메뉴 건너뛰기




Volumn 15, Issue 11, 2005, Pages 608-617

Cellular integrity plus: Organelle-related and protein-targeting functions of intermediate filaments

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; DESMIN; INTERMEDIATE FILAMENT PROTEIN; K 18; KERATIN; LAMIN A; LAMIN C; NEUROFILAMENT PROTEIN; VIMENTIN;

EID: 27744556965     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tcb.2005.09.004     Document Type: Review
Times cited : (221)

References (98)
  • 1
    • 0028283501 scopus 로고
    • Intermediate filaments: Structure, dynamics, function, and disease
    • E. Fuchs, and K. Weber Intermediate filaments: structure, dynamics, function, and disease Annu. Rev. Biochem. 63 1994 345 382
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 345-382
    • Fuchs, E.1    Weber, K.2
  • 2
    • 0033401358 scopus 로고    scopus 로고
    • The cytoskeleton of digestive epithelia in health and disease
    • N.O. Ku The cytoskeleton of digestive epithelia in health and disease Am. J. Physiol. 277 1999 G1108 G1137
    • (1999) Am. J. Physiol. , vol.277
    • Ku, N.O.1
  • 3
    • 1842381834 scopus 로고
    • Different intermediate-sized filaments distinguished by immunofluorescence microscopy
    • W.W. Franke Different intermediate-sized filaments distinguished by immunofluorescence microscopy Proc. Natl. Acad. Sci. U. S. A. 75 1978 5034 5038
    • (1978) Proc. Natl. Acad. Sci. U. S. A. , vol.75 , pp. 5034-5038
    • Franke, W.W.1
  • 4
    • 0018842868 scopus 로고
    • Intermediate filaments as mechanical integrators of cellular space
    • E. Lazarides Intermediate filaments as mechanical integrators of cellular space Nature 283 1980 249 256
    • (1980) Nature , vol.283 , pp. 249-256
    • Lazarides, E.1
  • 5
    • 3943078618 scopus 로고    scopus 로고
    • Intermediate filaments: Molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds
    • H. Herrmann, and U. Aebi Intermediate filaments: molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds Annu. Rev. Biochem. 73 2004 749 789
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 749-789
    • Herrmann, H.1    Aebi, U.2
  • 6
    • 0032559341 scopus 로고    scopus 로고
    • A structural scaffolding of intermediate filaments in health and disease
    • E. Fuchs, and D.W. Cleveland A structural scaffolding of intermediate filaments in health and disease Science 279 1998 514 519
    • (1998) Science , vol.279 , pp. 514-519
    • Fuchs, E.1    Cleveland, D.W.2
  • 7
    • 4143134431 scopus 로고    scopus 로고
    • Cytoplasmic intermediate filaments revealed as dynamic and multipurpose scaffolds
    • P.A. Coulombe, and P. Wong Cytoplasmic intermediate filaments revealed as dynamic and multipurpose scaffolds Nat. Cell Biol. 6 2004 699 706
    • (2004) Nat. Cell Biol. , vol.6 , pp. 699-706
    • Coulombe, P.A.1    Wong, P.2
  • 8
    • 6344273968 scopus 로고    scopus 로고
    • Intermediate filament proteins and their associated diseases
    • M.B. Omary Intermediate filament proteins and their associated diseases N. Engl. J. Med. 351 2004 2087 2100
    • (2004) N. Engl. J. Med. , vol.351 , pp. 2087-2100
    • Omary, M.B.1
  • 9
    • 0030023118 scopus 로고    scopus 로고
    • Integration of intermediate filaments into cellular organelles
    • S.D. Georgatos, and C. Maison Integration of intermediate filaments into cellular organelles Int. Rev. Cytol. 164 1996 91 138
    • (1996) Int. Rev. Cytol. , vol.164 , pp. 91-138
    • Georgatos, S.D.1    Maison, C.2
  • 10
    • 17444383492 scopus 로고    scopus 로고
    • Intermediate filaments and vesicular membrane traffic: The odd couple's first dance?
