메뉴 건너뛰기




Volumn 27, Issue 2, 2003, Pages 331-337

Relationship between self-association of insulin and its secretion efficiency in yeast

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; DIMERIZATION; HYDROGEN-ION CONCENTRATION; INSULIN; MODELS, MOLECULAR; PROTEIN FOLDING; SACCHAROMYCES CEREVISIAE; TIME FACTORS;

EID: 0037296154     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1046-5928(02)00640-X     Document Type: Article
Times cited : (17)

References (31)
  • 1
    • 0030005908 scopus 로고    scopus 로고
    • A removable spacer peptide in an α-factor-leader/insulin precursor fusion protein improves processing and concomitant yield of the insulin precursor in Saccharomyces cerevisiae
    • T. Kjeldsen, J. Brandt, A.S. Andersen, M. Egel-Mitani, M. Hach, A.F. Pettersson, K. Vad, A removable spacer peptide in an α-factor-leader/insulin precursor fusion protein improves processing and concomitant yield of the insulin precursor in Saccharomyces cerevisiae, Gene 170 (1996) 107-112.
    • (1996) Gene , vol.170 , pp. 107-112
    • Kjeldsen, T.1    Brandt, J.2    Andersen, A.S.3    Egel-Mitani, M.4    Hach, M.5    Pettersson, A.F.6    Vad, K.7
  • 2
    • 0033807177 scopus 로고    scopus 로고
    • Yeast secretory expression of insulin precursors
    • T. Kjeldsen, Yeast secretory expression of insulin precursors, Appl. Microbiol. Biotechnol. 54 (2000) 277-286.
    • (2000) Appl. Microbiol. Biotechnol. , vol.54 , pp. 277-286
    • Kjeldsen, T.1
  • 5
    • 0032584722 scopus 로고    scopus 로고
    • Protein folding stability can determine the efficiency of escape from endoplasmic reticulum quality control
    • J.M. Kowalski, R.N. Parekh, J. Mao, K.D. Wittrup, Protein folding stability can determine the efficiency of escape from endoplasmic reticulum quality control, J. Biol. Chem. 273 (1998) 19453-19458.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19453-19458
    • Kowalski, J.M.1    Parekh, R.N.2    Mao, J.3    Wittrup, K.D.4
  • 6
    • 0032477891 scopus 로고    scopus 로고
    • Secretion efficiency in Saccharomyces cerevisiae of bovine pancreatic trypsin inhibitor mutants lacking disulfide bonds is correlated with thermodynamic stability
    • J.M. Kowalski, N. Rajesh, R.N. Parekh, K.D. Wittrup, Secretion efficiency in Saccharomyces cerevisiae of bovine pancreatic trypsin inhibitor mutants lacking disulfide bonds is correlated with thermodynamic stability, Biochemistry 37 (1998) 1264-1273.
    • (1998) Biochemistry , vol.37 , pp. 1264-1273
    • Kowalski, J.M.1    Rajesh, N.2    Parekh, R.N.3    Wittrup, K.D.4
  • 7
    • 0028241787 scopus 로고
    • High-resolution structure of an engineered biologically potent insulin monomer, B16 Tyr → His, as determined by nuclear magnetic resonance spectroscopy
    • S. Ludvigsen, M. Roy, H. Thogersen, N.C. Kaarsholm, High-resolution structure of an engineered biologically potent insulin monomer, B16 Tyr → His, as determined by nuclear magnetic resonance spectroscopy, Biochemistry 33 (1994) 7998-8006.
    • (1994) Biochemistry , vol.33 , pp. 7998-8006
    • Ludvigsen, S.1    Roy, M.2    Thogersen, H.3    Kaarsholm, N.C.4
  • 8
    • 0032054714 scopus 로고    scopus 로고
    • The role of assembly in insulin's biosynthesis
    • G. Dodson, D. Steiner, The role of assembly in insulin's biosynthesis, Curr. Opin. Struct. Biol. 8 (1998) 189-194.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 189-194
    • Dodson, G.1    Steiner, D.2
  • 11
    • 77956751025 scopus 로고
    • Insulin: The structure in the crystal and its reflection in chemistry and biology
    • T. Blundell, G. Dodson, D.C. Hodgkin, D.A. Mercola, Insulin: the structure in the crystal and its reflection in chemistry and biology, Adv. Protein Chem. 26 (1972) 279-402.
    • (1972) Adv. Protein Chem. , vol.26 , pp. 279-402
    • Blundell, T.1    Dodson, G.2    Hodgkin, D.C.3    Mercola, D.A.4
  • 13
    • 0024356816 scopus 로고
    • Comparison of solution structural flexibility and zinc binding domains for insulin, proinsulin, and miniproinsulin
    • N.C. Kaarsholm, H.C. Ko, M.F. Dunn, Comparison of solution structural flexibility and zinc binding domains for insulin, proinsulin, and miniproinsulin, Biochemistry 28 (1989) 4427-4435.
    • (1989) Biochemistry , vol.28 , pp. 4427-4435
    • Kaarsholm, N.C.1    Ko, H.C.2    Dunn, M.F.3
  • 14
    • 0344980439 scopus 로고    scopus 로고
    • The role of leaders in intracellular transport and secretion of the insulin precursor in the yeast Saccharomyces cerevisiae
