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Volumn 14, Issue 1, 2013, Pages 55-61

Protein homeostasis: Live long, won't prosper

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; CHOLESTEROL; COLLAGEN; CRYSTALLIN; ELASTIN; HISTONE; MESSENGER RNA; MYELIN; PHOSPHOLIPID; POLYPEPTIDE; PROTEOME;

EID: 84871502515     PISSN: 14710072     EISSN: 14710080     Source Type: Journal    
DOI: 10.1038/nrm3496     Document Type: Review
Times cited : (213)

References (88)
  • 3
    • 58249089343 scopus 로고    scopus 로고
    • Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells
    • D'Angelo, M. A., Raices, M., Panowski, S. H. & Hetzer, M. W. Age-dependent deterioration of nuclear pore complexes causes a loss of nuclear integrity in postmitotic cells. Cell 136, 284-295 (2009).
    • (2009) Cell , vol.136 , pp. 284-295
    • D'Angelo, M.A.1    Raices, M.2    Panowski, S.H.3    Hetzer, M.W.4
  • 4
    • 84857649763 scopus 로고    scopus 로고
    • Extremely long-lived nuclear pore proteins in the rat brain
    • Savas, J. N. et al. Extremely long-lived nuclear pore proteins in the rat brain. Science 335, 942 (2012).
    • (2012) Science , vol.335 , pp. 942
    • Savas, J.N.1
  • 6
    • 82755184981 scopus 로고    scopus 로고
    • Systems-wide proteomic analysis in mammalian cells reveals conserved, functional protein turnover
    • Cambridge, S. B. et al. Systems-wide proteomic analysis in mammalian cells reveals conserved, functional protein turnover. J. Proteome Res. 10, 5275-5284 (2011).
    • (2011) J. Proteome Res , vol.10 , pp. 5275-5284
    • Cambridge, S.B.1
  • 7
    • 55849136903 scopus 로고    scopus 로고
    • Global protein stability profiling in mammalian cells
    • Yen, H. C., Xu, Q., Chou, D. M., Zhao, Z. & Elledge, S. J. Global protein stability profiling in mammalian cells. Science 322, 918-923 (2008).
    • (2008) Science , vol.322 , pp. 918-923
    • Yen, H.C.1    Xu, Q.2    Chou, D.M.3    Zhao, Z.4    Elledge, S.J.5
  • 9
    • 0014027484 scopus 로고
    • Metabolism of histones of brain and liver
    • Piha, R. S., Cuenod, M. & Waelsch, H. Metabolism of histones of brain and liver. J. Biol. Chem. 241, 2397-2404 (1966).
    • (1966) J. Biol. Chem , vol.241 , pp. 2397-2404
    • Piha, R.S.1    Cuenod, M.2    Waelsch, H.3
  • 10
    • 0016167897 scopus 로고
    • Turnover of proteins in myelin and myelin-like material of mouse brain
    • Fischer, C. A. & Morell, P. Turnover of proteins in myelin and myelin-like material of mouse brain. Brain Res. 74, 51-65 (1974).
    • (1974) Brain Res , vol.74 , pp. 51-65
    • Fischer, C.A.1    Morell, P.2
  • 11
    • 0015214082 scopus 로고
    • Turnover of proteins in subcellular fractions of rat cerebral cortex
    • Rodriguez de Lores, A., Alberici de Canal, M. & De Robertis, E. Turnover of proteins in subcellular fractions of rat cerebral cortex. Brain Res. 31, 179-184 (1971).
    • (1971) Brain Res , vol.31 , pp. 179-184
    • Rodriguez De Lores, A.1    Alberici De Canal, M.2    De Robertis, E.3
  • 12
    • 0034671714 scopus 로고    scopus 로고
    • Effect of collagen turnover on the accumulation of advanced glycation end products
    • Verzijl, N. et al. Effect of collagen turnover on the accumulation of advanced glycation end products. J. Biol. Chem. 275, 39027-39031 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 39027-39031
    • Verzijl, N.1
  • 13
    • 0000353211 scopus 로고    scopus 로고
    • Aging of long-lived proteins: Extracellular matrix (collagens, elastins, proteoglycans) and lens crystallins
    • John Wiley & Sons
    • Sell, D. R. & Monnier, V. M. Aging of long-lived proteins: extracellular matrix (collagens, elastins, proteoglycans) and lens crystallins. in Comprehensive Physiology 235-305 (John Wiley & Sons, 2011).
