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Volumn 351, Issue 20, 2004, Pages 2087-2100

Intermediate filament proteins and their associated diseases

Author keywords

[No Author keywords available]

Indexed keywords

INTERMEDIATE FILAMENT PROTEIN;

EID: 6344273968     PISSN: 00284793     EISSN: None     Source Type: Journal    
DOI: 10.1056/NEJMra040319     Document Type: Review
Times cited : (417)

References (108)
  • 1
    • 0033401358 scopus 로고    scopus 로고
    • The cytoskeleton of digestive epithelia in health and disease
    • Ku N-O, Zhou X, Toivola DM, Omary MB. The cytoskeleton of digestive epithelia in health and disease. Am J Physiol 1999;277:G1108-G1137.
    • (1999) Am J Physiol , vol.277
    • Ku, N.-O.1    Zhou, X.2    Toivola, D.M.3    Omary, M.B.4
  • 2
    • 0032559341 scopus 로고    scopus 로고
    • A structural scaffolding of intermediate filaments in health and disease
    • Fuchs E, Cleveland DW. A structural scaffolding of intermediate filaments in health and disease. Science 1998;279:514-9.
    • (1998) Science , vol.279 , pp. 514-519
    • Fuchs, E.1    Cleveland, D.W.2
  • 3
    • 0037282536 scopus 로고    scopus 로고
    • Functional complexity of intermediate filament cytoskeletons: From structure to assembly to gene ablation
    • Herrmann H, Hesse M, Reichenzeller M, Aebi U, Magin TM. Functional complexity of intermediate filament cytoskeletons: from structure to assembly to gene ablation. Int Rev Cytol 2003;223:83-175.
    • (2003) Int Rev Cytol , vol.223 , pp. 83-175
    • Herrmann, H.1    Hesse, M.2    Reichenzeller, M.3    Aebi, U.4    Magin, T.M.5
  • 4
    • 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
    • Hesse M, Magin TM, Weber K. 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 2001;114:2569-75.
    • (2001) J Cell Sci , vol.114 , pp. 2569-2575
    • Hesse, M.1    Magin, T.M.2    Weber, K.3
  • 6
    • 0036699522 scopus 로고    scopus 로고
    • Mutations in the gene encoding the lamin B receptor produce an altered nuclear morphology in granulocytes (Pelger-Huet anomaly)
    • Hoffmann K, Dreger CK, Olins AL, et al. Mutations in the gene encoding the lamin B receptor produce an altered nuclear morphology in granulocytes (Pelger-Huet anomaly). Nat Genet 2002;31:410-4.
    • (2002) Nat Genet , vol.31 , pp. 410-414
    • Hoffmann, K.1    Dreger, C.K.2    Olins, A.L.3
  • 7
    • 8344262483 scopus 로고    scopus 로고
    • National Institutes of Health Office of Rare Diseases
    • National Institutes of Health Office of Rare Diseases. (Accessed October 18, 2004, at http://rarediseases.info.nih.gov.)
  • 8
    • 0032432844 scopus 로고    scopus 로고
    • Molecular phytogeny of metazoan intermediate filament proteins
    • Erber A, Riemer D, Bovenschulte M, Weber K. Molecular phytogeny of metazoan intermediate filament proteins. J Mol Evol 1998;47:751-62.
    • (1998) J Mol Evol , vol.47 , pp. 751-762
    • Erber, A.1    Riemer, D.2    Bovenschulte, M.3    Weber, K.4
  • 9
    • 0346020436 scopus 로고    scopus 로고
    • The bacterial cytoskeleton: An intermediate filament-like function in cell shape
    • Ausmees N, Kuhn JR, Jacobs-Wagner C. The bacterial cytoskeleton: an intermediate filament-like function in cell shape. Cell 2003;115:705-13.
    • (2003) Cell , vol.115 , pp. 705-713
    • Ausmees, N.1    Kuhn, J.R.2    Jacobs-Wagner, C.3
  • 10
    • 0036468732 scopus 로고    scopus 로고
    • 'Hard' and 'soft' principles defining the structure, function and regulation of keratin intermediate filaments
    • Coulombe PA, Omary MB. 'Hard' and 'soft' principles defining the structure, function and regulation of keratin intermediate filaments. Curr Opin Cell Biol 2002;14:110-22.
    • (2002) Curr Opin Cell Biol , vol.14 , pp. 110-122
    • Coulombe, P.A.1    Omary, M.B.2
  • 11
    • 0032965997 scopus 로고    scopus 로고
    • Human keratin diseases: The in creasing spectrum of disease and subtlety of the phenotype-genotype correlation
    • Irvine AD, McLean WH. Human keratin diseases: the in creasing spectrum of disease and subtlety of the phenotype-genotype correlation. Br J Dermatol 1999;140:815-28.
    • (1999) Br J Dermatol , vol.140 , pp. 815-828
    • Irvine, A.D.1    McLean, W.H.2
  • 12
    • 0037407006 scopus 로고    scopus 로고
    • Phenotypes, genotypes and their contribution to understandingkeratin function
    • Porter RM, Lane EB. Phenotypes, genotypes and their contribution to understandingkeratin function. Trends Genet 2003;19:278-85.
    • (2003) Trends Genet , vol.19 , pp. 278-285
    • Porter, R.M.1    Lane, E.B.2
  • 14
    • 0348011603 scopus 로고    scopus 로고
    • Functions of intermediate filaments in neuronal development and disease
    • Lariviere RC, Julien JP. Functions of intermediate filaments in neuronal development and disease. J Neurobiol 2004;58:131-48.
    • (2004) J Neurobiol , vol.58 , pp. 131-148
    • Lariviere, R.C.1    Julien, J.P.2
  • 15
    • 85047692354 scopus 로고    scopus 로고
    • How do mutations in lamins A and C cause disease?
    • Worman HJ, Courvalin JC. How do mutations in lamins A and C cause disease? J Clin Invest 2004;113:349-51.
