Primary sequence and heterologous expression of nuclear pore glycoprotein p62
暂无分享,去创建一个
[1] J. Hanover,et al. Glycosylation of nuclear pore protein p62. Reticulocyte lysate catalyzes O-linked N-acetylglucosamine addition in vitro. , 1990, The Journal of biological chemistry.
[2] D. Forbes,et al. Reconstitution of biochemically altered nuclear pores: Transport can be eliminated and restored , 1990, Cell.
[3] G. Hart,et al. Partial cDNA sequence encoding a nuclear pore protein modified by O-linked N-acetylglucosamine. , 1988, Proceedings of the National Academy of Sciences of the United States of America.
[4] R. Tjian,et al. O-glycosylation of eukaryotic transcription factors: Implications for mechanisms of transcriptional regulation , 1988, Cell.
[5] M. Willingham,et al. Nuclear protein import: specificity for transport across the nuclear pore. , 1988, Experimental cell research.
[6] L. Gerace,et al. A monoclonal antibody against the nuclear pore complex inhibits nucleocytoplasmic transport of protein and RNA in vivo , 1988, The Journal of cell biology.
[7] D. Newmeyer,et al. Nuclear import can be separated into distinct steps in vitro: Nuclear pore binding and translocation , 1988, Cell.
[8] G. Blobel,et al. Nuclear pore complex contains a family of glycoproteins that includes p62: glycosylation through a previously unidentified cellular pathway. , 1987, Proceedings of the National Academy of Sciences of the United States of America.
[9] M. Willingham,et al. A monoclonal antibody against a family of nuclear pore proteins (nucleoporins): O-linked N-acetylglucosamine is part of the immunodeterminant. , 1987, Proceedings of the National Academy of Sciences of the United States of America.
[10] M. Willingham,et al. O-linked N-acetylglucosamine is attached to proteins of the nuclear pore. Evidence for cytoplasmic and nucleoplasmic glycoproteins. , 1987, The Journal of biological chemistry.
[11] L. Gerace,et al. Monoclonal antibodies identify a group of nuclear pore complex glycoproteins , 1987, The Journal of cell biology.
[12] G. Hart,et al. Nuclear pore complex glycoproteins contain cytoplasmically disposed O- linked N-acetylglucosamine , 1987, The Journal of cell biology.
[13] D. Newmeyer,et al. Inhibition of in vitro nuclear transport by a lectin that binds to nuclear pores , 1987, The Journal of cell biology.
[14] J. Kleinschmidt,et al. Molecular characterization of a karyophilic, histone‐binding protein: cDNA cloning, amino acid sequence and expression of nuclear protein N1/N2 of Xenopus laevis. , 1986, The EMBO journal.
[15] G. Blobel,et al. Identification and characterization of a nuclear pore complex protein , 1986, Cell.
[16] M. Kozak. Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes , 1986, Cell.
[17] C DeLisi,et al. The detection and classification of membrane-spanning proteins. , 1985, Biochimica et biophysica acta.
[18] M. Monsigny,et al. Sugar-lectin interactions: how does wheat-germ agglutinin bind sialoglycoconjugates? , 1980, European journal of biochemistry.
[19] J. Garnier,et al. Analysis of the accuracy and implications of simple methods for predicting the secondary structure of globular proteins. , 1978, Journal of molecular biology.
[20] V. Potter,et al. Nuclei from Rat Liver: Isolation Method That Combines Purity with High Yield , 1966, Science.
[21] C Burks,et al. The GenBank genetic sequence data bank. , 1988, Nucleic acids research.
[22] P. Deininger. Full-length cDNA clones: vector-primed cDNA synthesis. , 1987, Methods in enzymology.
[23] U. Gubler. Second-strand cDNA synthesis: mRNA fragments as primers. , 1987, Methods in enzymology.
[24] E. Nadezhdina,et al. The centrosome and its role in the organization of microtubules. , 1987, International review of cytology.
[25] P. K. Hepler,et al. Membranes in the mitotic apparatus: their structure and function. , 1984, International review of cytology.
[26] A. van der Eb,et al. Assay of transforming activity of tumor virus DNA. , 1980, Methods in enzymology.