    • (2011) Comprehensive Physiology , pp. 235-305
    • Sell, D.R.1    Monnier, V.M.2
  • 14
    • 0025780051 scopus 로고
    • Marked longevity of human lung parenchymal elastic fibers deduced from prevalence of D-aspartate and nuclear weapons-related radiocarbon
    • Shapiro, S. D., Endicott, S. K., Province, M. A., Pierce, J. A. & Campbell, E. J. Marked longevity of human lung parenchymal elastic fibers deduced from prevalence of D-aspartate and nuclear weapons-related radiocarbon. J. Clin. Invest. 87, 1828-1834 (1991).
    • (1991) J. Clin. Invest , vol.87 , pp. 1828-1834
    • Shapiro, S.D.1    Endicott, S.K.2    Province, M.A.3    Pierce, J.A.4    Campbell, E.J.5
  • 15
    • 0017375375 scopus 로고
    • Aspartic acid racemisation in the human lens during ageing and in cataract formation
    • Masters, P. M., Bada, J. L. & Zigler, J. S. Jr. Aspartic acid racemisation in the human lens during ageing and in cataract formation. Nature 268, 71-73 (1977).
    • (1977) Nature , vol.268 , pp. 71-73
    • Masters, P.M.1    Bada, J.L.2    Zigler Jr., J.S.3
  • 16
    • 0001359236 scopus 로고
    • Aspartic acid racemization in tooth enamel from living humans
    • Helfman, P. M. & Bada, J. L. Aspartic acid racemization in tooth enamel from living humans. Proc. Natl Acad. Sci. USA 72, 2891-2894 (1975).
    • (1975) Proc. Natl Acad. Sci. USA , vol.72 , pp. 2891-2894
    • Helfman, P.M.1    Bada, J.L.2
  • 17
    • 0017313486 scopus 로고
    • Aspartic acid racemisation in dentine as a measure of ageing
    • Helfman, P. M. & Bada, J. L. Aspartic acid racemisation in dentine as a measure of ageing. Nature 262, 279-281 (1976).
    • (1976) Nature , vol.262 , pp. 279-281
    • Helfman, P.M.1    Bada, J.L.2
  • 18
    • 78349291580 scopus 로고    scopus 로고
    • Rec8-containing cohesin maintains bivalents without turnover during the growing phase of mouse oocytes
    • Tachibana-Konwalski, K. et al. Rec8-containing cohesin maintains bivalents without turnover during the growing phase of mouse oocytes. Genes Dev. 24, 2505-2516 (2010).
    • (2010) Genes Dev , vol.24 , pp. 2505-2516
    • Tachibana-Konwalski, K.1
  • 19
    • 34249335982 scopus 로고    scopus 로고
    • 15N metabolic labeling of mammalian tissue with slow protein turnover
    • McClatchy, D. B., Dong, M. Q., Wu, C. C., Venable, J. D. & Yates, J. R. 15N metabolic labeling of mammalian tissue with slow protein turnover. J. Proteome Res. 6, 2005-2010 (2007).
    • (2007) J. Proteome Res , vol.6 , pp. 2005-2010
    • McClatchy, D.B.1    Dong, M.Q.2    Wu, C.C.3    Venable, J.D.4    Yates, J.R.5
  • 20
    • 0017389118 scopus 로고
    • The vertebrate eye lens
    • Bloemendal, H. The vertebrate eye lens. Science 197, 127-138 (1977).
    • (1977) Science , vol.197 , pp. 127-138
    • Bloemendal, H.1
  • 21
    • 61849122908 scopus 로고    scopus 로고
    • Genetics of crystallins: Cataract and beyond
    • Graw, J. Genetics of crystallins: cataract and beyond. Exp. Eye Res. 88, 173-189 (2009).
    • (2009) Exp. Eye Res , vol.88 , pp. 173-189
    • Graw, J.1
  • 22
    • 79960625179 scopus 로고    scopus 로고
    • Lens fibre cell differentiation and organelle loss: Many paths lead to clarity
    • Wride, M. A. Lens fibre cell differentiation and organelle loss: many paths lead to clarity. Phil. Trans. R. Soc. B 366, 1219-1233 (2011).
    • (2011) Phil. Trans. R. Soc. B , vol.366 , pp. 1219-1233
    • Wride, M.A.1
  • 23
    • 0036343618 scopus 로고    scopus 로고
    • Lens organelle degradation
    • Bassnett, S. Lens organelle degradation. Exp. Eye Res. 74, 1-6 (2002).
