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Volumn 41, Issue 3, 2005, Pages 221-226

Nuclear matrix proteins and hereditary diseases

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEAR MATRIX PROTEIN;

EID: 17844401254     PISSN: 10227954     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11177-005-0076-y     Document Type: Review
Times cited : (5)

References (37)
  • 1
    • 0007109410 scopus 로고    scopus 로고
    • On the History of Nuclear Matrix Manifestation
    • Zbarsky, I.B., On the History of Nuclear Matrix Manifestation, Cell Res., 1998, vol. 8, pp. 99-103.
    • (1998) Cell Res. , vol.8 , pp. 99-103
    • Zbarsky, I.B.1
  • 2
    • 7044230197 scopus 로고
    • Enzyme Activities of Nuclear Matrix
    • Moscow
    • Sjakste, N.I. and Sjakste, T.G., Enzyme Activities of Nuclear Matrix, Biochemistry (Moscow), 1994, vol. 50, pp. 1239-1246.
    • (1994) Biochemistry , vol.50 , pp. 1239-1246
    • Sjakste, N.I.1    Sjakste, T.G.2
  • 3
    • 0035438241 scopus 로고    scopus 로고
    • Transcription Factors and the Nuclear Matrix
    • Moscow
    • Sjakste, N.I. and Sjakste, T.G., Transcription Factors and the Nuclear Matrix, Mol. Biol. (Moscow), 2001, vol. 35, pp. 627-635.
    • (2001) Mol. Biol. , vol.35 , pp. 627-635
    • Sjakste, N.I.1    Sjakste, T.G.2
  • 4
    • 0027636436 scopus 로고
    • Modification of the Structure of Chromatin and the Nuclear Matrix in Pathological Processes: Prospects for Correction with Drugs
    • Sjakste, N.I., Modification of the Structure of Chromatin and the Nuclear Matrix in Pathological Processes: Prospects for Correction with Drugs, Vopr. Med. Khim., 1993, vol. 39, pp. 10-16.
    • (1993) Vopr. Med. Khim. , vol.39 , pp. 10-16
    • Sjakste, N.I.1
  • 5
    • 0007109183 scopus 로고
    • Modification of the Structure of Chromatin and the Nuclear Matrix in Cell Malignant Transformation and Cancer Treatment
    • Sjakste, N.I., Modification of the Structure of Chromatin and the Nuclear Matrix in Cell Malignant Transformation and Cancer Treatment, Eksp. Onkol., 1992, vol. 14, pp. 19-23.
    • (1992) Eksp. Onkol. , vol.14 , pp. 19-23
    • Sjakste, N.I.1
  • 6
    • 0037077223 scopus 로고    scopus 로고
    • Colocalization, Physical, and Functional Interaction between Werner and Bloom Syndrome Proteins
    • Von Kobbe, C., Karmakar, P., Dawut, L., et al., Colocalization, Physical, and Functional Interaction between Werner and Bloom Syndrome Proteins, J. Biol. Chem., 2002, vol. 277, pp. 22 035-22 044.
    • (2002) J. Biol. Chem. , vol.277 , pp. 22035-22044
    • Von Kobbe, C.1    Karmakar, P.2    Dawut, L.3
  • 7
    • 0032760273 scopus 로고    scopus 로고
    • Localization of the Bloom Syndrome Helicase to Punctate Nuclear Structures and the Nuclear Matrix and Regulation during the Cell Cycle: Comparison with the Werner's Syndrome Helicase
    • Gharibyan, V. and Youssoufian, H., Localization of the Bloom Syndrome Helicase to Punctate Nuclear Structures and the Nuclear Matrix and Regulation during the Cell Cycle: Comparison with the Werner's Syndrome Helicase, Mol. Carcinogen., 1999, vol. 26, pp. 261-273.
    • (1999) Mol. Carcinogen. , vol.26 , pp. 261-273
    • Gharibyan, V.1    Youssoufian, H.2
  • 8
    • 0035897415 scopus 로고    scopus 로고
    • Regulation and Localization of the Bloom Syndrome Protein in Response to DNA Damage
    • Bischof, O., Kim, S.H., Irving, J., et al., Regulation and Localization of the Bloom Syndrome Protein in Response to DNA Damage, J. Cell Biol., 2001, vol. 153, pp. 367-380.