    • (2004) J Clin Invest , vol.113 , pp. 349-351
    • Worman, H.J.1    Courvalin, J.C.2
  • 16
    • 0037390202 scopus 로고    scopus 로고
    • Neurofilaments and neurological disease
    • Al-Chalabi A, Miller CCJ. Neurofilaments and neurological disease. Bioessays 2003;25:346-55.
    • (2003) Bioessays , vol.25 , pp. 346-355
    • Al-Chalabi, A.1    Miller, C.C.J.2
  • 17
    • 0141681225 scopus 로고    scopus 로고
    • The strange case of the "lumper" lamin A/C gene and human premature aging
    • Novelli G, D'Apice MR, The strange case of the "lumper" lamin A/C gene and human premature aging. Trends Mol Med 2003;9:370-5.
    • (2003) Trends Mol Med , vol.9 , pp. 370-375
    • Novelli, G.1    D'Apice, M.R.2
  • 18
    • 0024817731 scopus 로고
    • The CaaX motif of lamin A functions in conjunction with the nuclear localization signal to target assembly to the nuclear envelope
    • Holtz D, Tanaka RA, Hartwig J, McKeon F. The CaaX motif of lamin A functions in conjunction with the nuclear localization signal to target assembly to the nuclear envelope. Cell 1989;59:969-77.
    • (1989) Cell , vol.59 , pp. 969-977
    • Holtz, D.1    Tanaka, R.A.2    Hartwig, J.3    McKeon, F.4
  • 19
    • 0001481064 scopus 로고    scopus 로고
    • Dynamic property of intermediate filaments: Regulation by phosphorylation
    • Inagaki M, Matsuoka Y, Tsujimura K, et al. Dynamic property of intermediate filaments: regulation by phosphorylation. Bioessays 1996;18:481-7.
    • (1996) Bioessays , vol.18 , pp. 481-487
    • Inagaki, M.1    Matsuoka, Y.2    Tsujimura, K.3
  • 20
    • 0034433275 scopus 로고    scopus 로고
    • Neurofilament protein synthesis and phosphorylation
    • Grant P, Pant HC. Neurofilament protein synthesis and phosphorylation. J Neurocytol 2000;29:843-72.
    • (2000) J Neurocytol , vol.29 , pp. 843-872
    • Grant, P.1    Pant, H.C.2
  • 21
    • 0032478181 scopus 로고    scopus 로고
    • A highly conserved lysine residue on the head domain of type II keratins is essential for the attachment of keratin intermediate filaments to the cornified cell envelope through isopeptide crosslinking by transglutaminases
    • Candi E, Tarcsa E, Digiovanna JJ, et al. A highly conserved lysine residue on the head domain of type II keratins is essential for the attachment of keratin intermediate filaments to the cornified cell envelope through isopeptide crosslinking by transglutaminases. Proc Natl Acad Sci U S A 1998;95:2067-72.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 2067-2072
    • Candi, E.1    Tarcsa, E.2    Digiovanna, J.J.3
  • 22
    • 0029786683 scopus 로고    scopus 로고
    • Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H
    • Dong DL, Xu ZS, Hart GW, Cleveland DW. Cytoplasmic O-GlcNAc modification of the head domain and the KSP repeat motif of the neurofilament protein neurofilament-H. J Biol Chem 1996;271:20845-52.
    • (1996) J Biol Chem , vol.271 , pp. 20845-20852
    • Dong, D.L.1    Xu, Z.S.2    Hart, G.W.3    Cleveland, D.W.4
  • 23
    • 0344393065 scopus 로고    scopus 로고
    • The dynamic and motile properties of intermediate filaments
    • Helfend BT, Chang L, Goldman RD. The dynamic and motile properties of intermediate filaments. Annu Rev Cell Dev Biol 2003;19:445-67.
    • (2003) Annu Rev Cell Dev Biol , vol.19 , pp. 445-467
    • Helfend, B.T.1    Chang, L.2    Goldman, R.D.3
  • 24
    • 0036097410 scopus 로고    scopus 로고
    • Apoptosis and keratin intermediate filaments
    • Oshima RG. Apoptosis and keratin intermediate filaments. Cell Death Differ 2002;9:486-92.
    • (2002) Cell Death Differ , vol.9 , pp. 486-492
    • Oshima, R.G.1
  • 25
    • 0037470243 scopus 로고    scopus 로고
    • Caspase proteolysis of desmin produces a dominant-negative inhibitor of intermediate filaments and promotes apoptosis
    • Chen F, Chang R, Trivedi M, Capetanaki Y, Cryns VL. Caspase proteolysis of desmin produces a dominant-negative inhibitor of intermediate filaments and promotes apoptosis. J Biol Chem 2003;278:6848-53.
    • (2003) J Biol Chem , vol.278 , pp. 6848-6853
    • Chen, F.1    Chang, R.2    Trivedi, M.3    Capetanaki, Y.4    Cryns, V.L.5
  • 26
    • 0034568948 scopus 로고    scopus 로고
    • Are desmosomes more than tethers for intermediate filaments?
    • Green KJ, Gaudry CA. Are desmosomes more than tethers for intermediate filaments? Nat Rev Mol Cell Biol 2000;1:208-16.
    • (2000) Nat Rev Mol Cell Biol , vol.1 , pp. 208-216
    • Green, K.J.1    Gaudry, C.A.2
  • 27
    • 3042822399 scopus 로고    scopus 로고
    • Plakins: Goliaths that link cell junctions and the cytoskeleton
    • Jefferson JJ, Leung CL, Liem RK. Plakins: goliaths that link cell junctions and the cytoskeleton. Nat Rev Mol Cell Biol 2004;5:542-53.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 542-553
    • Jefferson, J.J.1    Leung, C.L.2    Liem, R.K.3
  • 28
    • 1842584782 scopus 로고    scopus 로고
    • Proteins that bind A-type lamins: Integrating isolated clues
    • Zasttow MS, Vlcek S, Wilson KL. Proteins that bind A-type lamins: integrating isolated clues. J Cell Sci 2004;117:979-87.