    • (2002) Exp. Eye Res , vol.74 , pp. 1-6
    • Bassnett, S.1
  • 24
    • 79960629881 scopus 로고    scopus 로고
    • Biological glass: Structural determinants of eye lens transparency
    • Bassnett, S., Shi, Y. & Vrensen, G. F. Biological glass: structural determinants of eye lens transparency. Phil. Trans. R. Soc. B 366, 1250-1264 (2011).
    • (2011) Phil. Trans. R. Soc. B , vol.366 , pp. 1250-1264
    • Bassnett, S.1    Shi, Y.2    Vrensen, G.F.3
  • 25
    • 0026483279 scopus 로고
    • α-crystallin can function as a molecular chaperone
    • Horwitz, J. α-crystallin can function as a molecular chaperone. Proc. Natl Acad. Sci. USA 89, 10449-10453 (1992).
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 10449-10453
    • Horwitz, J.1
  • 26
    • 0028973109 scopus 로고
    • Evidence that α-crystallin prevents non-specific protein aggregation in the intact eye lens
    • Rao, P. V., Huang, Q. L., Horwitz, J. & Zigler, J. S. Jr. Evidence that α-crystallin prevents non-specific protein aggregation in the intact eye lens. Biochim. Biophys. Acta 1245, 439-447 (1995).
    • (1995) Biochim. Biophys. Acta , vol.1245 , pp. 439-447
    • Rao, P.V.1    Huang, Q.L.2    Horwitz, J.3    Zigler Jr., J.S.4
  • 27
    • 41949133095 scopus 로고    scopus 로고
    • Mechanism of small heat shock protein function in vivo: A knock-in mouse model demonstrates that the R49C mutation in αa-crystallin enhances protein insolubility and cell death
    • Xi, J. H. et al. Mechanism of small heat shock protein function in vivo: a knock-in mouse model demonstrates that the R49C mutation in αA-crystallin enhances protein insolubility and cell death. J. Biol. Chem. 283, 5801-5814 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 5801-5814
    • Xi, J.H.1
  • 28
    • 0034012636 scopus 로고    scopus 로고
    • Glutathione: A vital lens antioxidant
    • Giblin, F. J. Glutathione: a vital lens antioxidant. J. Ocul. Pharmacol. Ther. 16, 121-135 (2000).
    • (2000) J. Ocul. Pharmacol. Ther , vol.16 , pp. 121-135
    • Giblin, F.J.1
  • 29
    • 0042198801 scopus 로고    scopus 로고
    • Redox regulation in the lens
    • Lou, M. F. Redox regulation in the lens. Prog. Retin. Eye Res. 22, 657-682 (2003).
    • (2003) Prog. Retin. Eye Res , vol.22 , pp. 657-682
    • Lou, M.F.1
  • 30
    • 79955958811 scopus 로고    scopus 로고
    • Effect of age on the thioltransferase (glutaredoxin) and thioredoxin systems in the human lens
    • Xing, K. Y. & Lou, M. F. Effect of age on the thioltransferase (glutaredoxin) and thioredoxin systems in the human lens. Invest. Ophthalmol. Vis. Sci. 51, 6598-6604 (2010).
    • (2010) Invest. Ophthalmol. Vis. Sci , vol.51 , pp. 6598-6604
    • Xing, K.Y.1    Lou, M.F.2
  • 31
    • 0028811434 scopus 로고
    • Effect of cross-linking on the chaperone-like function of α-crystallin
    • Sharma, K. K. & Ortwerth, B. J. Effect of cross-linking on the chaperone-like function of α-crystallin. Exp. Eye Res. 61, 413-421 (1995).
    • (1995) Exp. Eye Res , vol.61 , pp. 413-421
    • Sharma, K.K.1    Ortwerth, B.J.2
  • 32
    • 7244227985 scopus 로고    scopus 로고
    • Deamidation affects structural and functional properties of human αa-crystallin and its oligomerization with αb-crystallin
    • Gupta, R. & Srivastava, O. P. Deamidation affects structural and functional properties of human αA-crystallin and its oligomerization with αB-crystallin. J. Biol. Chem. 279, 44258-44269 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 44258-44269
    • Gupta, R.1    Srivastava, O.P.2
  • 33
    • 0014787125 scopus 로고
    • Free and protein-bound glutathione in normal and cataractous human lenses
    • Harding, J. J. Free and protein-bound glutathione in normal and cataractous human lenses. Biochem. J. 117, 957-960 (1970).
