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Agard, D. A (1993). To fold or not to fold. Science 260, 1903-1904.[Free Full Text]

Arias, A. E., Velez-Granell, C. S., Torres-Ruiz, J. A. and Bendayan, M (1994). Involvement of molecular chaperones in the aberrant aggregation of secretory proteins in pancreatic acinar cells. Exp. Cell Res 215, 1-8.[Medline]

Arias, A. E. and Bendayan, M (1993). Pancreatic acinar and islet cells in coculture: Selectivity of non-B endocrine cells. Eur. J. Cell Biol 61, 193-196.[Medline]

Bailyes, E. M., Shennan, K. I., Seal, A. J., Smeekens, S. P., Steiner, D. F. Hutton, J. C. and Docherry, K (1992). A member of the eukaryotic subtilisin family (PC3) has the enzymic properties of the type 1 proinsulin-converting endopeptidase. Biochem. J 285, 391-394.

Bassan, M., Zamostiano, R., Giladi, E., Davidson, A., Wollman, Y., Pitman, J., Hauser, J., Brenneman, D. E. and Gozes, I (1998). The identification of secreted heat shock 60-like protein from rat glial cells and a human neuroblastoma cell line. Neurosci. Lett 250, 37-40.[Medline]

Bendayan, M (1984). Concentration of amylase along its secretory pathway in the pancreatic acinar cell as revealed by high resolution immunocytochemistry. Histochem. J 16, 85-108.[Medline]

Bendayan, M (1989). Ultrastructural localization of insulin and C-peptide antigenic sites in rat pancreatic B cell obtained by applying the quantitative high-resolution protein A-gold approach. Am. J. Anat 185, 205-216.[Medline]

Bendayan, M (1995). Colloidal gold post-embedding immunocytochemistry. Prog. Histochem. Cytochem 29, 1-159.[Medline]

Bendayan, M., Malide, D., Ziv, E. et al (1995). Immunocytochemical investigation of insulin secretion by pancreatic-cells in control and diabetic Psammomys obsesus. J. Histochem. Cytochem 45, 771-784.

Benjannet, S., Reudelhubert, T., Mercure, C., Rondeau, N., Chretien, M. and Seidah, N. G (1992). Proprotein conversion is determined by a multiplicity of factors including convertase processing, substrate specificity and intracellular environment. J. Biol. Chem 267, 11417-11423.[Abstract/Free Full Text]

Bertsch,U., Soll, J., Seetharam, R. and Viitanen, P. V (1992). Identification, characterization, and DNA sequence of a functional \324double' groES-like chaperonin from chloroplasts of higher plants. Proc. Natl. Acad. Sci. USA 89, 8696-86700.[Abstract/Free Full Text]

Brown, H., Larsson, O., Branstrom, R. et al (1998). Cysteine string protein (CSP) is an insulin secretory granule-associated protein regulating beta-cell exocytosis. EMBO J 17, 5048-5058.[Medline]

Brudzynski, K., Martinez, V. and Gupta, R. S (1992). Secretory granule autoantigen in insulin-dependent diabetes mellitus is related to 62 kDa heat-shock protein (Hsp60). J. Autoimmun 5, 453-463.[Medline]

Brudzynski, K., Cunningham, I. A. and Martinez, V (1995). A family of Hsp60-related proteins in pancreatic beta cells of non-obese diabetic (NOD) mice. J. Autoimmun 8, 859-874.[Medline]

Chandrasekhar, G. N., Tilly, K., Woolford, C., Hendrix, R. and Georgopoulos, C (1986). Purification and properties of the groES morphogenetic protein of Escherichia coli. J. Biol. Chem 261, 12414-12419.[Abstract/Free Full Text]

Craig, E. A (1993). Chaperones: helpers along the pathways to protein folding. Science 260, 1902-1903.[Free Full Text]

Dannies, P. S (1999). Protein hormone storage in secretory granules: mechanisms for concentration and sorting. Endocr. Rev 20, 3-21.[Abstract/Free Full Text]

Ellis, R. J. and Van der Vies, S. M (1991). Molecular chaperones. Annu. Rev. Biochem 60, 321-347.[Medline]

Feder, M. E. and Hofmann, G. E (1999). Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology. Annu. Rev. Physiol 61, 243-282.[Medline]

Gatenby, A. A (1992). Protein folding and chaperonins. Plant Mol. Biol 19, 677-687.[Medline]

Gething, M. J. and Sambrook, J (1992). Protein folding in the cell. Nature 355, 33-45.[Medline]

Hartman, D. J., Dougman, D., Hoogenraad, N. J. and Hoj, P. B (1992). Heat shock proteins of barley mitochondria and chloroplasts identification of organellar Hsp 10 and 12: putative chaperonin 10 homologues. FEBS Lett 305, 147-150.[Medline]

Hemmingsen, S. M., Woolford, C., Van der Vies, S. M., Tilly, K., Dennis,D. T., Georgopoulos, C. P., Hendrix, R. W. and Ellis, R. J (1988). Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Nature 333, 330-334.[Medline]

Hendrick, J. P. and Ulrich-Hartl, F (1993). Molecular chaperone functions of heat-shock proteins. Annu. Rev. Biochem 62, 349-384.[Medline]