    • M.L. Styers intermediate filaments and vesicular membrane traffic: the odd couple's first dance? Traffic 6 2005 359 365
    • (2005) Traffic , vol.6 , pp. 359-365
    • Styers, M.L.1
  • 11
    • 0141954052 scopus 로고    scopus 로고
    • Mechanisms of mitochondria-neurofilament interactions
    • O.I. Wagner Mechanisms of mitochondria-neurofilament interactions J. Neurosci. 23 2003 9046 9058
    • (2003) J. Neurosci. , vol.23 , pp. 9046-9058
    • Wagner, O.I.1
  • 12
    • 0029810901 scopus 로고    scopus 로고
    • The genetic basis of epidermolysis bullosa simplex with mottled pigmentation
    • J. Uttam The genetic basis of epidermolysis bullosa simplex with mottled pigmentation Proc. Natl. Acad. Sci. U. S. A. 93 1996 9079 9084
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 9079-9084
    • Uttam, J.1
  • 13
    • 0036872241 scopus 로고    scopus 로고
    • Desmin cytoskeleton: A potential regulator of muscle mitochondrial behavior and function
    • Y. Capetanaki Desmin cytoskeleton: a potential regulator of muscle mitochondrial behavior and function Trends Cardiovasc. Med. 12 2002 339 348
    • (2002) Trends Cardiovasc. Med. , vol.12 , pp. 339-348
    • Capetanaki, Y.1
  • 14
    • 6344260556 scopus 로고    scopus 로고
    • Desmin: A major intermediate filament protein essential for the structural integrity and function of muscle
    • D. Paulin, and Z. Li Desmin: a major intermediate filament protein essential for the structural integrity and function of muscle Exp. Cell Res. 301 2004 1 7
    • (2004) Exp. Cell Res. , vol.301 , pp. 1-7
    • Paulin, D.1    Li, Z.2
  • 15
    • 0029738727 scopus 로고    scopus 로고
    • Disruption of muscle architecture and myocardial degeneration in mice lacking desmin
    • D.J. Milner Disruption of muscle architecture and myocardial degeneration in mice lacking desmin J. Cell Biol. 134 1996 1255 1270
    • (1996) J. Cell Biol. , vol.134 , pp. 1255-1270
    • Milner, D.J.1
  • 16
    • 0029893923 scopus 로고    scopus 로고
    • Cardiovascular lesions and skeletal myopathy in mice lacking desmin
    • Z. Li Cardiovascular lesions and skeletal myopathy in mice lacking desmin Dev. Biol. 175 1996 362 366
    • (1996) Dev. Biol. , vol.175 , pp. 362-366
    • Li, Z.1
  • 17
    • 0034683573 scopus 로고    scopus 로고
    • Desmin cytoskeleton linked to muscle mitochondrial distribution and respiratory function
    • D.J. Milner Desmin cytoskeleton linked to muscle mitochondrial distribution and respiratory function J. Cell Biol. 150 2000 1283 1298
    • (2000) J. Cell Biol. , vol.150 , pp. 1283-1298
    • Milner, D.J.1
  • 18
    • 0034750422 scopus 로고    scopus 로고
    • Effects of desmin gene knockout on mice heart mitochondria
    • M. Linden Effects of desmin gene knockout on mice heart mitochondria J. Bioenerg. Biomembr. 33 2001 333 341
    • (2001) J. Bioenerg. Biomembr. , vol.33 , pp. 333-341
    • Linden, M.1
  • 19
    • 1642433232 scopus 로고    scopus 로고
    • Bcl-2 overexpression corrects mitochondrial defects and ameliorates inherited desmin null cardiomyopathy
    • N. Weisleder Bcl-2 overexpression corrects mitochondrial defects and ameliorates inherited desmin null cardiomyopathy Proc. Natl. Acad. Sci. U. S. A. 101 2004 769 774
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 769-774
    • Weisleder, N.1
  • 20
    • 0037444403 scopus 로고    scopus 로고
    • On noxious desmin: Functional effects of a novel heterozygous desmin insertion mutation on the extrasarcomeric desmin cytoskeleton and mitochondria
    • R. Schroder On noxious desmin: functional effects of a novel heterozygous desmin insertion mutation on the extrasarcomeric desmin cytoskeleton and mitochondria Hum. Mol. Genet. 12 2003 657 669
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 657-669
    • Schroder, R.1
  • 21
    • 0036849511 scopus 로고    scopus 로고
    • Charcot-Marie-Tooth disease neurofilament mutations disrupt neurofilament assembly and axonal transport
    • J. Brownlees Charcot-Marie-Tooth disease neurofilament mutations disrupt neurofilament assembly and axonal transport Hum. Mol. Genet. 11 2002 2837 2844
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2837-2844
    • Brownlees, J.1
  • 22
    • 18844446126 scopus 로고    scopus 로고
    • Mutations in the neurofilament light gene linked to Charcot-Marie-Tooth disease cause defects in transport
    • R. Perez-Olle Mutations in the neurofilament light gene linked to Charcot-Marie-Tooth disease cause defects in transport J. Neurochem. 93 2005 861 874
