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Volumn 120, Issue 2, 1996, Pages 161-168

Peptide biosynthetic processing: Distinguishing prohormone convertases PC1 and PC2

Author keywords

AtT 20; GH3; Neuropeptide Y; NPY; POMC; Proopiomelanocortin

Indexed keywords

HORMONE PRECURSOR; NEUROPEPTIDE Y; PROOPIOMELANOCORTIN; PROTEINASE;

EID: 0030199686     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/0303-7207(96)03834-8     Document Type: Article
Times cited : (33)

References (49)
  • 1
    • 0027265563 scopus 로고
    • The eukaryotic prohormone-processing endoproteases
    • [1] Bloomquist, B.T. and Mains, R.E. (1993) The eukaryotic prohormone-processing endoproteases. Cell Physiol. Biochem. 3, 197-212.
    • (1993) Cell Physiol. Biochem. , vol.3 , pp. 197-212
    • Bloomquist, B.T.1    Mains, R.E.2
  • 2
    • 0025937852 scopus 로고
    • The new eukaryotic precursor processing proteinases
    • [2] Lindberg, I. (1991) The new eukaryotic precursor processing proteinases. Mol. Endocrinol. 5, 1361-1365.
    • (1991) Mol. Endocrinol. , vol.5 , pp. 1361-1365
    • Lindberg, I.1
  • 3
    • 0025733702 scopus 로고
    • Mammalian subtilisins: The long-sought dibasic processing endoproteases
    • [3] Barr, P.J. (1991) Mammalian subtilisins: the long-sought dibasic processing endoproteases. Cell 66, 1-3.
    • (1991) Cell , vol.66 , pp. 1-3
    • Barr, P.J.1
  • 4
    • 0027078415 scopus 로고
    • The new enzymology of precursor processing enzymes
    • [4] Steiner, D.F., Smeekens, S.P., Ohagi, S. and Chan, S.J. (1992) The new enzymology of precursor processing enzymes. J. Biol. Chem. 267, 23435-23438.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23435-23438
    • Steiner, D.F.1    Smeekens, S.P.2    Ohagi, S.3    Chan, S.J.4
  • 5
    • 0027965348 scopus 로고
    • The family of subtilisin/kexin like proprotein and prohormone convertases: Divergent or shared functions
    • [5] Seidah, N.G., Chretien, M. and Day, R. (1994) The family of subtilisin/kexin like proprotein and prohormone convertases: divergent or shared functions. Biochimie 76, 197-209.
    • (1994) Biochimie , vol.76 , pp. 197-209
    • Seidah, N.G.1    Chretien, M.2    Day, R.3
  • 6
    • 0025762119 scopus 로고
    • PC1 and PC2 are proprotein convertases capable of cleaving proopiomelanocortin at distinct pairs of basic residues
    • [6] Benjannet, S., Rondeau, N., Day, R., Chretien, M. and Seidah, N.G. (1991) PC1 and PC2 are proprotein convertases capable of cleaving proopiomelanocortin at distinct pairs of basic residues. Proc. Natl. Acad. Sci. USA 88, 3564-3568.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3564-3568
    • Benjannet, S.1    Rondeau, N.2    Day, R.3    Chretien, M.4    Seidah, N.G.5
  • 7
    • 0025945724 scopus 로고
    • Kex2-like endoproteases PC2 and PC3 accurately cleave a model prohormone in mammalian cells: Evidence for a common core of neuroendocrine processing enzymes
    • [7] Thomas, L., Leduc, R., Thorne, B.A., Smeekens, S.P., Steiner, D.F. and Thomas, G. (1991) Kex2-like endoproteases PC2 and PC3 accurately cleave a model prohormone in mammalian cells: evidence for a common core of neuroendocrine processing enzymes. Proc. Natl. Acad. Sci. USA 88, 5297-5301.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5297-5301
    • Thomas, L.1    Leduc, R.2    Thorne, B.A.3    Smeekens, S.P.4    Steiner, D.F.5    Thomas, G.6
  • 8
    • 0027488373 scopus 로고
    • The prohormone convertases PC1 and PC2 mediate distinct endoproteolytic cleavages in a strict temporal order during POMC biosynthetic processing
    • [8] Zhou, A., Bloomquist, B.T. and Mains, R.E. (1993) The prohormone convertases PC1 and PC2 mediate distinct endoproteolytic cleavages in a strict temporal order during POMC biosynthetic processing. J. Biol. Chem. 268, 1763-1769.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1763-1769
    • Zhou, A.1    Bloomquist, B.T.2    Mains, R.E.3
  • 9
    • 0028276806 scopus 로고
    • Endoproteolytic processing of POMC and the peptide biosynthetic endoproteases PC1 and PC2 in neuroendocrine cells overexpressing PC1 or PC2
    • [9] Zhou, A. and Mains, R.E. (1994) Endoproteolytic processing of POMC and the peptide biosynthetic endoproteases PC1 and PC2 in neuroendocrine cells overexpressing PC1 or PC2. J. Biol. Chem. 269, 17440-17447.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17440-17447
    • Zhou, A.1    Mains, R.E.2
  • 10
    • 0028203583 scopus 로고
    • Differential effects of temperature blockade on the proteolytic processing of three secretory granule-associated proteins
    • [10] Milgram, S.L. and Mains, R.E. (1994) Differential effects of temperature blockade on the proteolytic processing of three secretory granule-associated proteins. J. Cell Sci. 107, 737-745.