    • (1970) Biochem. J , vol.117 , pp. 957-960
    • Harding, J.J.1
  • 35
    • 0033829222 scopus 로고    scopus 로고
    • The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage
    • Hanson, S. R., Hasan, A., Smith, D. L. & Smith, J. B. The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation and backbone cleavage. Exp. Eye Res. 71, 195-207 (2000).
    • (2000) Exp. Eye Res , vol.71 , pp. 195-207
    • Hanson, S.R.1    Hasan, A.2    Smith, D.L.3    Smith, J.B.4
  • 36
    • 0027081126 scopus 로고
    • Studies on the solubilization of the water-insoluble fraction from human lens and cataract
    • Ortwerth, B. J. & Olesen, P. R. Studies on the solubilization of the water-insoluble fraction from human lens and cataract. Exp. Eye Res. 55, 777-783 (1992).
    • (1992) Exp. Eye Res , vol.55 , pp. 777-783
    • Ortwerth, B.J.1    Olesen, P.R.2
  • 37
    • 0345282976 scopus 로고    scopus 로고
    • Methylglyoxal-derived hydroimidazolone advanced glycation end-products of human lens proteins
    • Ahmed, N. et al. Methylglyoxal-derived hydroimidazolone advanced glycation end-products of human lens proteins. Invest. Ophthalmol. Vis. Sci. 44, 5287-5292 (2003).
    • (2003) Invest. Ophthalmol. Vis. Sci , vol.44 , pp. 5287-5292
    • Ahmed, N.1
  • 38
    • 0031909588 scopus 로고    scopus 로고
    • Quantitation of asparagine-101 deamidation from αa crystallin during aging of the human lens
    • Takemoto, L. J. Quantitation of asparagine-101 deamidation from αA crystallin during aging of the human lens. Curr. Eye Res. 17, 247-250 (1998).
    • (1998) Curr. Eye Res , vol.17 , pp. 247-250
    • Takemoto, L.J.1
  • 39
    • 33750142707 scopus 로고    scopus 로고
    • Age-related changes in human crystallins determined from comparative analysis of post-translational modifications in young and aged lens: Does deamidation contribute to crystallin insolubility?
    • Wilmarth, P. A. et al. Age-related changes in human crystallins determined from comparative analysis of post-translational modifications in young and aged lens: does deamidation contribute to crystallin insolubility? J. Proteome Res. 5, 2554-2566 (2006).
    • (2006) J. Proteome Res , vol.5 , pp. 2554-2566
    • Wilmarth, P.A.1
  • 40
    • 4143088433 scopus 로고    scopus 로고
    • Ageing and vision: Structure, stability and function of lens crystallins
    • Bloemendal, H. et al. Ageing and vision: structure, stability and function of lens crystallins. Prog. Biophys. Mol. Biol. 86, 407-485 (2004).
    • (2004) Prog. Biophys. Mol. Biol , vol.86 , pp. 407-485
    • Bloemendal, H.1
  • 41
    • 0013358797 scopus 로고
    • Absence of low-molecular-weight α-crystallin in nuclear region of old human lenses
    • Roy, D. & Spector, A. Absence of low-molecular-weight α-crystallin in nuclear region of old human lenses. Proc. Natl Acad. Sci. USA 73, 3484-3487 (1976).
    • (1976) Proc. Natl Acad. Sci. USA , vol.73 , pp. 3484-3487
    • Roy, D.1    Spector, A.2
  • 43
    • 0020049070 scopus 로고
    • Studies in cutaneous aging: I. The elastic fiber network
    • Braverman, I. M. & Fonferko, E. Studies in cutaneous aging: I. The elastic fiber network. J. Invest. Dermatol. 78, 434-443 (1982).
    • (1982) J. Invest. Dermatol , vol.78 , pp. 434-443
    • Braverman, I.M.1    Fonferko, E.2
  • 44
    • 82455201152 scopus 로고    scopus 로고
    • Structural biochemical, cellular, and functional changes in skeletal muscle extracellular matrix with aging
    • Kragstrup, T. W., Kjaer, M. & Mackey, A. L. Structural, biochemical, cellular, and functional changes in skeletal muscle extracellular matrix with aging. Scand. J. Med. Sci. Sports 21, 749-757 (2011).
    • (2011) Scand. J. Med. Sci. Sports , vol.21 , pp. 749-757
    • Kragstrup, T.W.1    Kjaer, M.2    MacKey, A.L.3
  • 45
    • 84860348119 scopus 로고    scopus 로고
    • Molecular basis of arterial stiffening: Role of glycation-a mini-review
    • Sell, D. R. & Monnier, V. M. Molecular basis of arterial stiffening: role of glycation-a mini-review. Gerontology 58, 227-237 (2012).