    • (2004) J Cell Sci , vol.117 , pp. 979-987
    • Zasttow, M.S.1    Vlcek, S.2    Wilson, K.L.3
  • 29
    • 4143134431 scopus 로고    scopus 로고
    • Cytoplasmic intermediate filaments revealed as dynamic and multipurpose scaffolds
    • Coulombe PA, Wong P. Cytoplasmic intermediate filaments revealed as dynamic and multipurpose scaffolds. Nat Cell Biol 2004;6:699-706.
    • (2004) Nat Cell Biol , vol.6 , pp. 699-706
    • Coulombe, P.A.1    Wong, P.2
  • 30
    • 0037386189 scopus 로고    scopus 로고
    • Mallory body formation in primary biliary cirrhosis is associated with increased amounts and abnormal phosphorylation and ubiquitination of cytokeratins
    • Fickert P, Trauner M, Fuchsbichler A, Stumptner C, Zatloukal K, Denk H. Mallory body formation in primary biliary cirrhosis is associated with increased amounts and abnormal phosphorylation and ubiquitination of cytokeratins. J Hepatol 2003;38:387-94.
    • (2003) J Hepatol , vol.38 , pp. 387-394
    • Fickert, P.1    Trauner, M.2    Fuchsbichler, A.3    Stumptner, C.4    Zatloukal, K.5    Denk, H.6
  • 32
    • 0242298585 scopus 로고    scopus 로고
    • Loss of keratin 6 (K6) proteins reveals a function for intermediate filaments during wound repair
    • Wong P, Coulombe PA. Loss of keratin 6 (K6) proteins reveals a function for intermediate filaments during wound repair. J Cell Biol 2003;163:327-37.
    • (2003) J Cell Biol , vol.163 , pp. 327-337
    • Wong, P.1    Coulombe, P.A.2
  • 33
    • 2342434472 scopus 로고    scopus 로고
    • Organ-specific stress induces mouse pancreatic keratin overexpression in association with NF-kB activation
    • Zhong B, Zhou Q, Toivola DM, Tao G-Z, Resurreccion EZ, Omary MB. Organ-specific stress induces mouse pancreatic keratin overexpression in association with NF-kB activation. J Cell Sci 2004;117:1709-19.
    • (2004) J Cell Sci , vol.117 , pp. 1709-1719
    • Zhong, B.1    Zhou, Q.2    Toivola, D.M.3    Tao, G.-Z.4    Resurreccion, E.Z.5    Omary, M.B.6
  • 35
    • 0037407386 scopus 로고    scopus 로고
    • Congenital myopathies at their molecular dawning
    • Goebel HH. Congenital myopathies at their molecular dawning. Muscle Nerve 2003;27:527-48.
    • (2003) Muscle Nerve , vol.27 , pp. 527-548
    • Goebel, H.H.1
  • 36
    • 0037609535 scopus 로고    scopus 로고
    • Keratin 8 and 18 mutations are risk factors for developing liver disease of multiple etiologies
    • Ku N-O, Darling JM, Krams SM, et al. Keratin 8 and 18 mutations are risk factors for developing liver disease of multiple etiologies. Proc Natl Acad Sci U S A 2003;100:6063-8.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 6063-6068
    • Ku, N.-O.1    Darling, J.M.2    Krams, S.M.3
  • 37
    • 0037847551 scopus 로고    scopus 로고
    • Keratin mutation in transgenic mice predisposes to FAS but not TNF-induced apoptosis and massive liver injury
    • Ku N-O, Soetikno RM, Omary MB. Keratin mutation in transgenic mice predisposes to FAS but not TNF-induced apoptosis and massive liver injury. Hepatology 2003;37:1006-14.
    • (2003) Hepatology , vol.37 , pp. 1006-1014
    • Ku, N.-O.1    Soetikno, R.M.2    Omary, M.B.3
  • 38
    • 0025861772 scopus 로고
    • Point mutations in human keratin 14 genes of epidermolysis bullosa simplex patients: Genetic and functional analyses
    • Coulombe PA, Hutton ME, Letai A, Hebert A, Palier AS, Fuchs E. Point mutations in human keratin 14 genes of epidermolysis bullosa simplex patients: genetic and functional analyses. Cell 1991;66:1301-11.
    • (1991) Cell , vol.66 , pp. 1301-1311
    • Coulombe, P.A.1    Hutton, M.E.2    Letai, A.3    Hebert, A.4    Palier, A.S.5    Fuchs, E.6
  • 39
    • 3543009577 scopus 로고    scopus 로고
    • Keratins modulate c-Flip/exttacellular signal-regulated kinase 1 and 2 antiapoptotic signaling in simple epithelial cells
    • Gilbert S, Loranger A, Marceau N. Keratins modulate c-Flip/exttacellular signal-regulated kinase 1 and 2 antiapoptotic signaling in simple epithelial cells. Mol Cell Biol 2004;24:7072-81.
    • (2004) Mol Cell Biol , vol.24 , pp. 7072-7081
    • Gilbert, S.1    Loranger, A.2    Marceau, N.3
  • 40
    • 3943102116 scopus 로고    scopus 로고
    • Unraveling the mechanisms involved in motor neuron degeneration in ALS
    • Bruijn LI, Miller TM, Cleveland DW. Unraveling the mechanisms involved in motor neuron degeneration in ALS. Annu Rev Neurosci 2004;27:723-49.
    • (2004) Annu Rev Neurosci , vol.27 , pp. 723-749
    • Bruijn, L.I.1    Miller, T.M.2    Cleveland, D.W.3
  • 41
    • 0026345962 scopus 로고
    • Epidermolysis bullosa simplex: Evidence in two families for keratin gene abnormalities
    • Bonifas JM, Rothman AL, Epstein EH Jr. Epidermolysis bullosa simplex: evidence in two families for keratin gene abnormalities. Science 1991;254:1202-5.
    • (1991) Science , vol.254 , pp. 1202-1205
    • Bonifas, J.M.1    Rothman, A.L.2    Epstein Jr., E.H.3
  • 42
    • 0032233043 scopus 로고    scopus 로고
    • Cytokeratins as markers of differentiation in the diagnosis of epithelial tumors
    • Moll R. Cytokeratins as markers of differentiation in the diagnosis of epithelial tumors. Subcell Biochem 1998;31:205-62.