    • T. Kjeldsen, A.F. Pettersson, M. Hach, The role of leaders in intracellular transport and secretion of the insulin precursor in the yeast Saccharomyces cerevisiae, J. Biotechnol. 75 (1999) 195-208.
    • (1999) J. Biotechnol. , vol.75 , pp. 195-208
    • Kjeldsen, T.1    Pettersson, A.F.2    Hach, M.3
  • 16
    • 0023794957 scopus 로고
    • Proinsulin heterogeneity in pigs
    • L. Snel, U. Damgaard, Proinsulin heterogeneity in pigs, Horm. Metab. Res. 20 (1988) 476-480.
    • (1988) Horm. Metab. Res. , vol.20 , pp. 476-480
    • Snel, L.1    Damgaard, U.2
  • 18
    • 0025078913 scopus 로고
    • Monomeric insulins and their experimental and clinical implications
    • J. Brange, D.R. Owens, S. Kang, A. Vølund, Monomeric insulins and their experimental and clinical implications, Diabetes Care 13 (1990) 923-954.
    • (1990) Diabetes Care , vol.13 , pp. 923-954
    • Brange, J.1    Owens, D.R.2    Kang, S.3    Vølund, A.4
  • 21
    • 0030015918 scopus 로고    scopus 로고
    • Solution structure of an engineered insulin monomer at neutral pH
    • H.B. Olsen, S. Ludvigsen, N.C. Kaarsholm, Solution structure of an engineered insulin monomer at neutral pH, Biochemistry 35 (1996) 8836-8845.
    • (1996) Biochemistry , vol.35 , pp. 8836-8845
    • Olsen, H.B.1    Ludvigsen, S.2    Kaarsholm, N.C.3
  • 22
    • 0024368808 scopus 로고
    • Partial diversion of a mutant proinsulin (B10 aspartic acid) from the regulated to the constitutive secretory pathway in transfected AtT-20 cells
    • D.J. Gross, P.A. Halban, C.R. Kahn, G.C. Weir, L. Villa-Komaroff, Partial diversion of a mutant proinsulin (B10 aspartic acid) from the regulated to the constitutive secretory pathway in transfected AtT-20 cells, Proc. Natl. Acad. Sci. USA 86 (1989) 4107-4111.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4107-4111
    • Gross, D.J.1    Halban, P.A.2    Kahn, C.R.3    Weir, G.C.4    Villa-Komaroff, L.5
  • 23
    • 0025786795 scopus 로고
    • Intracellular transport and sorting of mutant human proinsulins that fail to form hexamers
    • D. Quinn, L. Orci, M. Ravazzola, H.P. Moore, Intracellular transport and sorting of mutant human proinsulins that fail to form hexamers, J. Cell Biol. 113 (1991) 987-996.
    • (1991) J. Cell Biol. , vol.113 , pp. 987-996
    • Quinn, D.1    Orci, L.2    Ravazzola, M.3    Moore, H.P.4
  • 25
    • 0035844876 scopus 로고    scopus 로고
    • Intracellular retention of newly synthesized insulin in yeast is caused by endoproteolytic processing in the Golgi complex
    • B. Zhang, A. Chang, T.B. Kjeldsen, P. Arvan, Intracellular retention of newly synthesized insulin in yeast is caused by endoproteolytic processing in the Golgi complex, J. Cell Biol. 153 (2001) 1187-1198.
    • (2001) J. Cell Biol. , vol.153 , pp. 1187-1198
    • Zhang, B.1    Chang, A.2    Kjeldsen, T.B.3    Arvan, P.4
  • 26
    • 0035037739 scopus 로고    scopus 로고
    • Effects of cysteine to serine substitutions in the two inter-chain disulfide bonds of insulin
    • Z.-Y. Guo, Y.-M. Feng, Effects of cysteine to serine substitutions in the two inter-chain disulfide bonds of insulin, Biol. Chem. 382 (2001) 443-448.
    • (2001) Biol. Chem. , vol.382 , pp. 443-448
    • Guo, Z.-Y.1    Feng, Y.-M.2
  • 27
    • 0026908303 scopus 로고
    • Genetic and biochemical analysis of vesicular traffic in yeast
    • R. Schekman, Genetic and biochemical analysis of vesicular traffic in yeast, Curr. Opin. Cell Biol. 4 (1992) 587-592.
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 587-592
    • Schekman, R.1
  • 28
    • 0033521072 scopus 로고    scopus 로고
    • Setting the standards: Quality control in the secretory pathway
    • L. Ellgaard, M. Molinari, A. Helenius, Setting the standards: quality control in the secretory pathway, Science 286 (1999) 1882-1888.
    • (1999) Science , vol.286 , pp. 1882-1888
    • Ellgaard, L.1    Molinari, M.2    Helenius, A.3
  • 29
    • 0026555196 scopus 로고
    • Molecular dissection of the secretory pathway
    • J. Rothman, L. Orci, Molecular dissection of the secretory pathway, Nature 355 (1992) 409-415.
    • (1992) Nature , vol.355 , pp. 409-415
    • Rothman, J.1    Orci, L.2
  • 31
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • P.J. Kraulis, MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures, J. Appl. Crystallogr. 24 (1991) 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.