    • (2012) Gerontology , vol.58 , pp. 227-237
    • Sell, D.R.1    Monnier, V.M.2
  • 46
    • 67650032512 scopus 로고    scopus 로고
    • Effect of aging on elastin functionality in human cerebral arteries
    • Fonck, E. et al. Effect of aging on elastin functionality in human cerebral arteries. Stroke 40, 2552-2556 (2009).
    • (2009) Stroke , vol.40 , pp. 2552-2556
    • Fonck, E.1
  • 47
    • 0031687318 scopus 로고    scopus 로고
    • Effect of exercise training on passive stiffness in locomotor skeletal muscle: Role of extracellular matrix
    • Gosselin, L. E., Adams, C., Cotter, T. A., McCormick, R. J. & Thomas, D. P. Effect of exercise training on passive stiffness in locomotor skeletal muscle: role of extracellular matrix. J. Appl. Physiol. 85, 1011-1016 (1998).
    • (1998) J. Appl. Physiol , vol.85 , pp. 1011-1016
    • Gosselin, L.E.1    Adams, C.2    Cotter, T.A.3    McCormick, R.J.4    Thomas, D.P.5
  • 48
    • 36849055964 scopus 로고    scopus 로고
    • Collagen cross-linking, and advanced glycation end products in aging human skeletal muscle
    • Haus, J. M., Carrithers, J. A., Trappe, S. W. & Trappe, T. A. Collagen, cross-linking, and advanced glycation end products in aging human skeletal muscle. J. Appl. Physiol. 103, 2068-2076 (2007).
    • (2007) J. Appl. Physiol , vol.103 , pp. 2068-2076
    • Haus, J.M.1    Carrithers, J.A.2    Trappe, S.W.3    Trappe, T.A.4
  • 49
    • 79959423595 scopus 로고    scopus 로고
    • The structure of the nuclear pore complex
    • Hoelz, A., Debler, E. W. & Blobel, G. The structure of the nuclear pore complex. Annu. Rev. Biochem. 80, 613-643 (2011).
    • (2011) Annu. Rev. Biochem , vol.80 , pp. 613-643
    • Hoelz, A.1    Debler, E.W.2    Blobel, G.3
  • 51
    • 71549126814 scopus 로고    scopus 로고
    • Border control at the nucleus: Biogenesis and organization of the nuclear membrane and pore complexes
    • Hetzer, M. W. & Wente, S. R. Border control at the nucleus: biogenesis and organization of the nuclear membrane and pore complexes. Dev. Cell 17, 606-616 (2009).
    • (2009) Dev. Cell , vol.17 , pp. 606-616
    • Hetzer, M.W.1    Wente, S.R.2
  • 53
    • 0035869022 scopus 로고    scopus 로고
    • Kinetic analysis of translocation through nuclear pore complexes
    • Ribbeck, K. & Gorlich, D. Kinetic analysis of translocation through nuclear pore complexes. EMBO J. 20, 1320-1330 (2001).
    • (2001) EMBO J , vol.20 , pp. 1320-1330
    • Ribbeck, K.1    Gorlich, D.2
  • 54
    • 0024804516 scopus 로고
    • Distribution of nuclear pores and chromatin organization in neurons and glial cells of the rat cerebellar cortex
    • Garcia-Segura, L. M., Lafarga, M., Berciano, M. T., Hernandez, P. & Andres, M. A. Distribution of nuclear pores and chromatin organization in neurons and glial cells of the rat cerebellar cortex. J. Comp. Neurol. 290, 440-450 (1989).
    • (1989) J. Comp. Neurol , vol.290 , pp. 440-450
    • Garcia-Segura, L.M.1    Lafarga, M.2    Berciano, M.T.3    Hernandez, P.4    Andres, M.A.5
  • 55
    • 33646804467 scopus 로고    scopus 로고
    • NDC1: A crucial membrane-integral nucleoporin of metazoan nuclear pore complexes
    • Stavru, F. et al. NDC1: a crucial membrane-integral nucleoporin of metazoan nuclear pore complexes. J. Cell Biol. 173, 509-519 (2006).
    • (2006) J. Cell Biol , vol.173 , pp. 509-519
    • Stavru, F.1
  • 56
    • 0027236761 scopus 로고
    • An integral membrane protein of the pore membrane domain of the nuclear envelope contains a nucleoporin-like region
    • Hallberg, E., Wozniak, R. W. & Blobel, G. An integral membrane protein of the pore membrane domain of the nuclear envelope contains a nucleoporin-like region. J. Cell Biol. 122, 513-521 (1993).