    • (1994) J. Cell Sci. , vol.107 , pp. 737-745
    • Milgram, S.L.1    Mains, R.E.2
  • 11
    • 0028238009 scopus 로고
    • Evidence for cleavage of the PC1 PC3 prosegment in the endoplasmic reticulum
    • [11] Lindberg, I. (1994) Evidence for cleavage of the PC1 PC3 prosegment in the endoplasmic reticulum. Mol. Cell. Neurosci. 5, 263-268.
    • (1994) Mol. Cell. Neurosci. , vol.5 , pp. 263-268
    • Lindberg, I.1
  • 12
    • 0027268151 scopus 로고
    • Enzymic characterization of murine and human prohormone convertase-1 (mPC1 and hPC1) expressed in mammalian GH4C1 cells
    • [12] Jean, F., Basak, A., Rondeau, N., Benjannet, S., Hendy, G.N., Seidah, N.G., Chretien, M. and Lazure, C. (1993) Enzymic characterization of murine and human prohormone convertase-1 (mPC1 and hPC1) expressed in mammalian GH4C1 cells. Biochem. J. 292, 891-900.
    • (1993) Biochem. J. , vol.292 , pp. 891-900
    • Jean, F.1    Basak, A.2    Rondeau, N.3    Benjannet, S.4    Hendy, G.N.5    Seidah, N.G.6    Chretien, M.7    Lazure, C.8
  • 13
    • 0027460523 scopus 로고
    • Purification and characterization of the prohormone convertase PC1(PC3)
    • [13] Zhou, Y. and Lindberg, I. (1993) Purification and characterization of the prohormone convertase PC1(PC3). J. Biol. Chem. 268, 5615-5623.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5615-5623
    • Zhou, Y.1    Lindberg, I.2
  • 14
    • 0028337442 scopus 로고
    • Enzymatic properties of carboxyl-terminally truncated prohormone convertase 1 (PC1 SPC3) and evidence for autocatalytic conversion
    • [14] Zhou, Y. and Lindberg, I. (1994) Enzymatic properties of carboxyl-terminally truncated prohormone convertase 1 (PC1 SPC3) and evidence for autocatalytic conversion. J. Biol. Chem. 269, 18408-18413.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18408-18413
    • Zhou, Y.1    Lindberg, I.2
  • 15
    • 0028801027 scopus 로고
    • Ionic milieu controls the compartment-specific activation of POMC processing in AtT-20 cells
    • [15] Schmidt, W.K. and Moore, H.P.H. (1995) Ionic milieu controls the compartment-specific activation of POMC processing in AtT-20 cells. Mol. Biol. Cell 6, 1271-1285.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1271-1285
    • Schmidt, W.K.1    Moore, H.P.H.2
  • 16
    • 0024380456 scopus 로고
    • Proteolytic processing of pro-ACTH/endorphin begins in the Golgi complex of pituitary corticotropes and AtT-20 cells
    • [16] Schnabel, E., Mains, R.E. and Farquhar, M.G. (1989) Proteolytic processing of pro-ACTH/endorphin begins in the Golgi complex of pituitary corticotropes and AtT-20 cells. Mol. Endocrinol. 3, 1223-1235.
