Activation of the grp78 andgrp94 Promoters by Hepatitis C Virus E2 Envelope Protein
暂无分享,去创建一个
M. Houghton | Y. Fong | Q. Choo | M. Selby | L. Cousens | T. B. Benedict Yen | Eva Liberman | T. Benedict Yen
[1] J. Dubuisson,et al. Involvement of Endoplasmic Reticulum Chaperones in the Folding of Hepatitis C Virus Glycoproteins , 1998, Journal of Virology.
[2] T. Yen,et al. Activation of hepatitis B virus S promoter by the viral large surface protein via induction of stress in the endoplasmic reticulum , 1997, Journal of virology.
[3] J. Ou. Molecular biology of hepatitis B virus e antigen , 1997, Journal of gastroenterology and hepatology.
[4] C. Rice,et al. Characterization of truncated forms of hepatitis C virus glycoproteins. , 1997, The Journal of general virology.
[5] C. Rice,et al. Formation of native hepatitis C virus glycoprotein complexes , 1997, Journal of virology.
[6] Amy S. Lee,et al. Inhibition of tumor progression by suppression of stress protein GRP78/BiP induction in fibrosarcoma B/C10ME. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[7] C. Rice,et al. Hepatitis C virus glycoprotein folding: disulfide bond formation and association with calnexin , 1996, Journal of virology.
[8] S. Tugizov,et al. Conformation-defective herpes simplex virus 1 glycoprotein B activates the promoter of the grp94 gene that codes for the 94-kD stress protein in the endoplasmic reticulum. , 1995, DNA and cell biology.
[9] C. Rice,et al. Formation and intracellular localization of hepatitis C virus envelope glycoprotein complexes expressed by recombinant vaccinia and Sindbis viruses , 1994, Journal of virology.
[10] S. Chatterjee,et al. Induction of M(r) 78,000 glucose-regulated stress protein in poly(adenosine diphosphate-ribose) polymerase- and nicotinamide adenine dinucleotide-deficient V79 cell lines and its relation to resistance to the topoisomerase II inhibitor etoposide. , 1994, Cancer research.
[11] C. Rice,et al. Processing in the hepatitis C virus E2-NS2 region: identification of p7 and two distinct E2-specific products with different C termini , 1994, Journal of virology.
[12] K. Burns,et al. Modulation of gene expression by calreticulin binding to the glucocorticoid receptor , 1994, Nature.
[13] M. Shago,et al. Inhibition of nuclear hormone receptor activity by calreticulin , 1994, Nature.
[14] K. Méflah,et al. Expression of the 100‐kDa glucose‐regulated protein (grp100/endoplasmin) is associated with tumorigenicity in a model of rat colon adenocarcinoma , 1994, International journal of cancer.
[15] A. Lee,et al. Suppression of stress protein GRP78 induction in tumor B/C10ME eliminates resistance to cell mediated cytotoxicity. , 1993, Cancer research.
[16] R. Lanford,et al. Analysis of hepatitis C virus capsid, E1, and E2/NS1 proteins expressed in insect cells. , 1993, Virology.
[17] M. Houghton,et al. Characterization of hepatitis C virus envelope glycoprotein complexes expressed by recombinant vaccinia viruses , 1993, Journal of virology.
[18] X. Cao,et al. Transactivation of the grp78 promoter by Ca2+ depletion. A comparative analysis with A23187 and the endoplasmic reticulum Ca(2+)-ATPase inhibitor thapsigargin. , 1993, The Journal of biological chemistry.
[19] Zhou Xj. The ultrastructural pathology of chronic hepatitis C , 1993 .
[20] M. Houghton,et al. Expression, identification and subcellular localization of the proteins encoded by the hepatitis C viral genome. , 1993, The Journal of general virology.
[21] N. Brot,et al. Dissociation of glucose-regulated protein Grp78 and Grp78-IgE Fc complexes by ATP. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[22] B. Price. Signalling across the endoplasmic reticulum membrane: potential mechanisms. , 1992, Cellular signalling.
[23] N. Haigwood,et al. Effect of intron A from human cytomegalovirus (Towne) immediate-early gene on heterologous expression in mammalian cells. , 1991, Nucleic acids research.
[24] M. Rose,et al. KAR2, a karyogamy gene, is the yeast homolog of the mammalian BiP/GRP78 gene , 1989, Cell.
[25] M. Houghton,et al. Isolation of a cDNA clone derived from a blood-borne non-A, non-B viral hepatitis genome. , 1989, Science.
[26] P. Luciw,et al. Human immunodeficiency virus long terminal repeat responds to T-cell activation signals. , 1987, Proceedings of the National Academy of Sciences of the United States of America.
[27] S. Munro,et al. An hsp70-like protein in the ER: Identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein , 1986, Cell.
[28] C. Rice,et al. The Hepatitis C Viruses , 2000, Current Topics in Microbiology and Immunology.
[29] C. Rice,et al. Molecular characterization of hepatitis C virus. , 1998, Current studies in hematology and blood transfusion.
[30] Amy S. Lee,et al. The glucose-regulated proteins (GRP78 and GRP94): functions, gene regulation, and applications. , 1994, Critical reviews in eukaryotic gene expression.
[31] X. Zhou. [The ultrastructural pathology of chronic hepatitis C]. , 1993, Zhonghua bing li xue za zhi = Chinese journal of pathology.
[32] R. Kriz,et al. The nucleotide sequence encoding the hamster 78-kDa glucose-regulated protein (GRP78) and its conservation between hamster and rat. , 1987, Gene.