    • (1998) Subcell Biochem , vol.31 , pp. 205-262
    • Moll, R.1
  • 43
    • 12144290503 scopus 로고    scopus 로고
    • Differentiation between cell death modes using measurements of different soluble forms of extracellular cytokeratin 18
    • Kramer G, Erdal H, Mertens HJ, et al. Differentiation between cell death modes using measurements of different soluble forms of extracellular cytokeratin 18. Cancer Res 2004;64:1751-6.
    • (2004) Cancer Res , vol.64 , pp. 1751-1756
    • Kramer, G.1    Erdal, H.2    Mertens, H.J.3
  • 44
    • 0036264261 scopus 로고    scopus 로고
    • Multiparameter flow cytometry as a tool for the detection of micrometastatic tumour cells in the sentinel lymph node procedure of patients with breast cancer
    • Leers MP, Schoffelen RH, Hoop JG, et al. Multiparameter flow cytometry as a tool for the detection of micrometastatic tumour cells in the sentinel lymph node procedure of patients with breast cancer. J Clin Pathol 2002;55:359-66.
    • (2002) J Clin Pathol , vol.55 , pp. 359-366
    • Leers, M.P.1    Schoffelen, R.H.2    Hoop, J.G.3
  • 45
    • 0020031469 scopus 로고
    • Epidermolysis bullosa herpetiformis Dowling-Meara: Report of a case and pathomorphogenesis
    • Anton-Lamprecht I, Schnyder UW. Epidermolysis bullosa herpetiformis Dowling-Meara: report of a case and pathomorphogenesis. Dermatologica 1982;164:221-35.
    • (1982) Dermatologica , vol.164 , pp. 221-235
    • Anton-Lamprecht, I.1    Schnyder, U.W.2
  • 46
    • 0023545331 scopus 로고
    • The expression of mutant epidermal keratin cDNAs transfected in simple epithelial and squamous cell carcinoma lines
    • Albers K, Fuchs E. The expression of mutant epidermal keratin cDNAs transfected in simple epithelial and squamous cell carcinoma lines. J Cell Biol 1987;105:791-806.
    • (1987) J Cell Biol , vol.105 , pp. 791-806
    • Albers, K.1    Fuchs, E.2
  • 47
    • 0025976155 scopus 로고
    • Mutant keratin expression in transgenic mice causes marked abnormalities resembling a human genetic skin disease
    • Vassar R, Coulombe PA, Degenstein L, Albers K, Fuchs E. Mutant keratin expression in transgenic mice causes marked abnormalities resembling a human genetic skin disease. Cell 1991;64:365-80.
    • (1991) Cell , vol.64 , pp. 365-380
    • Vassar, R.1    Coulombe, P.A.2    Degenstein, L.3    Albers, K.4    Fuchs, E.5
  • 48
    • 0026545645 scopus 로고
    • A mutation in the conserved helix termination peptide of keratin 5 in hereditary skin blistering
    • Lane EB, Rugg EL, Navsaria H, et al. A mutation in the conserved helix termination peptide of keratin 5 in hereditary skin blistering. Nature 1992;356:244-6.
    • (1992) Nature , vol.356 , pp. 244-246
    • Lane, E.B.1    Rugg, E.L.2    Navsaria, H.3
  • 49
    • 0026699760 scopus 로고
    • The genetic basis of epidermolytic hyperkeratosis: A disorder of differentiation-specific epidermal keratin genes
    • Cheng J, Syder AJ, Yu Q-C, Letai A, Paller AS, Fuchs E. The genetic basis of epidermolytic hyperkeratosis: a disorder of differentiation-specific epidermal keratin genes. Cell 1992;70:811-9.
    • (1992) Cell , vol.70 , pp. 811-819
    • Cheng, J.1    Syder, A.J.2    Yu, Q.-C.3    Letai, A.4    Paller, A.S.5    Fuchs, E.6
  • 50
    • 0026612429 scopus 로고
    • A leucine-proline mutation in the H1 subdomain of keratin 1 causes epidermolytic hyperkeratosis
    • Chipev CC, Korge BP, Markova N, et al. A leucine-proline mutation in the H1 subdomain of keratin 1 causes epidermolytic hyperkeratosis. Cell 1992;70:821-8.
    • (1992) Cell , vol.70 , pp. 821-828
    • Chipev, C.C.1    Korge, B.P.2    Markova, N.3
  • 53
    • 2942576061 scopus 로고    scopus 로고
    • Human keratin 8 mutations that disturb filament assembly observed in inflammatory bowel disease patients
    • Owens DW, Wilson NJ, Hill AJM, et al. Human keratin 8 mutations that disturb filament assembly observed in inflammatory bowel disease patients. J Cell Sci 2004;117:1989-99.
    • (2004) J Cell Sci , vol.117 , pp. 1989-1999
    • Owens, D.W.1    Wilson, N.J.2    Hill, A.J.M.3
  • 54
    • 0142093584 scopus 로고    scopus 로고
    • Association of keratin 8 gene mutation with chronic pancreatitis
    • Cavestro GM, Frulloni L, Nouvenne A, et al. Association of keratin 8 gene mutation with chronic pancreatitis. Dig Liver Dis 2003;35:416-20.
    • (2003) Dig Liver Dis , vol.35 , pp. 416-420
    • Cavestro, G.M.1    Frulloni, L.2    Nouvenne, A.3
  • 55
    • 0035860762 scopus 로고    scopus 로고
    • The catalog of human hair keratins. II. Expression of the six type II members in the hair follicle and the combined catalog of human type I and II keratins
    • Langbein L, Rogers MA, Winter H, Praetzel S, Schweizer J. The catalog of human hair keratins. II. Expression of the six type II members in the hair follicle and the combined catalog of human type I and II keratins. J Biol Chem 2001;276:35123-32.