    • (1989) Mol. Endocrinol. , vol.3 , pp. 1223-1235
    • Schnabel, E.1    Mains, R.E.2    Farquhar, M.G.3
  • 17
    • 0028241106 scopus 로고
    • Distinct molecular mechanisms for protein sorting within immature secretory granules of pancreatic beta cells
    • [17] Kuliawat, R. and Arvan, P. (1994) Distinct molecular mechanisms for protein sorting within immature secretory granules of pancreatic beta cells. J. Cell Biol. 126, 77-86.
    • (1994) J. Cell Biol. , vol.126 , pp. 77-86
    • Kuliawat, R.1    Arvan, P.2
  • 18
    • 0026695156 scopus 로고
    • Protein targeting via the constitutive-like secretory pathway in isolated pancreatic islets
    • [18] Kuliawat, R. and Arvan, P. (1992) Protein targeting via the constitutive-like secretory pathway in isolated pancreatic islets. J. Cell Biol. 118, 521-529.
    • (1992) J. Cell Biol. , vol.118 , pp. 521-529
    • Kuliawat, R.1    Arvan, P.2
  • 19
    • 0026555196 scopus 로고
    • Molecular dissection of the secretory pathway
    • [19] Rothman, J.E. and Orci, L. (1992) Molecular dissection of the secretory pathway. Nature 355, 409-415.
    • (1992) Nature , vol.355 , pp. 409-415
    • Rothman, J.E.1    Orci, L.2
  • 20
    • 0027368472 scopus 로고
    • Comparative biosynthesis, covalenl post-translational modifications and efficiency of prosegment cleavage of PC1 and PC2; glycosylation, sulfation and identification of the intracellular site of prosegment cleavage of PC1 and PC2
    • [20] Benjannet, S., Rondeau, N., Paquet, L., Boudreault, A., Lazure, C., Chretien, M. and Seidah, N.G. (1993) Comparative biosynthesis, covalenl post-translational modifications and efficiency of prosegment cleavage of PC1 and PC2; glycosylation, sulfation and identification of the intracellular site of prosegment cleavage of PC1 and PC2. Biochem. J. 294, 735-743.
    • (1993) Biochem. J. , vol.294 , pp. 735-743
    • Benjannet, S.1    Rondeau, N.2    Paquet, L.3    Boudreault, A.4    Lazure, C.5    Chretien, M.6    Seidah, N.G.7
  • 21
    • 0023895049 scopus 로고
    • Intraorganellar calcium and pH control proinsulin cleavage in the pancreatic beta cell via two distinct site-specific endopeptidases
    • [21] Davidson, H.W., Rhodes, C.J. and Hutton, J.C. (1988) Intraorganellar calcium and pH control proinsulin cleavage in the pancreatic beta cell via two distinct site-specific endopeptidases. Nature 333, 93-96.
    • (1988) Nature , vol.333 , pp. 93-96
    • Davidson, H.W.1    Rhodes, C.J.2    Hutton, J.C.3
  • 23
    • 0025801016 scopus 로고
    • Characterization of PC2, a mammalian Kex2 homologue, following expression of the cDNA in microinjected Xenopus oocytes
    • [23] Shennan, K.I.J., Smeekens, S.P., Steiner, D.F. and Docherty, K. (1991) Characterization of PC2, a mammalian Kex2 homologue, following expression of the cDNA in microinjected Xenopus oocytes. FEBS Lett. 284, 277-280.
    • (1991) FEBS Lett. , vol.284 , pp. 277-280
    • Shennan, K.I.J.1    Smeekens, S.P.2    Steiner, D.F.3    Docherty, K.4
  • 24
    • 0027436437 scopus 로고
    • Biosynthesis of the prohormone convertase PC2 in CHO cells and in rat insulinoma cells
    • [24] Shen, F.S., Seidah, N.G. and Lindberg, I. (1993) Biosynthesis of the prohormone convertase PC2 in CHO cells and in rat insulinoma cells. J. Biol. Chem. 268, 24910-24915.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24910-24915
    • Shen, F.S.1    Seidah, N.G.2    Lindberg, I.3
  • 25
    • 0029075455 scopus 로고
    • 7B2 facilitates the maturation of proPC2 in neuroendocrine cells and is required for the expression of enzymatic activity
    • [25] Zhu, X. and Lindberg, I. (1995) 7B2 facilitates the maturation of proPC2 in neuroendocrine cells and is required for the expression of enzymatic activity. J. Cell Biol. 129, 1641-1650.