    • (2005) J. Neurochem. , vol.93 , pp. 861-874
    • Perez-Olle, R.1
  • 23
    • 0029833513 scopus 로고    scopus 로고
    • Alterations in neural intermediate filament organization: Functional implications and the induction of pathological changes related to motor neuron disease
    • K. Straube-West Alterations in neural intermediate filament organization: functional implications and the induction of pathological changes related to motor neuron disease J. Cell Sci. 109 1996 2319 2329
    • (1996) J. Cell Sci. , vol.109 , pp. 2319-2329
    • Straube-West, K.1
  • 24
    • 26444595257 scopus 로고    scopus 로고
    • Expression of an LMNA-N195K variant of A-type lamins results in cardiac conduction defects and death in mice
    • L.C. Mounkes Expression of an LMNA-N195K variant of A-type lamins results in cardiac conduction defects and death in mice Hum. Mol. Genet. 14 2005 2167 2180
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 2167-2180
    • Mounkes, L.C.1
  • 25
    • 14744290497 scopus 로고    scopus 로고
    • Alterations in the heart mitochondrial proteome in a desmin null heart failure model
    • M. Fountoulakis Alterations in the heart mitochondrial proteome in a desmin null heart failure model J. Mol. Cell. Cardiol. 38 2005 461 474
    • (2005) J. Mol. Cell. Cardiol. , vol.38 , pp. 461-474
    • Fountoulakis, M.1
  • 26
    • 0034599872 scopus 로고    scopus 로고
    • Keratin-dependent, epithelial resistance to tumor necrosis factor-induced apoptosis
    • C. Caulin Keratin-dependent, epithelial resistance to tumor necrosis factor-induced apoptosis J. Cell Biol. 149 2000 17 22
    • (2000) J. Cell Biol. , vol.149 , pp. 17-22
    • Caulin, C.1
  • 27
    • 0035921430 scopus 로고    scopus 로고
    • Simple epithelium keratins 8 and 18 provide resistance to Fas-mediated apoptosis. the protection occurs through a receptor-targeting modulation
    • S. Gilbert Simple epithelium keratins 8 and 18 provide resistance to Fas-mediated apoptosis. The protection occurs through a receptor-targeting modulation J. Cell Biol. 154 2001 763 773
    • (2001) J. Cell Biol. , vol.154 , pp. 763-773
    • Gilbert, S.1
  • 28
    • 0037847551 scopus 로고    scopus 로고
    • Keratin mutation in transgenic mice predisposes to Fas but not TNF-induced apoptosis and massive liver injury
    • N.O. Ku Keratin mutation in transgenic mice predisposes to Fas but not TNF-induced apoptosis and massive liver injury Hepatology 37 2003 1006 1014
    • (2003) Hepatology , vol.37 , pp. 1006-1014
    • Ku, N.O.1
  • 29
    • 0036606803 scopus 로고    scopus 로고
    • Keratin 17 null mice exhibit age- and strain-dependent alopecia
    • K.M. McGowan Keratin 17 null mice exhibit age- and strain-dependent alopecia Genes Dev. 16 2002 1412 1422
    • (2002) Genes Dev. , vol.16 , pp. 1412-1422
    • McGowan, K.M.1
  • 30
    • 0034614647 scopus 로고    scopus 로고
    • The road taken: Past and future foundations of membrane traffic
    • I. Mellman, and G. Warren The road taken: past and future foundations of membrane traffic Cell 100 2000 99 112
    • (2000) Cell , vol.100 , pp. 99-112
    • Mellman, I.1    Warren, G.2
  • 31
    • 0026110741 scopus 로고
    • Association of cytoskeletons with the Golgi apparatus: Three-dimensional observation and computer-graphic reconstruction
    • T. Katsumoto Association of cytoskeletons with the Golgi apparatus: three-dimensional observation and computer-graphic reconstruction J. Electron Microsc. (Tokyo) 40 1991 24 28
    • (1991) J. Electron Microsc. (Tokyo) , vol.40 , pp. 24-28
    • Katsumoto, T.1
  • 32
    • 0035809911 scopus 로고    scopus 로고
    • A novel interaction of the Golgi complex with the vimentin intermediate filament cytoskeleton
    • Y. Gao, and E. Sztul A novel interaction of the Golgi complex with the vimentin intermediate filament cytoskeleton J. Cell Biol. 152 2001 877 894
    • (2001) J. Cell Biol. , vol.152 , pp. 877-894
    • Gao, Y.1    Sztul, E.2
  • 33
    • 0036020958 scopus 로고    scopus 로고
    • A novel type of regulation of the vimentin intermediate filament cytoskeleton by a Golgi protein
    • Y.S. Gao A novel type of regulation of the vimentin intermediate filament cytoskeleton by a Golgi protein Eur. J. Cell Biol. 81 2002 391 401
    • (2002) Eur. J. Cell Biol. , vol.81 , pp. 391-401
    • Gao, Y.S.1
  • 34
    • 9444239263 scopus 로고    scopus 로고
    • The endo-lysosomal sorting machinery interacts with the intermediate filament cytoskeleton
    • M.L. Styers The endo-lysosomal sorting machinery interacts with the intermediate filament cytoskeleton Mol. Biol. Cell 15 2004 5369 5382
