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Journal Abstract Search

196 related items for PubMed ID: 11190669

  • 1. Lectins of the ER quality control machinery.
    Jakob CA, Chevet E, Thomas DY, Bergeron JJ.
    Results Probl Cell Differ; 2001; 33():1-17. PubMed ID: 11190669
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  • 3. Lectins as chaperones in glycoprotein folding.
    Trombetta ES, Helenius A.
    Curr Opin Struct Biol; 1998 Oct; 8(5):587-92. PubMed ID: 9818262
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  • 6. Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin.
    Vassilakos A, Michalak M, Lehrman MA, Williams DB.
    Biochemistry; 1998 Mar 10; 37(10):3480-90. PubMed ID: 9521669
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  • 8. Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins.
    Peterson JR, Ora A, Van PN, Helenius A.
    Mol Biol Cell; 1995 Sep 10; 6(9):1173-84. PubMed ID: 8534914
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  • 9. The Structure of calnexin, an ER chaperone involved in quality control of protein folding.
    Schrag JD, Bergeron JJ, Li Y, Borisova S, Hahn M, Thomas DY, Cygler M.
    Mol Cell; 2001 Sep 10; 8(3):633-44. PubMed ID: 11583625
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  • 10. Transient association of calnexin and calreticulin with newly synthesized G1 and G2 glycoproteins of uukuniemi virus (family Bunyaviridae).
    Veijola J, Pettersson RF.
    J Virol; 1999 Jul 10; 73(7):6123-7. PubMed ID: 10364370
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  • 11. Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum.
    Land A, Braakman I.
    Biochimie; 2001 Aug 10; 83(8):783-90. PubMed ID: 11530211
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  • 13. Calreticulin: one protein, one gene, many functions.
    Michalak M, Corbett EF, Mesaeli N, Nakamura K, Opas M.
    Biochem J; 1999 Dec 01; 344 Pt 2(Pt 2):281-92. PubMed ID: 10567207
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  • 14. Protein glucosylation and its role in protein folding.
    Parodi AJ.
    Annu Rev Biochem; 2000 Dec 01; 69():69-93. PubMed ID: 10966453
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  • 15. Rubella virus glycoprotein interaction with the endoplasmic reticulum calreticulin and calnexin.
    Nakhasi HL, Ramanujam M, Atreya CD, Hobman TC, Lee N, Esmaili A, Duncan RC.
    Arch Virol; 2001 Dec 01; 146(1):1-14. PubMed ID: 11266204
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  • 16. Chaperone selection during glycoprotein translocation into the endoplasmic reticulum.
    Molinari M, Helenius A.
    Science; 2000 Apr 14; 288(5464):331-3. PubMed ID: 10764645
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  • 17. Folding of insulin receptor monomers is facilitated by the molecular chaperones calnexin and calreticulin and impaired by rapid dimerization.
    Bass J, Chiu G, Argon Y, Steiner DF.
    J Cell Biol; 1998 May 04; 141(3):637-46. PubMed ID: 9566965
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  • 18. Involvement of endoplasmic reticulum chaperones in the folding of hepatitis C virus glycoproteins.
    Choukhi A, Ung S, Wychowski C, Dubuisson J.
    J Virol; 1998 May 04; 72(5):3851-8. PubMed ID: 9557669
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  • 20. Mutations in the carboxyl-terminal hydrophobic sequence of human cytomegalovirus glycoprotein B alter transport and protein chaperone binding.
    Zheng Z, Maidji E, Tugizov S, Pereira L.
    J Virol; 1996 Nov 04; 70(11):8029-40. PubMed ID: 8892927
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