    • (2001) J Biol Chem , vol.276 , pp. 35123-35132
    • Langbein, L.1    Rogers, M.A.2    Winter, H.3    Praetzel, S.4    Schweizer, J.5
  • 56
    • 0030747138 scopus 로고    scopus 로고
    • Mutations in the hair cortex keratin hHb6 cause the inherited hair disease monilethrix
    • Winter H, Rogers MA, Langbein L, et al. Mutations in the hair cortex keratin hHb6 cause the inherited hair disease monilethrix. Nat Genet 1997;16:372-4.
    • (1997) Nat Genet , vol.16 , pp. 372-374
    • Winter, H.1    Rogers, M.A.2    Langbein, L.3
  • 57
    • 0036220262 scopus 로고    scopus 로고
    • Is the loose anagen hair syndrome a keratin disorder? A clinical and molecular study
    • Chapalain V, Winter H, Langbein L, et al. Is the loose anagen hair syndrome a keratin disorder? A clinical and molecular study. Arch Dermatol 2002;138:501-6.
    • (2002) Arch Dermatol , vol.138 , pp. 501-506
    • Chapalain, V.1    Winter, H.2    Langbein, L.3
  • 58
    • 11144357354 scopus 로고    scopus 로고
    • An unusual Alal2Thr polymorphism in the 1Aα-helical segment of the companion layer-specific keratin K6hf: Evidence for a risk factor in the etiology of the common hair disorder pseudofolliculitis barbae
    • Winter H, Schissel D, Parry DA, et al. An unusual Alal2Thr polymorphism in the 1Aα-helical segment of the companion layer-specific keratin K6hf: evidence for a risk factor in the etiology of the common hair disorder pseudofolliculitis barbae. J Invest Dermatol 2004;122:652-7.
    • (2004) J Invest Dermatol , vol.122 , pp. 652-657
    • Winter, H.1    Schissel, D.2    Parry, D.A.3
  • 59
    • 0038669889 scopus 로고    scopus 로고
    • A dysfunctional desmin mutation in a patient with severe generalized myopathy
    • Munoz-Marmol AM, Strasser G, Isamat M, et al. A dysfunctional desmin mutation in a patient with severe generalized myopathy. Proc Natl Acad Sci U S A 1998;95:11312-7.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 11312-11317
    • Munoz-Marmol, A.M.1    Strasser, G.2    Isamat, M.3
  • 61
    • 0034765821 scopus 로고    scopus 로고
    • Alpha-B crystallin gene (CRYAB) mutation causes dominant congenital posterior polar cataract in humans
    • Berry V, Francis P, Reddy MA, et al. Alpha-B crystallin gene (CRYAB) mutation causes dominant congenital posterior polar cataract in humans. Am J Hum Genet 2001;69:1141-5.
    • (2001) Am J Hum Genet , vol.69 , pp. 1141-1145
    • Berry, V.1    Francis, P.2    Reddy, M.A.3
  • 62
    • 0033942142 scopus 로고    scopus 로고
    • Autosomal-dominant congenital cataract associated with a deletion mutation in the human beaded filament protein gene BFSP2
    • Jakobs PM, Hess JF, FitzGerald PG, Kramer P, Weleber RG, Litt M. Autosomal-dominant congenital cataract associated with a deletion mutation in the human beaded filament protein gene BFSP2. Am J Hum Genet 2000;66:1432-6.
    • (2000) Am J Hum Genet , vol.66 , pp. 1432-1436
    • Jakobs, P.M.1    Hess, J.F.2    FitzGerald, P.G.3    Kramer, P.4    Weleber, R.G.5    Litt, M.6
  • 63
    • 0033942141 scopus 로고    scopus 로고
    • A juvenile-onset, progressive cataract locus on chromosome 3q21-q22 is associated with a missense mutation in the beaded filament structural protein-2
    • Conley YP, Erturk D, Keverline A, et al. A juvenile-onset, progressive cataract locus on chromosome 3q21-q22 is associated with a missense mutation in the beaded filament structural protein-2. Am J Hum Genet 2000;66:1426-31.
    • (2000) Am J Hum Genet , vol.66 , pp. 1426-1431
    • Conley, Y.P.1    Erturk, D.2    Keverline, A.3
  • 65
    • 0033911099 scopus 로고    scopus 로고
    • A new variant of Charcot-Marie-Tooth disease type 2 is probably the result of a mutation in the neurofilament-light gene
    • Mersiyanova IV, Perepelov AV, Polyakov AV, et al. A new variant of Charcot-Marie-Tooth disease type 2 is probably the result of a mutation in the neurofilament-light gene. Am J Hum Genet 2000;67:37-46.
    • (2000) Am J Hum Genet , vol.67 , pp. 37-46
    • Mersiyanova, I.V.1    Perepelov, A.V.2    Polyakov, A.V.3
  • 66
    • 8544222694 scopus 로고    scopus 로고
    • A frameshift deletion in peripherin gene associated with amyotrophic lateral sclerosis
    • in press
    • Gros-Louis F, Lariviere R, Gowing G, et al. A frameshift deletion in peripherin gene associated with amyotrophic lateral sclerosis. J Biol Chem (in press).
    • J Biol Chem
    • Gros-Louis, F.1    Lariviere, R.2    Gowing, G.3
  • 67
    • 0033050072 scopus 로고    scopus 로고
    • Hereditary skin diseases of hemidesmosomes
    • Jonkman MF. Hereditary skin diseases of hemidesmosomes. J Dermatol Sci 1999;20:103-21.
    • (1999) J Dermatol Sci , vol.20 , pp. 103-121
    • Jonkman, M.F.1
  • 68
    • 0031663054 scopus 로고    scopus 로고
    • Role of plectin in cytoskeleton organization and dynamics
    • Wiche G. Role of plectin in cytoskeleton organization and dynamics. J Cell Sci 1998;111:2477-86.