    • (1995) J. Cell Biol. , vol.129 , pp. 1641-1650
    • Zhu, X.1    Lindberg, I.2
  • 26
    • 0026475382 scopus 로고
    • Preferential cleavage of des-31,32-proinsulin over intact proinsulin by the insulin secretory granule type II endopeptidase
    • [26] Rhodes, C.J., Lincoln, B. and Shoelson, S.E. (1992) Preferential cleavage of des-31,32-proinsulin over intact proinsulin by the insulin secretory granule type II endopeptidase. J. Biol. Chem. 267, 22719-22727.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22719-22727
    • Rhodes, C.J.1    Lincoln, B.2    Shoelson, S.E.3
  • 27
    • 0023610730 scopus 로고
    • Proteolytic maturation of insulin is a post-Golgi event which occurs in acidifying clathrin-coated secretory vesicles
    • [27] 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.
    • (1987) Cell , vol.49 , pp. 865-868
    • Orci, L.1    Ravazzola, M.2    Storch, M.J.3    Anderson, R.G.W.4    Vassalli, J.D.5    Perrelet, A.6
  • 28
    • 0028074665 scopus 로고
    • Formation of the insulin-containing secretory granule core occurs within immature beta granules
    • [28] Huang, X.F. and Arvan, P. (1994) Formation of the insulin-containing secretory granule core occurs within immature beta granules. J. Biol. Chem. 269, 20838-20844.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20838-20844
    • Huang, X.F.1    Arvan, P.2
  • 29
    • 0027362080 scopus 로고
    • Post-translational processing of POMC in mouse pituitary melanotroph tumors induced by a POMC-SV40 large T antigen transgene
    • [29] Low, M.J., Liu, B., Hammer, G.D., Rubinstein, M. and Allen, R.G. (1993) Post-translational processing of POMC in mouse pituitary melanotroph tumors induced by a POMC-SV40 large T antigen transgene. J. Biol. Chem. 268, 24967-24975.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24967-24975
    • Low, M.J.1    Liu, B.2    Hammer, G.D.3    Rubinstein, M.4    Allen, R.G.5
  • 30
    • 0027486180 scopus 로고
    • Processing of two homologous precursors, proneuropeptide Y and propancreatic polypeptide, in transfected cell lines expressing different precursor convertases
    • [30] Wulff, B.S., Johansen, T.E., Dalboge, H., O'Hare, M.M. and Schwartz, T.W. (1993) Processing of two homologous precursors, proneuropeptide Y and propancreatic polypeptide, in transfected cell lines expressing different precursor convertases. J. Biol. Chem. 268, 13327-13335.
    • (1993) J. Biol. Chem. , vol.268 , pp. 13327-13335
    • Wulff, B.S.1    Johansen, T.E.2    Dalboge, H.3    O'Hare, M.M.4    Schwartz, T.W.5
  • 32
    • 0026398206 scopus 로고
    • Prohormone-converting enzymes: Regulation and evaluation of function using antisense RNA
    • [32] Bloomquist, B.T., Eipper, B.A. and Mains, R.E. (1991) Prohormone-converting enzymes: regulation and evaluation of function using antisense RNA. Mol. Endocrinol. 5, 2014-2024.
    • (1991) Mol. Endocrinol. , vol.5 , pp. 2014-2024
    • Bloomquist, B.T.1    Eipper, B.A.2    Mains, R.E.3
  • 33
    • 0028017325 scopus 로고
    • Prohormone processing in permeabilized cells: Endoproteolytic cleavage of prosomatostatin in the trans-Golgi network
    • [33] Xu, H. and Shields, D. (1994) Prohormone processing in permeabilized cells: endoproteolytic cleavage of prosomatostatin in the trans-Golgi network. Biochimie 76, 257-264.