    • (2001) J. Cell Biol. , vol.153 , pp. 367-380
    • Bischof, O.1    Kim, S.H.2    Irving, J.3
  • 9
    • 0037039443 scopus 로고    scopus 로고
    • Translocation of Cockayne Syndrome Group A Protein to the Nuclear Matrix: Possible Relevance to Transcription-Coupled DNA Repair
    • Kamiuchi, S., Saijo, M., Citterio, E., et al., Translocation of Cockayne Syndrome Group A Protein to the Nuclear Matrix: Possible Relevance to Transcription-Coupled DNA Repair, Proc. Natl. Acad. Sci. USA, 2002, vol. 99, pp. 201-206.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 201-206
    • Kamiuchi, S.1    Saijo, M.2    Citterio, E.3
  • 10
    • 0034729458 scopus 로고    scopus 로고
    • Low Levels of NPM Gene Expression in UV-Sensitive Human Cell Lines
    • Hirano, J., Wang, X., Kita, K., et al., Low Levels of NPM Gene Expression in UV-Sensitive Human Cell Lines, Cancer Lett., 2000, vol. 153, pp. 183-188.
    • (2000) Cancer Lett. , vol.153 , pp. 183-188
    • Hirano, J.1    Wang, X.2    Kita, K.3
  • 11
    • 0033571205 scopus 로고    scopus 로고
    • Oxidative Damage-Induced PCNA Complex Formation Is Efficient in Xeroderma Pigmentosum Group A but Reduced in Cockayne Syndrome Group B Cells
    • Balajee, A.S., Dianova, I., and Bohr, V.A., Oxidative Damage-Induced PCNA Complex Formation Is Efficient in Xeroderma Pigmentosum Group A but Reduced in Cockayne Syndrome Group B Cells, Nucleic Acids Res., 1999, vol. 27, pp. 4476-4482.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 4476-4482
    • Balajee, A.S.1    Dianova, I.2    Bohr, V.A.3
  • 12
    • 0035968325 scopus 로고    scopus 로고
    • Fanconi Anemia Proteins Localize to Chromatin and the Nuclear Matrix in a DNA Damage- and Cell Cycle-Regulated Manner
    • Qiao, F., Moss, A., and Kupfer, G.M., Fanconi Anemia Proteins Localize to Chromatin and the Nuclear Matrix in a DNA Damage- and Cell Cycle-Regulated Manner, J. Biol. Chem., 2001, vol. 276, pp. 23 391-23 396.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23391-23396
    • Qiao, F.1    Moss, A.2    Kupfer, G.M.3
  • 13
    • 0037673950 scopus 로고    scopus 로고
    • Recurrent de Novo Point Mutations in Lamin a Cause Hutchinson-Gilford Progeria Syndrome
    • Eriksson, M., Brown, W.T., Gordon, L.B., et al., Recurrent De Novo Point Mutations in Lamin A Cause Hutchinson-Gilford Progeria Syndrome, Nature, 2003, vol. 423, pp. 293-298.
    • (2003) Nature , vol.423 , pp. 293-298
    • Eriksson, M.1    Brown, W.T.2    Gordon, L.B.3
  • 14
    • 0038376023 scopus 로고    scopus 로고
    • LMNA Is Mutated in Hutchinson-Gilford Progeria (MIM 176 670) but not in Wiedemann-Rautenstrauch Progeroid Syndrome (MIM 264090)
    • Cao, H. and Hegele, R.A., LMNA Is Mutated in Hutchinson-Gilford Progeria (MIM 176 670) but not in Wiedemann-Rautenstrauch Progeroid Syndrome (MIM 264090), J. Hum. Genet., 2003, vol. 48, pp. 271-274.
    • (2003) J. Hum. Genet. , vol.48 , pp. 271-274
    • Cao, H.1    Hegele, R.A.2
  • 15
    • 0342514792 scopus 로고    scopus 로고
    • Cell Cycle-Dependent Phosphorylation of the ATRX Protein Correlates with Changes in Nuclear Matrix and Chromatin Association
    • Berube, N.G., Smeenk, C.A., and Picketts, D.J., Cell Cycle-Dependent Phosphorylation of the ATRX Protein Correlates with Changes in Nuclear Matrix and Chromatin Association, Hum. Mol. Genet., 2000, vol. 9, pp. 539-547.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 539-547
    • Berube, N.G.1    Smeenk, C.A.2    Picketts, D.J.3
  • 16
    • 0036918231 scopus 로고    scopus 로고
    • Manifold Decreased Protein Levels of Matrin 3, Reduced Motor Protein HMP and Hlark in Fetal Down's Syndrome Brain
    • Bernert, G., Fountoulakis, M., and Lubec, G., Manifold Decreased Protein Levels of Matrin 3, Reduced Motor Protein HMP and Hlark in Fetal Down's Syndrome Brain, Proteomics, 2002, vol. 2, pp. 1752-1757.