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5369-5382
    • Styers, M.L.1
  • 35
    • 0032146206 scopus 로고    scopus 로고
    • Decreased synthesis of glycosphingolipids in cells lacking vimentin intermediate filaments
    • B.K. Gillard Decreased synthesis of glycosphingolipids in cells lacking vimentin intermediate filaments Exp. Cell Res. 242 1998 561 572
    • (1998) Exp. Cell Res. , vol.242 , pp. 561-572
    • Gillard, B.K.1
  • 36
    • 0030464976 scopus 로고    scopus 로고
    • Disruption of the vimentin intermediate filament system during adipose conversion of 3T3-L1 cells inhibits lipid droplet accumulation
    • J.G. Lieber, and R.M. Evans Disruption of the vimentin intermediate filament system during adipose conversion of 3T3-L1 cells inhibits lipid droplet accumulation J. Cell Sci. 109 1996 3047 3058
    • (1996) J. Cell Sci. , vol.109 , pp. 3047-3058
    • Lieber, J.G.1    Evans, R.M.2
  • 37
    • 0026744762 scopus 로고
    • A functional role for vimentin intermediate filaments in the metabolism of lipoprotein-derived cholesterol in human SW-13 cells
    • A.J. Sarria A functional role for vimentin intermediate filaments in the metabolism of lipoprotein-derived cholesterol in human SW-13 cells J. Biol. Chem. 267 1992 19455 19463
    • (1992) J. Biol. Chem. , vol.267 , pp. 19455-19463
    • Sarria, A.J.1
  • 38
    • 0037177831 scopus 로고    scopus 로고
    • MICAL, a novel CasL interacting molecule, associates with vimentin
    • T. Suzuki MICAL, a novel CasL interacting molecule, associates with vimentin J. Biol. Chem. 277 2002 14933 14941
    • (2002) J. Biol. Chem. , vol.277 , pp. 14933-14941
    • Suzuki, T.1
  • 39
    • 0347362573 scopus 로고    scopus 로고
    • Aggregation and loss of cytokeratin filament networks inhibit Golgi organization in liver-derived epithelial cell lines
    • H. Kumemura Aggregation and loss of cytokeratin filament networks inhibit Golgi organization in liver-derived epithelial cell lines Cell Motil. Cytoskeleton 57 2004 37 52
    • (2004) Cell Motil. Cytoskeleton , vol.57 , pp. 37-52
    • Kumemura, H.1
  • 40
    • 0033972489 scopus 로고    scopus 로고
    • The neuronal Golgi apparatus is fragmented in transgenic mice expressing a mutant human SOD1, but not in mice expressing the human NF-H gene
    • A. Stieber The neuronal Golgi apparatus is fragmented in transgenic mice expressing a mutant human SOD1, but not in mice expressing the human NF-H gene J. Neurol. Sci. 173 2000 63 72
    • (2000) J. Neurol. Sci. , vol.173 , pp. 63-72
    • Stieber, A.1
  • 41
    • 0038697678 scopus 로고    scopus 로고
    • Golgi disassembly in apoptosis: Cause or effect?
    • C.E. Machamer Golgi disassembly in apoptosis: cause or effect? Trends Cell Biol. 13 2003 279 281
    • (2003) Trends Cell Biol. , vol.13 , pp. 279-281
    • MacHamer, C.E.1
  • 42
    • 1842556279 scopus 로고    scopus 로고
    • Adaptable adaptors for coated vesicles
    • M.S. Robinson Adaptable adaptors for coated vesicles Trends Cell Biol. 14 2004 167 174
    • (2004) Trends Cell Biol. , vol.14 , pp. 167-174
    • Robinson, M.S.1
  • 43
    • 0024808206 scopus 로고
    • Intermediate filaments and ubiquitin: A new thread in the understanding of chronic neurodegenerative diseases
    • R.J. Mayer Intermediate filaments and ubiquitin: a new thread in the understanding of chronic neurodegenerative diseases Prog. Clin. Biol. Res. 317 1989 809 818
    • (1989) Prog. Clin. Biol. Res. , vol.317 , pp. 809-818
    • Mayer, R.J.1
  • 44
    • 0022272935 scopus 로고
    • Intermediate filaments: Possible functions as cytoskeletal connecting links between the nucleus and the cell surface
    • R. Goldman Intermediate filaments: possible functions as cytoskeletal connecting links between the nucleus and the cell surface Ann. N. Y. Acad. Sci. 455 1985 1 17
    • (1985) Ann. N. Y. Acad. Sci. , vol.455 , pp. 1-17
    • Goldman, R.1
  • 45
    • 0028361169 scopus 로고
    • The presence or absence of a vimentin-type intermediate filament network affects the shape of the nucleus in human SW-13 cells
    • A.J. Sarria The presence or absence of a vimentin-type intermediate filament network affects the shape of the nucleus in human SW-13 cells J. Cell Sci. 107 1994 1593 1607
    • (1994) J. Cell Sci. , vol.107 , pp. 1593-1607
    • Sarria, A.J.1
  • 46
    • 2142816651 scopus 로고    scopus 로고
    • Structural and functional roles of desmin in mouse skeletal muscle during passive deformation