    • (1993) J. Cell Biol , vol.122 , pp. 513-521
    • Hallberg, E.1    Wozniak, R.W.2    Blobel, G.3
  • 57
    • 0025253486 scopus 로고
    • A major glycoprotein of the nuclear pore complex is a membrane-spanning polypeptide with a large lumenal domain and a small cytoplasmic tail
    • Greber, U. F., Senior, A. & Gerace, L. A major glycoprotein of the nuclear pore complex is a membrane-spanning polypeptide with a large lumenal domain and a small cytoplasmic tail. EMBO J. 9, 1495-1502 (1990).
    • (1990) EMBO J , vol.9 , pp. 1495-1502
    • Greber, U.F.1    Senior, A.2    Gerace, L.3
  • 58
    • 0030031968 scopus 로고    scopus 로고
    • A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores
    • Siniossoglou, S. et al. A novel complex of nucleoporins, which includes Sec13p and a Sec13p homolog, is essential for normal nuclear pores. Cell 84, 265-275 (1996).
    • (1996) Cell , vol.84 , pp. 265-275
    • Siniossoglou, S.1
  • 59
    • 0030824317 scopus 로고    scopus 로고
    • Nup93, a vertebrate homologue of yeast Nic96p, forms a complex with a novel 205 kDa protein and is required for correct nuclear pore assembly
    • Grandi, P. et al. Nup93, a vertebrate homologue of yeast Nic96p, forms a complex with a novel 205 kDa protein and is required for correct nuclear pore assembly. Mol. Biol. Cell 8, 2017-2038 (1997).
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2017-2038
    • Grandi, P.1
  • 60
    • 36749045172 scopus 로고    scopus 로고
    • The molecular architecture of the nuclear pore complex
    • Alber, F. et al. The molecular architecture of the nuclear pore complex. Nature 450, 695-701 (2007).
    • (2007) Nature , vol.450 , pp. 695-701
    • Alber, F.1
  • 61
    • 0029767680 scopus 로고    scopus 로고
    • Molecular and functional characterization of the p62 complex, an assembly of nuclear pore complex glycoproteins
    • Hu, T., Guan, T. & Gerace, L. Molecular and functional characterization of the p62 complex, an assembly of nuclear pore complex glycoproteins. J. Cell Biol. 134, 589-601 (1996).
    • (1996) J. Cell Biol , vol.134 , pp. 589-601
    • Hu, T.1    Guan, T.2    Gerace, L.3
  • 62
    • 33750701489 scopus 로고    scopus 로고
    • FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties
    • Frey, S., Richter, R. P. & Gorlich, D. FG-rich repeats of nuclear pore proteins form a three-dimensional meshwork with hydrogel-like properties. Science 314, 815-817 (2006).
    • (2006) Science , vol.314 , pp. 815-817
    • Frey, S.1    Richter, R.P.2    Gorlich, D.3
  • 63
    • 84865260520 scopus 로고    scopus 로고
    • The permeability of reconstituted nuclear pores provides direct evidence for the selective phase model
    • Hulsmann, B. B., Labokha, A. A. & Gorlich, D. The permeability of reconstituted nuclear pores provides direct evidence for the selective phase model. Cell 150, 738-751 (2012).
    • (2012) Cell , vol.150 , pp. 738-751
    • Hulsmann, B.B.1    Labokha, A.A.2    Gorlich, D.3
  • 64
    • 7944236264 scopus 로고    scopus 로고
    • Mapping the dynamic organization of the nuclear pore complex inside single living cells
    • Rabut, G., Doye, V. & Ellenberg, J. Mapping the dynamic organization of the nuclear pore complex inside single living cells. Nature Cell Biol. 6, 1114-1121 (2004).
    • (2004) Nature Cell Biol , vol.6 , pp. 1114-1121
    • Rabut, G.1    Doye, V.2    Ellenberg, J.3
  • 65
    • 33846262456 scopus 로고    scopus 로고
    • Abnormalities of the nucleus and nuclear inclusions in neurodegenerative disease: A work in progress
    • Woulfe, J. M. Abnormalities of the nucleus and nuclear inclusions in neurodegenerative disease: a work in progress. Neuropathol. Appl. Neurobiol. 33, 2-42 (2007).