    • (2002) Proteomics , vol.2 , pp. 1752-1757
    • Bernert, G.1    Fountoulakis, M.2    Lubec, G.3
  • 17
    • 0033523762 scopus 로고    scopus 로고
    • Presenilin 1 Suppresses the Function of c-Jun Homodimers via Interaction with QM/Jif-1
    • Imafuku, I., Masaki, T., Waragai, M., et al., Presenilin 1 Suppresses the Function of c-Jun Homodimers via Interaction with QM/Jif-1, J. Cell Biol., 1999, vol. 147, pp. 121-134.
    • (1999) J. Cell Biol. , vol.147 , pp. 121-134
    • Imafuku, I.1    Masaki, T.2    Waragai, M.3
  • 18
    • 18544368523 scopus 로고    scopus 로고
    • Huntingtin Is Present in the Nucleus, Interacts with the Transcriptional Corepressor C-Terminal Binding Protein, and Represses Transcription
    • Kegel, K.B., Meloni, A.R., Yi, Y., et al., Huntingtin Is Present in the Nucleus, Interacts with the Transcriptional Corepressor C-Terminal Binding Protein, and Represses Transcription, J. Biol. Chem., 2002, vol. 277, pp. 7466-7476.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7466-7476
    • Kegel, K.B.1    Meloni, A.R.2    Yi, Y.3
  • 19
    • 0035862167 scopus 로고    scopus 로고
    • Nuclear Localization of Cystatin B, the Cathepsin Inhibitor Implicated in Myoclonus Epilepsy (EPM1)
    • Riccio, M., Di Giaimo, R., Pianetti, S., et al., Nuclear Localization of Cystatin B, the Cathepsin Inhibitor Implicated in Myoclonus Epilepsy (EPM1), Exp. Cell Res., 2001, vol. 262, pp. 84-94.
    • (2001) Exp. Cell Res. , vol.262 , pp. 84-94
    • Riccio, M.1    Di Giaimo, R.2    Pianetti, S.3
  • 20
    • 0034605071 scopus 로고    scopus 로고
    • Atrophin-1, the Dentato-Rubral and Pallido-Luysian Atrophy Gene Product, Interacts with ETP/MTG8 in the Nuclear Matrix and Represses Transcription
    • Wood, J.D., Nucifora, F.C., Duan, K., et al., Atrophin-1, the Dentato-Rubral and Pallido-Luysian Atrophy Gene Product, Interacts with ETP/MTG8 in the Nuclear Matrix and Represses Transcription, J. Cell Biol., 2000, vol. 150, pp. 939-948.
    • (2000) J. Cell Biol. , vol.150 , pp. 939-948
    • Wood, J.D.1    Nucifora, F.C.2    Duan, K.3
  • 21
    • 0030841672 scopus 로고    scopus 로고
    • Expansion of a CUG Trinucleotide Repeat in the 3′-Untranslated Region of Myotonic Dystrophy Protein Kinase Transcripts Results in Nuclear Retention of Transcripts
    • Davis, B.M., McCurrach, M.E., Taneja, K.L., et al., Expansion of a CUG Trinucleotide Repeat in the 3′-Untranslated Region of Myotonic Dystrophy Protein Kinase Transcripts Results in Nuclear Retention of Transcripts, Proc. Natl. Acad. Sci. USA, 1997, vol. 94, pp. 7388-7393.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7388-7393
    • Davis, B.M.1    McCurrach, M.E.2    Taneja, K.L.3
  • 22
    • 0033786789 scopus 로고    scopus 로고
    • Nuclear Envelope Proteins and Associated Diseases
    • Nagano, A. and Arahata, K., Nuclear Envelope Proteins and Associated Diseases, Curr. Opin. Neurol., 2000, vol. 13, pp. 533-539.