    • (1998) J Cell Sci , vol.111 , pp. 2477-2486
    • Wiche, G.1
  • 69
    • 5444267945 scopus 로고    scopus 로고
    • Phenotypic analysis of neurofilament light gene mutations linked to Charcot-Marie-Tooth disease in cell culture models
    • Perez-Olle R, Jones ST, Liem RK. Phenotypic analysis of neurofilament light gene mutations linked to Charcot-Marie-Tooth disease in cell culture models. Hum Mol Genet 2004;13:2207-20.
    • (2004) Hum Mol Genet , vol.13 , pp. 2207-2220
    • Perez-Olle, R.1    Jones, S.T.2    Liem, R.K.3
  • 71
    • 10344262023 scopus 로고    scopus 로고
    • Effects of keratin 14 ablation on the clinical and cellular phenotype in a kindred with recessive epidermolysis bullosa simplex
    • Jonkman MF, Heeres K, Pas HH, et al. Effects of keratin 14 ablation on the clinical and cellular phenotype in a kindred with recessive epidermolysis bullosa simplex. J Invest Dermatol 1996;107:764-9.
    • (1996) J Invest Dermatol , vol.107 , pp. 764-769
    • Jonkman, M.F.1    Heeres, K.2    Pas, H.H.3
  • 73
    • 0042190215 scopus 로고    scopus 로고
    • Sphingosylphosphorylcholine regulates keratin network architecture and visco-elastic properties of human cancer cells
    • Beil M, Micoulet A, von Wiehert G, et al. Sphingosylphosphorylcholine regulates keratin network architecture and visco-elastic properties of human cancer cells. Nat Cell Biol 2003;5:803-11.
    • (2003) Nat Cell Biol , vol.5 , pp. 803-811
    • Beil, M.1    Micoulet, A.2    Von Wiehert, G.3
  • 74
    • 0035022929 scopus 로고    scopus 로고
    • A 'hot-spot' mutation alters the mechanical properties of keratin filament networks
    • Ma L, Yamada S, Wirtz D, Coulombe PA. A 'hot-spot' mutation alters the mechanical properties of keratin filament networks. Nat Cell Biol 2001;3:503-6.
    • (2001) Nat Cell Biol , vol.3 , pp. 503-506
    • Ma, L.1    Yamada, S.2    Wirtz, D.3    Coulombe, P.A.4
  • 75
    • 1542283819 scopus 로고    scopus 로고
    • Epidermolysis bullosa simplex-type mutations alter the dynamics of the keratin cytoskeleton and reveal a contribution of actin to the transport of keratin subunits
    • Werner NS, Windoffer R, Strnad P, Grund C, Leube RE, Magin TM. Epidermolysis bullosa simplex-type mutations alter the dynamics of the keratin cytoskeleton and reveal a contribution of actin to the transport of keratin subunits. Mol Biol Cell 2004;15:990-1002.
    • (2004) Mol Biol Cell , vol.15 , pp. 990-1002
    • Werner, N.S.1    Windoffer, R.2    Strnad, P.3    Grund, C.4    Leube, R.E.5    Magin, T.M.6
  • 76
    • 0029810901 scopus 로고    scopus 로고
    • The genetic basis of epidermolysis bullosa simplex with mottled pigmentation
    • Uttam J, Hutton E, Coulombe PA, et al. The genetic basis of epidermolysis bullosa simplex with mottled pigmentation. Proc Natl Acad Sci U S A 1996;93:9079-84.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 9079-9084
    • Uttam, J.1    Hutton, E.2    Coulombe, P.A.3
  • 77
    • 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
    • Ameen NA, Figueroa Y, Salas PJ. 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 2001;114:563-75.
    • (2001) J Cell Sci , vol.114 , pp. 563-575
    • Ameen, N.A.1    Figueroa, Y.2    Salas, P.J.3
  • 78
    • 1642348652 scopus 로고    scopus 로고
    • Keratins modulate colonocyte electrolyte transport via protein mistargeting
    • Toivola DM, Krishnan S, Binder HJ, Singh SK, Omary MB. Keratins modulate colonocyte electrolyte transport via protein mistargeting. J Cell Biol 2004;164:911-21.
    • (2004) J Cell Biol , vol.164 , pp. 911-921
    • Toivola, D.M.1    Krishnan, S.2    Binder, H.J.3    Singh, S.K.4    Omary, M.B.5
  • 79
    • 0034683573 scopus 로고    scopus 로고
    • Desmin cytoskeleton linked to muscle mitochondrial distribution and respiratory function
    • Milner DJ, Mavroidis M, Weisleder N, Capetanald Y. Desmin cytoskeleton linked to muscle mitochondrial distribution and respiratory function. J Cell Biol 2000;150:1283-98.
    • (2000) J Cell Biol , vol.150 , pp. 1283-1298
    • Milner, D.J.1    Mavroidis, M.2    Weisleder, N.3    Capetanald, Y.4
  • 80
    • 0037112998 scopus 로고    scopus 로고
    • Keratin mutations of epidermolysis bullosa simplex alter the kinetics of stress response to osmotic shock
    • D'Alessandro M, Russell D, Morley SM, Davies AM, Lane EB. Keratin mutations of epidermolysis bullosa simplex alter the kinetics of stress response to osmotic shock. J Cell Sci 2002;115:4341-51.
    • (2002) J Cell Sci , vol.115 , pp. 4341-4351
    • D'Alessandro, M.1    Russell, D.2    Morley, S.M.3    Davies, A.M.4    Lane, E.B.5
  • 81
    • 0028607055 scopus 로고
    • Colorectal hyperplasia and inflammation in keratin 8-deficient FVB/N mice
    • Baribault H, Penner J, Iozzo RV, Wilson-Heiner M. Colorectal hyperplasia and inflammation in keratin 8-deficient FVB/N mice. Genes Dev 1994;8:2964-73.
    • (1994) Genes Dev , vol.8 , pp. 2964-2973
    • Baribault, H.1    Penner, J.2    Iozzo, R.V.3    Wilson-Heiner, M.4
  • 82
    • 0037183491 scopus 로고    scopus 로고
    • Lamin A/C mutations with lipodystrophy, cardiac abnormalities, and muscular dystrophy
    • van der Kooi AJ, Bonne G, Eymard B, et al. Lamin A/C mutations with lipodystrophy, cardiac abnormalities, and muscular dystrophy. Neurology 2002;59:620-3.