    • (2007) Neuropathol. Appl. Neurobiol , vol.33 , pp. 2-42
    • Woulfe, J.M.1
  • 66
    • 0344835675 scopus 로고    scopus 로고
    • Nuclear envelope breakdown in starfish oocytes proceeds by partial NPC disassembly followed by a rapidly spreading fenestration of nuclear membranes
    • Lenart, P. et al. Nuclear envelope breakdown in starfish oocytes proceeds by partial NPC disassembly followed by a rapidly spreading fenestration of nuclear membranes. J. Cell Biol. 160, 1055-1068 (2003).
    • (2003) J. Cell Biol , vol.160 , pp. 1055-1068
    • Lenart, P.1
  • 68
    • 38949147783 scopus 로고    scopus 로고
    • Shaping the endoplasmic reticulum into the nuclear envelope
    • Anderson, D. J. & Hetzer, M. W. Shaping the endoplasmic reticulum into the nuclear envelope. J. Cell Sci. 121, 137-142 (2008).
    • (2008) J. Cell Sci , vol.121 , pp. 137-142
    • Anderson, D.J.1    Hetzer, M.W.2
  • 69
    • 77953724768 scopus 로고    scopus 로고
    • Cell cycle-dependent differences in nuclear pore complex assembly in metazoa
    • Doucet, C. M., Talamas, J. A. & Hetzer, M. W. Cell cycle-dependent differences in nuclear pore complex assembly in metazoa. Cell 141, 1030-1041 (2010).
    • (2010) Cell , vol.141 , pp. 1030-1041
    • Doucet, C.M.1    Talamas, J.A.2    Hetzer, M.W.3
  • 71
    • 0343463828 scopus 로고
    • Long-lived messenger RNA: Evidence from cotton seed germination
    • Dure, L. & Waters, L. Long-lived messenger RNA: evidence from cotton seed germination. Science 147, 410-412 (1965).
    • (1965) Science , vol.147 , pp. 410-412
    • Dure, L.1    Waters, L.2
  • 72
    • 0017402329 scopus 로고
    • Very long-lived messenger RNA in ovaries of Xenopus laevis
    • Ford, P. J., Mathieson, T. & Rosbash, M. Very long-lived messenger RNA in ovaries of Xenopus laevis. Dev. Biol. 57, 417-426 (1977).
    • (1977) Dev. Biol , vol.57 , pp. 417-426
    • Ford, P.J.1    Mathieson, T.2    Rosbash, M.3
  • 73
    • 84982342704 scopus 로고
    • Metabolism of myelin lipids: Incorporation of [3-14C]serine in brain lipids of the developing rabbit and their persistence in the central nervous system
    • Davison, A. N., Morgan, R. S., Wajda, M. & Wright, G. P. Metabolism of myelin lipids: incorporation of [3-14C]serine in brain lipids of the developing rabbit and their persistence in the central nervous system. J. Neurochem. 4, 360-365 (1959).
    • (1959) J. Neurochem , vol.4 , pp. 360-365
    • Davison, A.N.1    Morgan, R.S.2    Wajda, M.3    Wright, G.P.4
  • 74
    • 0344367465 scopus 로고
    • Metabolism of myelin lipids: Estimation and separation of brain lipids in the developing rabbit
    • Davison, A. N. & Wajda, M. Metabolism of myelin lipids: estimation and separation of brain lipids in the developing rabbit. J. Neurochem. 4, 353-359 (1959).
    • (1959) J. Neurochem , vol.4 , pp. 353-359
    • Davison, A.N.1    Wajda, M.2
  • 75
    • 79959836522 scopus 로고    scopus 로고
    • Chromatin structure as a mediator of aging
    • Feser, J. & Tyler, J. Chromatin structure as a mediator of aging. FEBS Lett. 585, 2041-2048 (2011).
    • (2011) FEBS Lett , vol.585 , pp. 2041-2048
    • Feser, J.1    Tyler, J.2
  • 76
    • 64249107059 scopus 로고    scopus 로고
    • Evidence for cardiomyocyte renewal in humans
    • Bergmann, O. et al. Evidence for cardiomyocyte renewal in humans. Science 324, 98-102 (2009).
    • (2009) Science , vol.324 , pp. 98-102
    • Bergmann, O.1
  • 78
    • 0016271161 scopus 로고
    • In vivo methylation and turnover of rat brain histones
    • Duerre, J. A. & Lee, C. T. In vivo methylation and turnover of rat brain histones. J. Neurochem. 23, 541-547 (1974).