    • (1994) Biochimie , vol.76 , pp. 257-264
    • Xu, H.1    Shields, D.2
  • 34
    • 0024278677 scopus 로고
    • The role of a low pH intracellular compartment in the processing, storage, and secretion of ACTH and endorphin
    • [34] Mains, R.E. and May, V. (1988) The role of a low pH intracellular compartment in the processing, storage, and secretion of ACTH and endorphin. J. Biol. Chem. 263, 7887-7894.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7887-7894
    • Mains, R.E.1    May, V.2
  • 35
    • 0028019850 scopus 로고
    • Prosomatostatin processing in pituitary GH3 cells: Identification and secretion of the intact propeptide
    • [35] Elgort, A. and Shields, D. (1994) Prosomatostatin processing in pituitary GH3 cells: identification and secretion of the intact propeptide. J. Biol. Chem. 269, 30668-30675.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30668-30675
    • Elgort, A.1    Shields, D.2
  • 36
    • 0024390850 scopus 로고
    • Biosynthesis, development, and regulation of neuropeptide Y in superior cervical ganglion culture
    • [36] Marek, K.L. and Mains, R.E. (1989) Biosynthesis, development, and regulation of neuropeptide Y in superior cervical ganglion culture. J. Neurochem. 52, 1807-1816.
    • (1989) J. Neurochem. , vol.52 , pp. 1807-1816
    • Marek, K.L.1    Mains, R.E.2
  • 37
    • 0025351483 scopus 로고
    • Cell-type specific post-translational processing of peptides by different pituitary cell lines
    • [37] Dickerson, I.M. and Mains, R.E. (1990) Cell-type specific post-translational processing of peptides by different pituitary cell lines. Endocrinology 127, 133-140.
    • (1990) Endocrinology , vol.127 , pp. 133-140
    • Dickerson, I.M.1    Mains, R.E.2
  • 38
    • 0025366334 scopus 로고
    • Biosynthesis and posttranslational processing of site-directed endoproteolytic cleavage mutants of pro-neuropeptide Y in mouse pituitary cells
    • [38] Dickerson, I.M., Dixon, J.E. and Mains, R.E. (1990) Biosynthesis and posttranslational processing of site-directed endoproteolytic cleavage mutants of pro-neuropeptide Y in mouse pituitary cells. J. Biol. Chem. 265, 2462-2469.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2462-2469
    • Dickerson, I.M.1    Dixon, J.E.2    Mains, R.E.3
  • 39
    • 0011996914 scopus 로고
    • Differential regulation of NPY and catecholamine production in SCG cultures
    • [39] Marek, K.L. and Mains, R.E. (1990) Differential regulation of NPY and catecholamine production in SCG cultures. Mol. Cell. Neurosci. 1, 262-269.
    • (1990) Mol. Cell. Neurosci. , vol.1 , pp. 262-269
    • Marek, K.L.1    Mains, R.E.2
  • 40
    • 0029160297 scopus 로고
    • Transport from late endosomes to lysosomes, but not sorting of integral membrane proteins in endosomes, depends on the vacuolar proton pump
    • [40] van Weert, A.W., Dunn, K.W., Geuze, H.J., Maxfield, F.R. and Stoorvogel, W. (1995) Transport from late endosomes to lysosomes, but not sorting of integral membrane proteins in endosomes, depends on the vacuolar proton pump. J. Cell Biol. 130, 821-834.
    • (1995) J. Cell Biol. , vol.130 , pp. 821-834
    • Van Weert, A.W.1    Dunn, K.W.2    Geuze, H.J.3    Maxfield, F.R.4    Stoorvogel, W.5
  • 41
    • 0029093967 scopus 로고
    • Function and structure of H-K-ATPase in the kidney
    • [41] Wingo, C.S. and Smolka, A.J. (1995) Function and structure of H-K-ATPase in the kidney. Am. J. Physiol. 269, F1-F16.