    • (2000) Curr. Opin. Neurol. , vol.13 , pp. 533-539
    • Nagano, A.1    Arahata, K.2
  • 23
    • 0034536268 scopus 로고    scopus 로고
    • Mutations in the LMNA Gene Encoding Lamin A/C
    • Genschel, J. and Schmidt, H.H., Mutations in the LMNA Gene Encoding Lamin A/C, Hum. Mutat., 2000, vol. 16, pp. 51-59.
    • (2000) Hum. Mutat. , vol.16 , pp. 51-59
    • Genschel, J.1    Schmidt, H.H.2
  • 24
    • 9144247168 scopus 로고    scopus 로고
    • Phenotypic Variability in Autosomal Recessive Axonal Charcot-Marie-Tooth Disease Due to the R298C Mutation in Lamin A/C
    • Tazir, M., Azzedine, H., Assami, S., et al., Phenotypic Variability in Autosomal Recessive Axonal Charcot-Marie-Tooth Disease Due to the R298C Mutation in Lamin A/C, Brain, 2004, vol. 127, pp. 154-163.
    • (2004) Brain , vol.127 , pp. 154-163
    • Tazir, M.1    Azzedine, H.2    Assami, S.3
  • 25
    • 0035996030 scopus 로고    scopus 로고
    • The Nuclear Muscular Dystrophies
    • Wehnert, M.S. and Bonne, G., The Nuclear Muscular Dystrophies, Semin. Pediatr. Neurol., 2002, vol. 9, pp. 100-107.
    • (2002) Semin. Pediatr. Neurol. , vol.9 , pp. 100-107
    • Wehnert, M.S.1    Bonne, G.2
  • 26
    • 0037342243 scopus 로고    scopus 로고
    • A New Clinical Condition Linked to A Novel Mutation in Lamins A and C with Generalized Lipoatrophy, Insulin-Resistant Diabetes, Disseminated Leukomelanodermic Papules, Liver Steatosis, and Cardiomyopathy
    • Caux, F., Dubosclard, E., Lascols, O., et al., A New Clinical Condition Linked to A Novel Mutation in Lamins A and C with Generalized Lipoatrophy, Insulin-Resistant Diabetes, Disseminated Leukomelanodermic Papules, Liver Steatosis, and Cardiomyopathy, J. Clin. Endocrinol. Metab., 2003, vol. 88, pp. 1006-1013.
    • (2003) J. Clin. Endocrinol. Metab. , vol.88 , pp. 1006-1013
    • Caux, F.1    Dubosclard, E.2    Lascols, O.3
  • 27
    • 2542423005 scopus 로고    scopus 로고
    • Lamin A/C Truncation in Dilated Cardiomyopathy with Conduction Disease
    • MacLeod, H.M., Culley, M.R., Huber, J.M., et al., Lamin A/C Truncation in Dilated Cardiomyopathy with Conduction Disease, BMC Med. Genet., 2003, vol. 4, p. 4.
    • (2003) BMC Med. Genet. , vol.4 , pp. 4
    • MacLeod, H.M.1    Culley, M.R.2    Huber, J.M.3
  • 28
    • 0036837219 scopus 로고    scopus 로고
    • Functional Domains of the Nucleus: Implications for Emery-Dreifuss Muscular Dystrophy
    • Maraldi, N.M., Lattanzi, G., Sabatelli, P., et al., Functional Domains of the Nucleus: Implications for Emery-Dreifuss Muscular Dystrophy, Neuromuscul. Disord., 2002, vol. 12, pp. 815-823.
    • (2002) Neuromuscul. Disord. , vol.12 , pp. 815-823
    • Maraldi, N.M.1    Lattanzi, G.2    Sabatelli, P.3
  • 29
    • 0037081564 scopus 로고    scopus 로고
    • The Cell Cycle-Dependent Mislocalisation of Emerin May Contribute to the Emery-Dreifuss Muscular Dystrophy Phenotype
    • Fairley, E.A., Riddell, A., Ellis, J.A., and Kendrick-Jones, J., The Cell Cycle-Dependent Mislocalisation of Emerin May Contribute to the Emery-Dreifuss Muscular Dystrophy Phenotype, J. Cell Sci., 2002, vol. 115, pp. 341-354.
    • (2002) J. Cell Sci. , vol.115 , pp. 341-354
    • Fairley, E.A.1    Riddell, A.2    Ellis, J.A.3    Kendrick-Jones, J.4
  • 30
    • 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, vol. 71, pp. 426-431.