    • (1974) J. Neurochem , vol.23 , pp. 541-547
    • Duerre, J.A.1    Lee, C.T.2
  • 79
    • 41549117597 scopus 로고    scopus 로고
    • A quantitative analysis software tool for mass spectrometry-based proteomics
    • Park, S. K., Venable, J. D., Xu, T. & Yates, J. R. A quantitative analysis software tool for mass spectrometry-based proteomics. Nature Methods 5, 319-322 (2008).
    • (2008) Nature Methods , vol.5 , pp. 319-322
    • Park, S.K.1    Venable, J.D.2    Xu, T.3    Yates, J.R.4
  • 81
    • 77955867860 scopus 로고    scopus 로고
    • Does accumulation of advanced glycation end products contribute to the aging phenotype?
    • Semba, R. D., Nicklett, E. J. & Ferrucci, L. Does accumulation of advanced glycation end products contribute to the aging phenotype? J. Gerontol. A Biol. Sci. Med. Sci. 65, 963-975 (2010).
    • (2010) J. Gerontol. A Biol. Sci. Med. Sci , vol.65 , pp. 963-975
    • Semba, R.D.1    Nicklett, E.J.2    Ferrucci, L.3
  • 82
    • 0030763201 scopus 로고    scopus 로고
    • Increased accumulation of the glycoxidation product Nε- (carboxymethyl)lysine in human tissues in diabetes and aging
    • Schleicher, E. D., Wagner, E. & Nerlich, A. G. Increased accumulation of the glycoxidation product Nε-(carboxymethyl)lysine in human tissues in diabetes and aging. J. Clin. Invest. 99, 457-468 (1997).
    • (1997) J. Clin. Invest , vol.99 , pp. 457-468
    • Schleicher, E.D.1    Wagner, E.2    Nerlich, A.G.3
  • 83
    • 0023769752 scopus 로고
    • Destabilization of lens protein conformation by glutathione mixed disulfide
    • Liang, J. N. & Pelletier, M. R. Destabilization of lens protein conformation by glutathione mixed disulfide. Exp. Eye Res. 47, 17-25 (1988).
    • (1988) Exp. Eye Res , vol.47 , pp. 17-25
    • Liang, J.N.1    Pelletier, M.R.2
  • 84
    • 0018194985 scopus 로고
    • Disulfide-linked high molecular weight protein associated with human cataract
    • Spector, A. & Roy, D. Disulfide-linked high molecular weight protein associated with human cataract. Proc. Natl Acad. Sci. USA 75, 3244-3248 (1978).
    • (1978) Proc. Natl Acad. Sci. USA , vol.75 , pp. 3244-3248
    • Spector, A.1    Roy, D.2
  • 85
    • 0028216737 scopus 로고
    • Post-translational modifications of water-soluble human lens crystallins from young adults
    • Miesbauer, L. R. et al. Post-translational modifications of water-soluble human lens crystallins from young adults. J. Biol. Chem. 269, 12494-12502 (1994).
    • (1994) J. Biol. Chem , vol.269 , pp. 12494-12502
    • Miesbauer, L.R.1
  • 86
    • 0030475908 scopus 로고    scopus 로고
    • Modifications of the water-insoluble human lens α-crystallins
    • Lund, A. L., Smith, J. B. & Smith, D. L. Modifications of the water-insoluble human lens α-crystallins. Exp. Eye Res. 63, 661-672 (1996).
    • (1996) Exp. Eye Res , vol.63 , pp. 661-672
    • Lund, A.L.1    Smith, J.B.2    Smith, D.L.3
  • 87
    • 84866488172 scopus 로고    scopus 로고
    • The heat shock response: Systems biology of proteotoxic stress in aging and disease
    • Morimoto, R. I. The heat shock response: systems biology of proteotoxic stress in aging and disease. Cold Spring Harb. Symp. Quant. Biol. 76, 91-99 (2011).
    • (2011) Cold Spring Harb. Symp. Quant. Biol , vol.76 , pp. 91-99
    • Morimoto, R.I.1
  • 88
    • 80053041158 scopus 로고    scopus 로고
    • Protein carbonylation and metal-catalyzed protein oxidation in a cellular perspective
    • Moller, I. M., Rogowska-Wrzesinska, A. & Rao, R. S. Protein carbonylation and metal-catalyzed protein oxidation in a cellular perspective. J. Proteom. 74, 2228-2242 (2011).
    • (2011) J. Proteom , vol.74 , pp. 2228-2242
    • Moller, I.M.1    Rogowska-Wrzesinska, A.2    Rao, R.S.3


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