    • S.B. Shah Structural and functional roles of desmin in mouse skeletal muscle during passive deformation Biophys. J. 86 2004 2993 3008
    • (2004) Biophys. J. , vol.86 , pp. 2993-3008
    • Shah, S.B.1
  • 47
    • 0036629336 scopus 로고    scopus 로고
    • Hyperproliferation, induction of c-Myc and 14-3-3sigma, but no cell fragility in keratin-10-null mice
    • J. Reichelt, and T.M. Magin Hyperproliferation, induction of c-Myc and 14-3-3sigma, but no cell fragility in keratin-10-null mice J. Cell Sci. 115 2002 2639 2650
    • (2002) J. Cell Sci. , vol.115 , pp. 2639-2650
    • Reichelt, J.1    Magin, T.M.2
  • 48
    • 0026725118 scopus 로고
    • Transgenic mice expressing a mutant keratin 10 gene reveal the likely genetic basis for epidermolytic hyperkeratosis
    • E. Fuchs Transgenic mice expressing a mutant keratin 10 gene reveal the likely genetic basis for epidermolytic hyperkeratosis Proc. Natl. Acad. Sci. U. S. A. 89 1992 6906 6910
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 6906-6910
    • Fuchs, E.1
  • 49
    • 0035180120 scopus 로고    scopus 로고
    • Disturbances in hepatic cell-cycle regulation in mice with assembly-deficient keratins 8/18
    • D.M. Toivola Disturbances in hepatic cell-cycle regulation in mice with assembly-deficient keratins 8/18 Hepatology 34 2001 1174 1183
    • (2001) Hepatology , vol.34 , pp. 1174-1183
    • Toivola, D.M.1
  • 50
    • 14244267052 scopus 로고    scopus 로고
    • Keratin mutation primes mouse liver to oxidative injury
    • Q. Zhou Keratin mutation primes mouse liver to oxidative injury Hepatology 41 2005 517 525
    • (2005) Hepatology , vol.41 , pp. 517-525
    • Zhou, Q.1
  • 51
    • 26444621444 scopus 로고    scopus 로고
    • Gene expression analysis in mice with elevated glial fibrillary acidic protein and Rosenthal fibers reveals a stress response followed by glial activation and neuronal dysfunction
    • T.L. Hagemann Gene expression analysis in mice with elevated glial fibrillary acidic protein and Rosenthal fibers reveals a stress response followed by glial activation and neuronal dysfunction Hum. Mol. Genet. 14 2005 2443 2458
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 2443-2458
    • Hagemann, T.L.1
  • 52
    • 0028197466 scopus 로고
    • Inhibition of desmin expression blocks myoblast fusion and interferes with the myogenic regulators MyoD and myogenin
    • H. Li Inhibition of desmin expression blocks myoblast fusion and interferes with the myogenic regulators MyoD and myogenin J. Cell Biol. 124 1994 827 841
    • (1994) J. Cell Biol. , vol.124 , pp. 827-841
    • Li, H.1
  • 53
    • 17444388553 scopus 로고    scopus 로고
    • Intermediate filament associated proteins
    • K.J. Green Intermediate filament associated proteins Adv. Protein Chem. 70 2005 143 202
    • (2005) Adv. Protein Chem. , vol.70 , pp. 143-202
    • Green, K.J.1
  • 54
    • 4143116817 scopus 로고    scopus 로고
    • Raf-1 activation disrupts its binding to keratins during cell stress
    • N.O. Ku Raf-1 activation disrupts its binding to keratins during cell stress J. Cell Biol. 166 2004 479 485
    • (2004) J. Cell Biol. , vol.166 , pp. 479-485
    • Ku, N.O.1
  • 55
    • 0037007011 scopus 로고    scopus 로고
    • Keratin binding to 14-3-3 proteins modulates keratin filaments and hepatocyte mitotic progression
    • N.O. Ku Keratin binding to 14-3-3 proteins modulates keratin filaments and hepatocyte mitotic progression Proc. Natl. Acad. Sci. U. S. A. 99 2002 4373 4378
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 4373-4378
    • Ku, N.O.1
  • 56
    • 7944219648 scopus 로고    scopus 로고
    • A-type lamins: Guardians of the soma?
    • C.J. Hutchison, and H.J. Worman A-type lamins: guardians of the soma? Nat. Cell Biol. 6 2004 1062 1067
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1062-1067
    • Hutchison, C.J.1    Worman, H.J.2
  • 57
    • 0027509502 scopus 로고
    • CDNA cloning of a germ cell specific lamin B3 from mouse spermatocytes and analysis of its function by ectopic expression in somatic cells
    • K. Furukawa, and Y. Hotta cDNA cloning of a germ cell specific lamin B3 from mouse spermatocytes and analysis of its function by ectopic expression in somatic cells EMBO J. 12 1993 97 106
    • (1993) EMBO J. , vol.12 , pp. 97-106
    • Furukawa, K.1    Hotta, Y.2
  • 58
    • 7944221826 scopus 로고    scopus 로고
    • Laminopathies
    • J.L. Broers Laminopathies J. Pathol. 204 2004 478 488
    • (2004) J. Pathol. , vol.204 , pp. 478-488
    • Broers, J.L.1
  • 59
    • 0344309291 scopus 로고    scopus 로고