    • (2002) Am. J. Hum. Genet. , vol.71 , pp. 426-431
    • Novelli, G.1    Muchir, A.2    Sangiuolo, F.3
  • 31
    • 0037564014 scopus 로고    scopus 로고
    • Genetic and Phenotypic Heterogeneity in Patients with Mandibuloacral Dysplasia-Associated Lipodystrophy
    • Simha, V., Agarwal, A.K., Oral, E.A., et al., Genetic and Phenotypic Heterogeneity in Patients with Mandibuloacral Dysplasia-Associated Lipodystrophy, J. Clin, Endocrinol. Metab., 2003, vol. 88, pp. 2821-2824.
    • (2003) J. Clin, Endocrinol. Metab. , vol.88 , pp. 2821-2824
    • Simha, V.1    Agarwal, A.K.2    Oral, E.A.3
  • 32
    • 0041919374 scopus 로고    scopus 로고
    • Zinc Metalloproteinase, ZMPSTE24, Is Mutated in Mandibuloacral Dysplasia
    • Agarwal, A.K., Fryns, J.P., Auchus, R.J., et al., Zinc Metalloproteinase, ZMPSTE24, Is Mutated in Mandibuloacral Dysplasia, Hum. Mol. Genet., 2003, vol. 12, pp. 1995-2001.
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 1995-2001
    • Agarwal, A.K.1    Fryns, J.P.2    Auchus, R.J.3
  • 33
    • 0345535128 scopus 로고    scopus 로고
    • Autosomal Recessive HEM/Greenberg Skeletal Dysplasia Is Caused by 3β-Hydroxysterol δ14-Reductase Deficiency Due to Mutations in the Lamin B Receptor Gene
    • Waterham, H.R., Koster, J., Mooyer, P., et al., Autosomal Recessive HEM/Greenberg Skeletal Dysplasia Is Caused by 3β-Hydroxysterol δ14-Reductase Deficiency Due to Mutations in the Lamin B Receptor Gene, Am. J. Hum. Genet., 2003, vol. 72, pp. 1013-1017.
    • (2003) Am. J. Hum. Genet. , vol.72 , pp. 1013-1017
    • Waterham, H.R.1    Koster, J.2    Mooyer, P.3
  • 34
    • 0033289292 scopus 로고    scopus 로고
    • Role of Nuclear Lamins in Nuclear Segmentation of Human Neutrophils
    • Yabuki, M., Miyake, T., Doi, Y., et al., Role of Nuclear Lamins in Nuclear Segmentation of Human Neutrophils, Physiol. Chem. Phys. Med. NMR., 1999, vol. 31, pp. 77-84.
    • (1999) Physiol. Chem. Phys. Med. NMR. , vol.31 , pp. 77-84
    • Yabuki, M.1    Miyake, T.2    Doi, Y.3
  • 35
    • 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, C.K., Olins, A.L., et al., Mutations in the Gene Encoding the Lamin B Receptor Produce an Altered Nuclear Morphology in Granulocytes (Pelger-Huet Anomaly), Nat. Genet., 2002, vol. 31, pp. 410-414.
    • (2002) Nat. Genet. , vol.31 , pp. 410-414
    • Hoffmann, K.1    Dreger, C.K.2    Olins, A.L.3
  • 36
    • 0242266432 scopus 로고    scopus 로고
    • Lamin B Receptor Mutations in Pelger-Huet Anomaly
    • Best, S., Salvati, E, Kallo, J., et al., Lamin B Receptor Mutations in Pelger-Huet Anomaly, Br. J. Haematol., 2003, vol. 123, pp. 542-544.
    • (2003) Br. J. Haematol. , vol.123 , pp. 542-544
    • Best, S.1    Salvati, E.2    Kallo, J.3
  • 37
    • 0347917296 scopus 로고    scopus 로고
    • Reduced Histone Biotinylation in Multiple Carboxylase Deficiency Patients: A Nuclear Role for Holocarboxylase Synthetase
    • Narang, M.A., Dumas, R., Ayer, L.M., et al., Reduced Histone Biotinylation in Multiple Carboxylase Deficiency Patients: A Nuclear Role for Holocarboxylase Synthetase, Hum. Mol. Genet., 2004, vol. 13, pp. 15-23.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 15-23
    • Narang, M.A.1    Dumas, R.2    Ayer, L.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.