Khan, I. U., Wallin, R., Gupta, R. S. and Kammer, G. M (1998). Protein kinase A-catalyzed phosphorylation of heat shock protein 60 chaperone regulates its attachment to histone 2B in the T lymphocyte plasma membrane. Proc. Natl. Acad. Sci. USA 95, 10425-10430.[Abstract/Free Full Text]

Landry, S. J. and Gierasch, L. M (1994). Polypeptide interactions with molecular chaperones and their relationship to in vivo protein folding. Annu. Rev. Biophys. Biomol. Struct 23, 645-669.[Medline]

LeGall, I. M. and Bendayan, M (1996). Possible association of chaperonin 60 with secretory proteins in pancreatic acinar cells. J. Histochem. Cytochem 44, 743-749.[Abstract]

Lipkind, G. and Steiner, D. F (1999). Predicted structural alterations in proinsulin during its interactions with prohormone convertases. Biochemistry 38, 890-896.[Medline]

Lubben, T. H., Gatenby, A. A., Donaldson, G. K., Lorimer, G. H. and Viitanen, P. V (1990). Identification of a groES-like chaperonin in mitochondria that facilitates protein folding. Proc. Natl. Acad. Sci. USA 87, 7683-7687.[Abstract/Free Full Text]

Malide, D., Seidah, N. G., Chretien, M. and Bendayan, M (1995). Electron microscopic immunocytochemical evidence for the involvement of the convertases PC1 and PC2 in the processing of proinsulin in pancreatic beta-cells. J. Histochem. Cytochem 43, 11-19.[Abstract]

Martin, J., Mayhew, M., Langer, T. and Ulrich-Hartl, F (1993). The reaction cycle of GroEl and GroES in chaperonin-assisted protein folding. Nature 352, 228-233.

McMullin, T. W. and Hallberg, R. L (1988). A highly evolutionarily conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene. Mol. Cell Biol 8, 371-380.[Abstract/Free Full Text]

Orci, L., Ravazzola, M., Amherdt, M., Madsen, O., Perrelet, A., Vassalli, J. D. and Anderson, R. G. W (1986). Conversion of proinsulin to insulin occurs coordinately with acidification of maturing secretory vesicles. J. Cell. Biol 103, 2273-2281.[Abstract/Free Full Text]

Orci, L., Ravazzola, M., Storch, M. J., Anderson, R. G. W., Vassalli, J. D. and Perrelet, A (1987). Proteolytic maturation of insulin is a post-Golgi event, which occurs in acidifying clathrin-coated secretory vesicles. Cell 49, 865-868.[Medline]

Schmitz, A., Maintz, M., Kehle, T. and Herzog, V (1995). In vivo iodination of a misfolded proinsulin reveals co-localized signals for Bip binding and for degradation in the ER. EMBO J 14, 1091-1098.[Medline]

Seidah, N. G., Marcinkiewicz, M., Benjannet, S., Gaspar, L., Beaubien, G., Mattei, M. G., Lazure, C., Mbikay, M. and Chretien, M (1991). Cloning and primary sequence of a mouse candidate prohormone convertase PC1 homologous to PC2, Furin, and Kex2: distinct chromosomal localization and messenger RNA distribution in brain and pituitary compared to PC2. Mol. Endocrinol 5, 111-122.[Abstract]

Sigler, P. B., Xu, Z., Rye, H. S., Burston,S. G., Fenton, W. A. and Horwich, A. L (1998). Structure and function in GroEL-mediated protein folding. Annu. Rev. Biochem 67, 581-608.[Medline]

Soltys, B. J. and Gupta, R. S (1999). Mitochondrial-matrix proteins at unexpected locations: Are they exported?. Trends Biochem. Sci 24, 174-177.[Medline]

Steiner, D. F., Docherty, K., and Carroll, R (1984). Golgi/granule processing of peptide hormone and neuropeptide precursors: A mini-review. J. Cell. Biochem 24, 121-130.[Medline]

Torres-Ruiz, J. A. and McFadden, B. A (1992). Purification and Characterization of Chaperonin 10 from Chromatium vinosum. Arch. Biochem. Biophys 295, 172-179.[Medline]

Towbin, H. and Gordon, J (1984). Immunoblotting and dot immunobinding \320 current status and outlook. J. Immunol. Methods 72, 313-340.[Medline]

Velez-Granell, C. S., Arias, A. E., Torres-Ruiz, J. A. and Bendayan, M (1994). Molecular chaperones in pancreatic tissue: The presence of Cpn10, Cpn60 and Hsp70 in distinct compartments along the secretory pathway of the acinar cells. J. Cell Sci 107, 539-549.[Abstract]

Xanthoudakis, S., Roy, S., Rasper, D., Hennessey, T., Aubin, Y., Cassady, R., Tawa, P., Ruel, R., Rosen, A. and Nicholson, D. W (1999). Hsp60 accelerates the maturation of pro-caspase-3 by upstream activator proteases during apoptosis. EMBO J 18, 2049-2056.[Medline]

Xu, Z. H., Horowich A. L. and Sigler, P. B (1997). The crystal structure of the asymmetric GroEl-GroES (ADP)7 chaperonin complex. Nature 388, 741-750.[Medline]


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