    • Nuclear envelope alterations in fibroblasts from LGMD1B patients carrying nonsense Y259X heterozygous or homozygous mutation in lamin A/C gene
    • A. Muchir Nuclear envelope alterations in fibroblasts from LGMD1B patients carrying nonsense Y259X heterozygous or homozygous mutation in lamin A/C gene Exp. Cell Res. 291 2003 352 362
    • (2003) Exp. Cell Res. , vol.291 , pp. 352-362
    • Muchir, A.1
  • 60
    • 0033615969 scopus 로고    scopus 로고
    • Loss of A-type lamin expression compromises nuclear envelope integrity leading to muscular dystrophy
    • T. Sullivan Loss of A-type lamin expression compromises nuclear envelope integrity leading to muscular dystrophy J. Cell Biol. 147 1999 913 920
    • (1999) J. Cell Biol. , vol.147 , pp. 913-920
    • Sullivan, T.1
  • 61
    • 11144355499 scopus 로고    scopus 로고
    • Defects in nuclear structure and function promote dilated cardiomyopathy in lamin A/C-deficient mice
    • V. Nikolova Defects in nuclear structure and function promote dilated cardiomyopathy in lamin A/C-deficient mice J. Clin. Invest. 113 2004 357 369
    • (2004) J. Clin. Invest. , vol.113 , pp. 357-369
    • Nikolova, V.1
  • 62
    • 1542317663 scopus 로고    scopus 로고
    • Lamin A/C deficiency causes defective nuclear mechanics and mechanotransduction
    • J. Lammerding Lamin A/C deficiency causes defective nuclear mechanics and mechanotransduction J. Clin. Invest. 113 2004 370 378
    • (2004) J. Clin. Invest. , vol.113 , pp. 370-378
    • Lammerding, J.1
  • 63
    • 1642503683 scopus 로고    scopus 로고
    • Intermediate filaments are dynamic and motile elements of cellular architecture
    • B.T. Helfand Intermediate filaments are dynamic and motile elements of cellular architecture J. Cell Sci. 117 2004 133 141
    • (2004) J. Cell Sci. , vol.117 , pp. 133-141
    • Helfand, B.T.1
  • 64
    • 14644401811 scopus 로고    scopus 로고
    • Organization of vesicular trafficking in epithelia
    • E. Rodriguez-Boulan Organization of vesicular trafficking in epithelia Nat. Rev. Mol. Cell Biol. 6 2005 233 247
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 233-247
    • Rodriguez-Boulan, E.1
  • 65
    • 0035110609 scopus 로고    scopus 로고
    • Anomalous apical plasma membrane phenotype in CK8-deficient mice indicates a novel role for intermediate filaments in the polarization of simple epithelia
    • N.A. Ameen Anomalous apical plasma membrane phenotype in CK8-deficient mice indicates a novel role for intermediate filaments in the polarization of simple epithelia J. Cell Sci. 114 2001 563 575
    • (2001) J. Cell Sci. , vol.114 , pp. 563-575
    • Ameen, N.A.1
  • 66
    • 0033790324 scopus 로고    scopus 로고
    • Vimentin filaments in fibroblasts are a reservoir for SNAP23, a component of the membrane fusion machinery
    • W. Faigle Vimentin filaments in fibroblasts are a reservoir for SNAP23, a component of the membrane fusion machinery Mol. Biol. Cell 11 2000 3485 3494
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3485-3494
    • Faigle, W.1
  • 67
    • 1642348652 scopus 로고    scopus 로고
    • Keratins modulate colonocyte electrolyte transport via protein mistargeting
    • D.M. Toivola Keratins modulate colonocyte electrolyte transport via protein mistargeting J. Cell Biol. 164 2004 911 921
    • (2004) J. Cell Biol. , vol.164 , pp. 911-921
    • Toivola, D.M.1
  • 68
    • 0030991810 scopus 로고    scopus 로고
    • The apical submembrane cytoskeleton participates in the organization of the apical pole in epithelial cells
    • P.J. Salas The apical submembrane cytoskeleton participates in the organization of the apical pole in epithelial cells J. Cell Biol. 137 1997 359 375
    • (1997) J. Cell Biol. , vol.137 , pp. 359-375
    • Salas, P.J.1
  • 69
    • 0033364677 scopus 로고    scopus 로고
    • Reduction of cytochemical ecto-ATPase activities in keratin 8-deficient FVB/N mouse livers
    • M.I. Satoh Reduction of cytochemical ecto-ATPase activities in keratin 8-deficient FVB/N mouse livers Med. Electron Microsc. 32 1999 209 212
    • (1999) Med. Electron Microsc. , vol.32 , pp. 209-212
    • Satoh, M.I.1
  • 70
    • 20044393806 scopus 로고    scopus 로고
    • Keratin-containing inclusions affect cell morphology and distribution of cytosolic cellular components
    • S. Hanada Keratin-containing inclusions affect cell morphology and distribution of cytosolic cellular components Exp. Cell Res. 304 2005 471 482
    • (2005) Exp. Cell Res. , vol.304 , pp. 471-482
    • Hanada, S.1
  • 72
