-T nuclear location signal to Met, Ile, Arg, Gln, Asn, Leu, or His. Except for the large-T antigen of the Arg mutation, which was present in cytoplasmic and nuclear compartments, the resultant proteins were unable to enter the nucleus. By contrast, mutations at other sites within the signal were generally less severe in their effect. In some cases (Lys-128 to Gln, Asn, and His), the apparently cytoplasmic variants were able to support limited plasmid DNA replication, suggesting that low levels of large-T antigen undetectable by immunofluorescence were present in the nucleus. Such mutants did not support viral DNA replication. We conclude that there is a strong requirement for a basic residue at position 128 in the large-T nuclear location signal, with Lys the preferred residue.


1986 ◽  
Vol 6 (11) ◽  
pp. 4136-4139 ◽  
Author(s):  
W H Colledge ◽  
W D Richardson ◽  
M D Edge ◽  
A E Smith

Site-directed mutagenesis was used to change Lys-128 of the simian virus 40 large-T nuclear location signal to Met, Ile, Arg, Gln, Asn, Leu, or His. Except for the large-T antigen of the Arg mutation, which was present in cytoplasmic and nuclear compartments, the resultant proteins were unable to enter the nucleus. By contrast, mutations at other sites within the signal were generally less severe in their effect. In some cases (Lys-128 to Gln, Asn, and His), the apparently cytoplasmic variants were able to support limited plasmid DNA replication, suggesting that low levels of large-T antigen undetectable by immunofluorescence were present in the nucleus. Such mutants did not support viral DNA replication. We conclude that there is a strong requirement for a basic residue at position 128 in the large-T nuclear location signal, with Lys the preferred residue.


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