AbstractChromatin and pore complex-lamina preparations were obtained from pig and chicken tissues, and their proteins were analysed by mono- and bidimensional electrophoresis. A glycosylated form of lamin A, recognized by concanavalin A, was shown to be present in at least 3 of the tissues examined. Glycosylation is suggested to be a further postsynthetic modification, besides phosphorylation and methylation, which can modify the properties of lamins
Laminin, a high molecular weight (1,000 kDa) glycoprotein located in basement membranes, appears to ...
Nuclear glycoproteins recognized by Concanavalin A have been isolated from pig, rabbit and chicken t...
lamina is a filamentous protein structure that is proximal to the inner nuclear membrane in multicel...
Chromatin and pore complex-lamina preparations were obtained from pig and chicken tissues, and their...
AbstractThe nuclear lamina formed by lamins is localized between the inner nuclear membrane and chro...
We have examined the nuclear localization of isoprenylated proteins in CHO-K1 cells labeled with [14...
We have examined the nuclear localization of isoprenylated proteins in CHO-K1 cells labeled with [14...
The lamins are a group of proteins in a residual nuclear envelope fraction derived from the nuclear ...
The lamins are components of the nuclear lamina, which forms a fibrous meshwork lining the inner nuc...
AbstractLamin B purified from murine EAT cells was characterized by partial protein sequences. Contr...
Lamin proteins are the major constituents of the nuclear lamina, a proteinaceous network that lines ...
Lamin proteins are the major constituents of the nuclear lamina, a proteinaceous network that lines ...
Lamin B purified from murine EAT cells was characterized by partial protein sequences. Contrary to t...
Chromatin glycoproteins recognized by Concanavalin A have been isolated from pig liver, kidney and h...
AbstractLamins are major structural components of the lamina providing mechanical support for the nu...
Laminin, a high molecular weight (1,000 kDa) glycoprotein located in basement membranes, appears to ...
Nuclear glycoproteins recognized by Concanavalin A have been isolated from pig, rabbit and chicken t...
lamina is a filamentous protein structure that is proximal to the inner nuclear membrane in multicel...
Chromatin and pore complex-lamina preparations were obtained from pig and chicken tissues, and their...
AbstractThe nuclear lamina formed by lamins is localized between the inner nuclear membrane and chro...
We have examined the nuclear localization of isoprenylated proteins in CHO-K1 cells labeled with [14...
We have examined the nuclear localization of isoprenylated proteins in CHO-K1 cells labeled with [14...
The lamins are a group of proteins in a residual nuclear envelope fraction derived from the nuclear ...
The lamins are components of the nuclear lamina, which forms a fibrous meshwork lining the inner nuc...
AbstractLamin B purified from murine EAT cells was characterized by partial protein sequences. Contr...
Lamin proteins are the major constituents of the nuclear lamina, a proteinaceous network that lines ...
Lamin proteins are the major constituents of the nuclear lamina, a proteinaceous network that lines ...
Lamin B purified from murine EAT cells was characterized by partial protein sequences. Contrary to t...
Chromatin glycoproteins recognized by Concanavalin A have been isolated from pig liver, kidney and h...
AbstractLamins are major structural components of the lamina providing mechanical support for the nu...
Laminin, a high molecular weight (1,000 kDa) glycoprotein located in basement membranes, appears to ...
Nuclear glycoproteins recognized by Concanavalin A have been isolated from pig, rabbit and chicken t...
lamina is a filamentous protein structure that is proximal to the inner nuclear membrane in multicel...