Substitution of the myristoylation signal of human immunodeficiency virus type 1 Pr55Gag with the phospholipase C-δ1 pleckstrin homology domain results in …

E Urano, T Aoki, Y Futahashi… - Journal of general …, 2008 - microbiologyresearch.org
The matrix domain (MA) of human immunodeficiency virus type 1 Pr55Gag is covalently
modified with a myristoyl group that mediates efficient viral production. However, the role of …

[PDF][PDF] Substitution of the myristoylation signal of human immunodeficiency virus type 1 Pr55 Gag with the phospholipase C-d1 pleckstrin homology domain results in …

E Urano, T Aoki, Y Futahashi, T Murakami… - Journal of General …, 2008 - scienceopen.com
The matrix domain (MA) of human immunodeficiency virus type 1 Pr55Gag is covalently
modified with a myristoyl group that mediates efficient viral production. However, the role of …

[引用][C] Substitution of the myristoylation signal of human immunodeficiency virus type 1 Pr55Gag with the phospholipase C-δ1 pleckstrin homology domain results in …

E URANO, T AOKI, Y FUTAHASHI… - Journal of general …, 2008 - pascal-francis.inist.fr
Substitution of the myristoylation signal of human immunodeficiency virus type 1 Pr55Gag
with the phospholipase C-δ1 pleckstrin homology domain results in infectious pseudovirion …

Substitution of the myristoylation signal of human immunodeficiency virus type 1 Pr55Gag with the phospholipase C-δ1 pleckstrin homology domain results in …

E Urano, T Aoki, Y Futahashi, T Murakami… - Journal of General …, 2008 - cir.nii.ac.jp
抄録< jats: p> The matrix domain (MA) of human immunodeficiency virus type 1 Pr55< jats:
sup> Gag</jats: sup> is covalently modified with a myristoyl group that mediates efficient …

Substitution of the myristoylation signal of human immunodeficiency virus type 1 Pr55Gag with the phospholipase C-δ1 pleckstrin homology domain results in …

E Urano, T Aoki, Y Futahashi… - Journal of General …, 2008 - microbiologyresearch.org
The matrix domain (MA) of human immunodeficiency virus type 1 Pr55Gag is covalently
modified with a myristoyl group that mediates efficient viral production. However, the role of …

[HTML][HTML] Substitution of the myristoylation signal of human immunodeficiency virus type 1 Pr55Gag with the phospholipase C-δ1 pleckstrin homology domain results in …

E Urano, T Aoki, Y Futahashi, T Murakami… - The Journal of …, 2008 - ncbi.nlm.nih.gov
The matrix domain (MA) of human immunodeficiency virus type 1 Pr55 Gag is covalently
modified with a myristoyl group that mediates efficient viral production. However, the role of …

Substitution of the myristoylation signal of human immunodeficiency virus type 1 Pr55Gag with the phospholipase C-delta1 pleckstrin homology domain results in …

E Urano, T Aoki, Y Futahashi… - The Journal of …, 2008 - pubmed.ncbi.nlm.nih.gov
The matrix domain (MA) of human immunodeficiency virus type 1 Pr55Gag is covalently
modified with a myristoyl group that mediates efficient viral production. However, the role of …

[PDF][PDF] Substitution of the myristoylation signal of human immunodeficiency virus type 1 Pr55 Gag with the phospholipase C-d1 pleckstrin homology domain results in …

E Urano, T Aoki, Y Futahashi, T Murakami… - Journal of General …, 2008 - Citeseer
The matrix domain (MA) of human immunodeficiency virus type 1 Pr55Gag is covalently
modified with a myristoyl group that mediates efficient viral production. However, the role of …

Substitution of the myristoylation signal of human immunodeficiency virus type 1 Pr55Gag with the phospholipase C-delta1 pleckstrin homology domain results in …

E Urano, T Aoki, Y Futahashi, T Murakami… - The Journal of …, 2008 - europepmc.org
The matrix domain (MA) of human immunodeficiency virus type 1 Pr55 Gag is covalently
modified with a myristoyl group that mediates efficient viral production. However, the role of …

[引用][C] Substitution of the myristoylation signal of human immunodeficiency virus type 1 Pr55Gag with the phospholipase C-δ1 pleckstrin homology domain results in …

E URANO, T AOKI… - Journal of …, 2008 - Society for General Microbiology