A purification method and N-glycosylation sites of a 36-cysteine-containing, putative cell/cell adhesion glycoprotein gp64 of the cellular slime mold, Polysphondylium pallidum
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1993.tb19881.x/fullpdf
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5. Contact sites in aggregating cells of Polysphondylium pallidum
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1. Element analysis of the Polysphondylium pallidum gp64 promoter;Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression;2002-04
2. Promoter analysis of the membrane protein gp64 gene of the cellular slime mold Polysphondylium pallidum;Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression;1999-10
3. Sequence pattern for the occurrence of N-glycosylation in proteins;Journal of Protein Chemistry;1999
4. Inhibitory effects of tunicamycin on cell-cell adhesion and cell reaggregation of the cellular slime mold,Polysphondylium pallidum;Journal of Plant Research;1996-06
5. Dimer Formation of a Cell-Cell Adhesion Protein, gp64 of the Cellular Slime Mold, Polysphondylium pallidum;Plant and Cell Physiology;1996-03-01
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