    • (1995) Am. J. Physiol. , vol.269
    • Wingo, C.S.1    Smolka, A.J.2
  • 42
    • 0028922667 scopus 로고
    • The vacuolar H + -ATPase inhibitor bafilomycin A1 differentially affects processing of mutant and wild-type beta-amyloid precursor protein
    • [42] Haass, C., Capell, A., Citron, M., Teplow, D.B. and Selkoe, D.J. (1995) The vacuolar H + -ATPase inhibitor bafilomycin A1 differentially affects processing of mutant and wild-type beta-amyloid precursor protein. J. Biol. Chem. 270, 6186-6192.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6186-6192
    • Haass, C.1    Capell, A.2    Citron, M.3    Teplow, D.B.4    Selkoe, D.J.5
  • 43
    • 0027528799 scopus 로고
    • COOH-terminal signals mediate the trafficking of a peptide processing enzyme in endocrine cells
    • [43] Milgram, S.L., Mains, R.E. and Eipper, B.A. (1993) COOH-terminal signals mediate the trafficking of a peptide processing enzyme in endocrine cells. J. Cell Biol. 121, 23-36.
    • (1993) J. Cell Biol. , vol.121 , pp. 23-36
    • Milgram, S.L.1    Mains, R.E.2    Eipper, B.A.3
  • 44
    • 0029147725 scopus 로고
    • Structural elements which direct specific processing of different mammalian subtilisin-like prohormone convertases
    • [44] Zhou, A., Paquet, L. and Mains, R.E. (1995) Structural elements which direct specific processing of different mammalian subtilisin-like prohormone convertases. J. Biol. Chem. 270, 21509-21516.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21509-21516
    • Zhou, A.1    Paquet, L.2    Mains, R.E.3
  • 45
    • 0023645729 scopus 로고
    • Transfected human neuropeptide Y cDNA expression in mouse pituitary cells. Inducible high expression, peptide characterization, and secretion
    • [45] Dickerson, I.M., Dixon, J.E. and Mains, R.E. (1987) Transfected human neuropeptide Y cDNA expression in mouse pituitary cells. Inducible high expression, peptide characterization, and secretion. J. Biol. Chem. 262, 13646-13653.
    • (1987) J. Biol. Chem. , vol.262 , pp. 13646-13653
    • Dickerson, I.M.1    Dixon, J.E.2    Mains, R.E.3
  • 46
    • 0022975133 scopus 로고
    • The trans-Golgi network: Sorting at the exit site of the Golgi complex
    • [46] Griffiths, G. and Simons, K. (1986) The trans-Golgi network: sorting at the exit site of the Golgi complex. Science 234, 438-443.
    • (1986) Science , vol.234 , pp. 438-443
    • Griffiths, G.1    Simons, K.2
  • 47
    • 0027989934 scopus 로고
    • The neuroendocrine precursor 7B2 is a sulfated protein proteolytically processed by a ubiquitous furin-like convertase
    • [47] Paquet, L., Bergeron, F., Boudreault, A., Seidah, N.G., Chretien, M., Mbikay, M. and Lazure, C. (1994) The neuroendocrine precursor 7B2 is a sulfated protein proteolytically processed by a ubiquitous furin-like convertase. J. Biol. Chem. 269, 19279-19285.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19279-19285
    • Paquet, L.1    Bergeron, F.2    Boudreault, A.3    Seidah, N.G.4    Chretien, M.5    Mbikay, M.6    Lazure, C.7
  • 48
    • 0026729952 scopus 로고
    • Protein sorting and secretion granule formation in regulated secretory cells
    • [48] Arvan, P. and Castle, J.D. (1992) Protein sorting and secretion granule formation in regulated secretory cells. Trends Cell. Biol. 2, 327-331.
    • (1992) Trends Cell. Biol. , vol.2 , pp. 327-331
    • Arvan, P.1    Castle, J.D.2
  • 49
    • 0029022254 scopus 로고
    • Enzymatic characterization of immunopurified prohormone convertase 2: Potent inhibition by a 7B2 peptide fragment
    • [49] Lindberg, I., van den Hurk, W.H., Bui, C. and Batic, C.J. (1995) Enzymatic characterization of immunopurified prohormone convertase 2: potent inhibition by a 7B2 peptide fragment. Biochemistry 34, 5486-5493.
    • (1995) Biochemistry , vol.34 , pp. 5486-5493
    • Lindberg, I.1    Van Den Hurk, W.H.2    Bui, C.3    Batic, C.J.4


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