    • (2002) Neurology , vol.59 , pp. 620-623
    • Van Der Kooi, A.J.1    Bonne, G.2    Eymard, B.3
  • 83
    • 0032977685 scopus 로고    scopus 로고
    • Mutations in the gene encoding lamin A/C cause autosomal dominant Emery-Dreifuss muscular dystrophy
    • Bonne G, Di Barletta MR, Varnous S, et al. Mutations in the gene encoding lamin A/C cause autosomal dominant Emery-Dreifuss muscular dystrophy. Nat Genet 1999;21:285-8.
    • (1999) Nat Genet , vol.21 , pp. 285-288
    • Bonne, G.1    Di Barletta, M.R.2    Varnous, S.3
  • 84
    • 0033518282 scopus 로고    scopus 로고
    • Missense mutations in the rod domain of the lamin A/C gene as causes of dilated cardiomyopathy and conduction-system disease
    • Fatkin D, MacRae C, Sasaki T, et al. Missense mutations in the rod domain of the lamin A/C gene as causes of dilated cardiomyopathy and conduction-system disease. N Engl J Med 1999;341:1715-24.
    • (1999) N Engl J Med , vol.341 , pp. 1715-1724
    • Fatkin, D.1    MacRae, C.2    Sasaki, T.3
  • 85
    • 0037630089 scopus 로고    scopus 로고
    • Lamin mutations come of age
    • Hegele RA. Lamin mutations come of age. Nat Med 2003;9:644-5.
    • (2003) Nat Med , vol.9 , pp. 644-645
    • Hegele, R.A.1
  • 86
    • 0037673950 scopus 로고    scopus 로고
    • Recurrent de novo point mutations in lamin A cause Hutchinson-Gilford progeria syndrome
    • Eriksson M, Brown WT, Gordon LB, et al. Recurrent de novo point mutations in lamin A cause Hutchinson-Gilford progeria syndrome. Nature 2003;423:293-8.
    • (2003) Nature , vol.423 , pp. 293-298
    • Eriksson, M.1    Brown, W.T.2    Gordon, L.B.3
  • 87
    • 10744229294 scopus 로고    scopus 로고
    • Lamin A truncation in Hutchinson-Gilford progeria
    • De Sandre-Giovannoli A, Bernard R, Cau P, et al. Lamin A truncation in Hutchinson-Gilford progeria. Science 2003;300:2055.
    • (2003) Science , vol.300 , pp. 2055
    • De Sandre-Giovannoli, A.1    Bernard, R.2    Cau, P.3
  • 89
    • 12244293441 scopus 로고    scopus 로고
    • Mandibuloacral dysplasia is caused by a mutation in LMNA-encoding lamin A/C
    • Novelli G, Muchir A, Sangiuolo F, et al. Mandibuloacral dysplasia is caused by a mutation in LMNA-encoding lamin A/C. Am J Hum Genet 2002;71:426-31.
    • (2002) Am J Hum Genet , vol.71 , pp. 426-431
    • Novelli, G.1    Muchir, A.2    Sangiuolo, F.3
  • 90
    • 0033615969 scopus 로고    scopus 로고
    • Loss of A-type lamin expression compromises nuclear envelope integrity leading to muscular dystrophy
    • Sullivan T, Escalante-Akalde D, Bhatt H, et al. Loss of A-type lamin expression compromises nuclear envelope integrity leading to muscular dystrophy. J Cell Biol 1999;147:913-20.
    • (1999) J Cell Biol , vol.147 , pp. 913-920
    • Sullivan, T.1    Escalante-Akalde, D.2    Bhatt, H.3
  • 91
    • 0036178210 scopus 로고    scopus 로고
    • Homozygous defects in LMNA, encoding lamin A/C nuclear-envelope proteins, cause autosomal recessive axonal neuropathy in human (Charcot-Marie-Tooth disorder type 2) and mouse
    • De Sandre-Giovannoli A, Chaouch M, Kozlov S, et al. Homozygous defects in LMNA, encoding lamin A/C nuclear-envelope proteins, cause autosomal recessive axonal neuropathy in human (Charcot-Marie-Tooth disorder type 2) and mouse. Am J Hum Genet 2002;70:726-36. [Erratum, Am J Hum Genet 2002;70:1075.]
    • (2002) Am J Hum Genet , vol.70 , pp. 726-736
    • De Sandre-Giovannoli, A.1    Chaouch, M.2    Kozlov, S.3
  • 92
    • 0036207807 scopus 로고    scopus 로고
    • Erratum
    • De Sandre-Giovannoli A, Chaouch M, Kozlov S, et al. Homozygous defects in LMNA, encoding lamin A/C nuclear-envelope proteins, cause autosomal recessive axonal neuropathy in human (Charcot-Marie-Tooth disorder type 2) and mouse. Am J Hum Genet 2002;70:726-36. [Erratum, Am J Hum Genet 2002;70:1075.]
    • (2002) Am J Hum Genet , vol.70 , pp. 1075
  • 94
    • 1542510700 scopus 로고    scopus 로고
    • Acquired and inherited lipodystrophies
    • Garg A. Acquired and inherited lipodystrophies. N Engl J Med 2004;350:1220-34.
    • (2004) N Engl J Med , vol.350 , pp. 1220-1234
    • Garg, A.1
  • 95
    • 0036843975 scopus 로고    scopus 로고
    • Lamins: Building blocks or regulators of gene expression?
    • Hutchison CJ. Lamins: building blocks or regulators of gene expression? Nat Rev Mol Cell Biol 2002;3:848-58.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 848-858
    • Hutchison, C.J.1
  • 96
    • 0029100609 scopus 로고
    • A chromatin binding site in the tail domain of nuclear lamins that interacts with core histones
    • Taniura H, Glass C, Gerace L. A chromatin binding site in the tail domain of nuclear lamins that interacts with core histones. J Cell Biol 1995;131:33-44.