    • 19444375279 scopus 로고    scopus 로고
    • Keratin-8-deficient mice develop chronic spontaneous Th2 colitis amenable to antibiotic treatment
    • A. Habtezion Keratin-8-deficient mice develop chronic spontaneous Th2 colitis amenable to antibiotic treatment J. Cell Sci. 118 2005 1971 1980
    • (2005) J. Cell Sci. , vol.118 , pp. 1971-1980
    • Habtezion, A.1
  • 73
    • 22544475951 scopus 로고    scopus 로고
    • Remodeling of gap junctions and slow conduction in a mouse model of desmin-related cardiomyopathy
    • J.J. Gard Remodeling of gap junctions and slow conduction in a mouse model of desmin-related cardiomyopathy Cardiovasc. Res. 67 2005 537 547
    • (2005) Cardiovasc. Res. , vol.67 , pp. 537-547
    • Gard, J.J.1
  • 74
    • 0037373876 scopus 로고    scopus 로고
    • Knockout of the intermediate filament protein CP49 destabilises the lens fibre cell cytoskeleton and decreases lens optical quality, but does not induce cataract
    • A. Sandilands Knockout of the intermediate filament protein CP49 destabilises the lens fibre cell cytoskeleton and decreases lens optical quality, but does not induce cataract Exp. Eye Res. 76 2003 385 391
    • (2003) Exp. Eye Res. , vol.76 , pp. 385-391
    • Sandilands, A.1
  • 75
    • 0037084401 scopus 로고    scopus 로고
    • Vimentin affects localization and activity of sodium-glucose cotransporter SGLT1 in membrane rafts
    • I. Runembert Vimentin affects localization and activity of sodium-glucose cotransporter SGLT1 in membrane rafts J. Cell Sci. 115 2002 713 724
    • (2002) J. Cell Sci. , vol.115 , pp. 713-724
    • Runembert, I.1
  • 76
    • 7944223409 scopus 로고    scopus 로고
    • Astrocyte intermediate filaments in CNS pathologies and regeneration
    • M. Pekny, and M. Pekna Astrocyte intermediate filaments in CNS pathologies and regeneration J. Pathol. 204 2004 428 437
    • (2004) J. Pathol. , vol.204 , pp. 428-437
    • Pekny, M.1    Pekna, M.2
  • 77
    • 0028238846 scopus 로고
    • Changes in proteasome localization during the cell cycle
    • A. Palmer Changes in proteasome localization during the cell cycle Eur. J. Cell Biol. 64 1994 163 175
    • (1994) Eur. J. Cell Biol. , vol.64 , pp. 163-175
    • Palmer, A.1
  • 78
    • 0033918858 scopus 로고    scopus 로고
    • Specific types of prosomes distribute differentially between intermediate and actin filaments in epithelial, fibroblastic and muscle cells
    • C. Arcangeletti Specific types of prosomes distribute differentially between intermediate and actin filaments in epithelial, fibroblastic and muscle cells Eur. J. Cell Biol. 79 2000 423 437
    • (2000) Eur. J. Cell Biol. , vol.79 , pp. 423-437
    • Arcangeletti, C.1
  • 79
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • J.A. Johnston Aggresomes: a cellular response to misfolded proteins J. Cell Biol. 143 1998 1883 1898
    • (1998) J. Cell Biol. , vol.143 , pp. 1883-1898
    • Johnston, J.A.1
  • 80
    • 4143087186 scopus 로고    scopus 로고
    • Neuronal diseases: Small heat shock proteins calm your nerves
    • M. Der Perng, and R.A. Quinlan Neuronal diseases: small heat shock proteins calm your nerves Curr. Biol. 14 2004 R625 R626
    • (2004) Curr. Biol. , vol.14
    • Der Perng, M.1    Quinlan, R.A.2
  • 81
    • 0242637569 scopus 로고    scopus 로고
    • AlphaB-crystallin modulates protein aggregation of abnormal desmin
    • X. Wang AlphaB-crystallin modulates protein aggregation of abnormal desmin Circ. Res. 93 2003 998 1005
    • (2003) Circ. Res. , vol.93 , pp. 998-1005
    • Wang, X.1
  • 82
    • 2642563501 scopus 로고    scopus 로고
    • Mutant small heat-shock protein 27 causes axonal Charcot-Marie-Tooth disease and distal hereditary motor neuropathy
    • O.V. Evgrafov Mutant small heat-shock protein 27 causes axonal Charcot-Marie-Tooth disease and distal hereditary motor neuropathy Nat. Genet. 36 2004 602 606
    • (2004) Nat. Genet. , vol.36 , pp. 602-606
    • Evgrafov, O.V.1
  • 83
    • 6344241870 scopus 로고    scopus 로고
    • Small heat shock protein alphaB-crystallin is part of cell cycle-dependent Golgi reorganization
    • R.K. Gangalum Small heat shock protein alphaB-crystallin is part of cell cycle-dependent Golgi reorganization J. Biol. Chem. 279 2004 43374 43377
    • (2004) J. Biol. Chem. , vol.279 , pp. 43374-43377
    • Gangalum, R.K.1
  • 84
    • 0037179756 scopus 로고    scopus 로고
    • Hsp27 upregulation and phosphorylation is required for injured sensory and motor neuron survival
    • S.C. Benn Hsp27 upregulation and phosphorylation is required for injured sensory and motor neuron survival Neuron 36 2002 45 56
    • (2002) Neuron , vol.36 , pp. 45-56
    • Benn, S.C.1
  • 85
    • 0842303213 scopus 로고    scopus 로고
    • Roles of molecular chaperones in protein misfolding diseases
    • J.M. Barral Roles of molecular chaperones in protein misfolding diseases Semin. Cell Dev. Biol. 15 2004 17 29
    • (2004) Semin. Cell Dev. Biol. , vol.15 , pp. 17-29
    • Barral, J.M.1
  • 86
    • 3543113113 scopus 로고    scopus 로고
    • Intermediate filaments mediate cytoskeletal crosstalk
    • L. Chang, and R.D. Goldman Intermediate filaments mediate cytoskeletal crosstalk Nat. Rev. Mol. Cell Biol. 5 2004 601 613
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 601-613
    • Chang, L.1    Goldman, R.D.2
  • 87
    • 0034783306 scopus 로고    scopus 로고
    • Pathogenesis of the permeability barrier abnormality in epidermolytic hyperkeratosis
    • M. Schmuth Pathogenesis of the permeability barrier abnormality in epidermolytic hyperkeratosis J. Invest. Dermatol. 117 2001 837 847
    • (2001) J. Invest. Dermatol. , vol.117 , pp. 837-847
    • Schmuth, M.1
  • 88
    • 0025308820 scopus 로고
    • Three-dimensional and histochemical studies of peroxisomes in cultured hepatocytes by quick-freezing and deep-etching method
    • S. Ohno, and Y. Fujii Three-dimensional and histochemical studies of peroxisomes in cultured hepatocytes by quick-freezing and deep-etching method Histochem. J. 22 1990 143 154
    • (1990) Histochem. J. , vol.22 , pp. 143-154
    • Ohno, S.1    Fujii, Y.2
  • 89
    • 16244397057 scopus 로고    scopus 로고
    • Absence of peroxisomes in mouse hepatocytes causes mitochondrial and ER abnormalities
    • R. Dirkx Absence of peroxisomes in mouse hepatocytes causes mitochondrial and ER abnormalities Hepatology 41 2005 868 878
    • (2005) Hepatology , vol.41 , pp. 868-878
    • Dirkx, R.1
  • 90
    • 0038731167 scopus 로고    scopus 로고
    • Caspase-independent cell death in T lymphocytes
    • M. Jaattela, and J. Tschopp Caspase-independent cell death in T lymphocytes Nat. Immunol. 4 2003 416 423
    • (2003) Nat. Immunol. , vol.4 , pp. 416-423
    • Jaattela, M.1    Tschopp, J.2
  • 91
    • 0034907507 scopus 로고    scopus 로고
    • Genes for intermediate filament proteins and the draft sequence of the human genome: Novel keratin genes and a surprisingly high number of pseudogenes related to keratin genes 8 and 18
    • M. Hesse Genes for intermediate filament proteins and the draft sequence of the human genome: novel keratin genes and a surprisingly high number of pseudogenes related to keratin genes 8 and 18 J. Cell Sci. 114 2001 2569 2575
    • (2001) J. Cell Sci. , vol.114 , pp. 2569-2575
    • Hesse, M.1
  • 93
    • 1842584782 scopus 로고    scopus 로고
    • Proteins that bind A-type lamins: Integrating isolated clues
    • M.S. Zastrow Proteins that bind A-type lamins: integrating isolated clues J. Cell Sci. 117 2004 979 987
    • (2004) J. Cell Sci. , vol.117 , pp. 979-987
    • Zastrow, M.S.1
  • 94
    • 14244262401 scopus 로고    scopus 로고
    • Intermediate filament protein inclusions
    • K. Zatloukal Intermediate filament protein inclusions Methods Cell Biol. 78 2004 205 228
    • (2004) Methods Cell Biol. , vol.78 , pp. 205-228
    • Zatloukal, K.1
  • 95
    • 1842734895 scopus 로고    scopus 로고
    • Desmin myopathy
    • L.G. Goldfarb Desmin myopathy Brain 127 2004 723 734
    • (2004) Brain , vol.127 , pp. 723-734
    • Goldfarb, L.G.1
  • 96
    • 7944236911 scopus 로고    scopus 로고
    • The cytoskeleton in neurodegenerative diseases
    • N.J. Cairns The cytoskeleton in neurodegenerative diseases J. Pathol. 204 2004 438 449
    • (2004) J. Pathol. , vol.204 , pp. 438-449
    • Cairns, N.J.1
  • 97
    • 6344280832 scopus 로고    scopus 로고
    • Emerging functions: Diseases and animal models reshape our view of the cytoskeleton
    • T.M. Magin Emerging functions: diseases and animal models reshape our view of the cytoskeleton Exp. Cell Res. 301 2004 91 102
    • (2004) Exp. Cell Res. , vol.301 , pp. 91-102
    • Magin, T.M.1
  • 98
    • 2342555610 scopus 로고    scopus 로고
    • Expression and localization of nuclear proteins in autosomal-dominant Emery-Dreifuss muscular dystrophy with LMNA R377H mutation
    • B. Reichart Expression and localization of nuclear proteins in autosomal-dominant Emery-Dreifuss muscular dystrophy with LMNA R377H mutation BMC Cell Biol. 5 2004 12
    • (2004) BMC Cell Biol. , vol.5 , pp. 12
    • Reichart, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.