    • (1995) J Cell Biol , vol.131 , pp. 33-44
    • Taniura, H.1    Glass, C.2    Gerace, L.3
  • 97
    • 0036537888 scopus 로고    scopus 로고
    • A novel interaction between lamin A and SREBP1: Implications for partial lipodystrophy and other laminopathies
    • Lloyd DJ, Trembath RC, Shackleton S. A novel interaction between lamin A and SREBP1: implications for partial lipodystrophy and other laminopathies. Hum Mol Genet 2002;11:769-77.
    • (2002) Hum Mol Genet , vol.11 , pp. 769-777
    • Lloyd, D.J.1    Trembath, R.C.2    Shackleton, S.3
  • 98
    • 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
    • Muchk A, van Engelen BG, Lammens M, et al. Nuclear envelope alterations in fibroblasts from LGMD1B patients carrying nonsense Y259X heterozygous or homozygous mutation in lamin A/C gene. Exp Cell Res 2003;291:352-62.
    • (2003) Exp Cell Res , vol.291 , pp. 352-362
    • Muchk, A.1    Van Engelen, B.G.2    Lammens, M.3
  • 99
    • 0036856008 scopus 로고    scopus 로고
    • Translational control in the endoplasmic reticulum stress response
    • Ron D. Translational control in the endoplasmic reticulum stress response. J Clin Invest 2002;110:1383-8.
    • (2002) J Clin Invest , vol.110 , pp. 1383-1388
    • Ron, D.1
  • 100
    • 18444382032 scopus 로고    scopus 로고
    • The Ig-like structure of the C-terminal domain of lamin A/C, mutated in muscular dystrophies, cardiomyopathy, and partial lipodystrophy
    • Krimm I, Ostlund C, Gilquin B, et al. The Ig-like structure of the C-terminal domain of lamin A/C, mutated in muscular dystrophies, cardiomyopathy, and partial lipodystrophy. Structure (Camb) 2002;10:811-23.
    • (2002) Structure (Camb) , vol.10 , pp. 811-823
    • Krimm, I.1    Ostlund, C.2    Gilquin, B.3
  • 102
    • 0042427279 scopus 로고    scopus 로고
    • Probing the fetal genome: Progress in non-invasive prenatal diagnosis
    • Uitto J, Pfendner E, Jackson LG. Probing the fetal genome: progress in non-invasive prenatal diagnosis. Trends Mol Med 2003;9:339-43.
    • (2003) Trends Mol Med , vol.9 , pp. 339-343
    • Uitto, J.1    Pfendner, E.2    Jackson, L.G.3
  • 103
    • 0035809198 scopus 로고    scopus 로고
    • An inducible mouse model for epidermolysis bullosa simplex: Implications for gene therapy
    • Cao T, Longley MA, Wang XI, Roop DR. An inducible mouse model for epidermolysis bullosa simplex: implications for gene therapy. J Cell Biol 2001;152:651-6.
    • (2001) J Cell Biol , vol.152 , pp. 651-656
    • Cao, T.1    Longley, M.A.2    Wang, X.I.3    Roop, D.R.4
  • 104
    • 0042208442 scopus 로고    scopus 로고
    • Robust neural integration from retinal transplants in mice deficient in GFAP and vimentin
    • Kinouchi R, Takeda M, Yang L, et al. Robust neural integration from retinal transplants in mice deficient in GFAP and vimentin. Nat Neurosci 2003;6:863-8.
    • (2003) Nat Neurosci , vol.6 , pp. 863-868
    • Kinouchi, R.1    Takeda, M.2    Yang, L.3
  • 105
    • 4444265587 scopus 로고    scopus 로고
    • Functional improvement of mutant keratin cells on addition of desmin: An alternative approach to gene therapy for dominant diseases
    • D'Alessandro M, Morley SM, Ogden PH, Liovic M, Porter RM, Lane EB. Functional improvement of mutant keratin cells on addition of desmin: an alternative approach to gene therapy for dominant diseases. Gene Ther 2004;11:1290-5.
    • (2004) Gene Ther , vol.11 , pp. 1290-1295
    • D'Alessandro, M.1    Morley, S.M.2    Ogden, P.H.3    Liovic, M.4    Porter, R.M.5    Lane, E.B.6
  • 106
    • 0036514095 scopus 로고    scopus 로고
    • Ectopic expression of desmin in the epidermis of transgenic mice permits development of a normal epidermis
    • Kirfel J, Peters B, Grund C, Reifenberg K, Magin TM. Ectopic expression of desmin in the epidermis of transgenic mice permits development of a normal epidermis. Differentiation 2002;70:56-68.
    • (2002) Differentiation , vol.70 , pp. 56-68
    • Kirfel, J.1    Peters, B.2    Grund, C.3    Reifenberg, K.4    Magin, T.M.5
  • 107
    • 0038104369 scopus 로고    scopus 로고
    • Distinct chaperone mechanisms can delay the formation of aggresomes by the myopathycausing R120G alphaB-crystallin mutant
    • Chavez Zobel AT, Loranger A, Marceau N, Theriault JR, Lambert H, Landry J. Distinct chaperone mechanisms can delay the formation of aggresomes by the myopathycausing R120G alphaB-crystallin mutant. Hum Mol Genet 2003;12:1609-20.
    • (2003) Hum Mol Genet , vol.12 , pp. 1609-1620
    • Chavez Zobel, A.T.1    Loranger, A.2    Marceau, N.3    Theriault, J.R.4    Lambert, H.5    Landry, J.6
  • 108
    • 1642433232 scopus 로고    scopus 로고
    • Bcl-2 overexpression corrects mitochondrial detects and ameliorates inherited desmin null cardiomyopathy
    • Weisleder N, Taffet GE, Capetanaki Y. Bcl-2 overexpression corrects mitochondrial detects and ameliorates inherited desmin null cardiomyopathy. Proc Natl Acad Sci U S A 2004;101:769-74.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 769-774
    • Weisleder, N.1    Taffet, G.E.2    Capetanaki, Y.3


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