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Volumn 12, Issue 10, 2002, Pages 472-478

SMN-mediated assembly of RNPs: A complex story

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; CHAPERONE; GENE PRODUCT; MESSENGER RNA; PROTEIN; RIBONUCLEOPROTEIN; SMALL NUCLEAR RIBONUCLEOPROTEIN; SURVIVAL MOTOR NEURON PROTEIN; UNCLASSIFIED DRUG;

EID: 0036809734     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0962-8924(02)02371-1     Document Type: Review
Times cited : (198)

References (64)
  • 1
    • 0032862988 scopus 로고    scopus 로고
    • Spliceosomal U snRNP core assembly: Sm proteins assemble onto an Sm site RNA nonanucleotide in a specific and thermodynamically stable manner
    • Raker V.A., et al. Spliceosomal U snRNP core assembly: Sm proteins assemble onto an Sm site RNA nonanucleotide in a specific and thermodynamically stable manner. Mol. Cell. Biol. 19:1999;6554-6565.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6554-6565
    • Raker, V.A.1
  • 2
    • 0034788276 scopus 로고    scopus 로고
    • Molecular mechanisms in spinal muscular atrophy: Models and perspectives
    • Sendtner M. Molecular mechanisms in spinal muscular atrophy: models and perspectives. Curr. Opin. Neurol. 14:2001;629-634.
    • (2001) Curr. Opin. Neurol. , vol.14 , pp. 629-634
    • Sendtner, M.1
  • 3
    • 0035092134 scopus 로고    scopus 로고
    • Spinal muscular atrophy: Present state
    • Schmalbruch H., Haase G. Spinal muscular atrophy: present state. Brain Pathol. 11:2001;231-247.
    • (2001) Brain Pathol. , vol.11 , pp. 231-247
    • Schmalbruch, H.1    Haase, G.2
  • 4
    • 0028797783 scopus 로고
    • Identification and characterization of a spinal muscular atrophy-determining gene
    • Lefebvre S., et al. Identification and characterization of a spinal muscular atrophy-determining gene. Cell. 80:1995;155-165.
    • (1995) Cell , vol.80 , pp. 155-165
    • Lefebvre, S.1
  • 5
    • 0033983258 scopus 로고    scopus 로고
    • An exonic enhancer is required for inclusion of an essential exon in the SMA-determining gene SMN
    • Lorson C.L., Androphy E.J. An exonic enhancer is required for inclusion of an essential exon in the SMA-determining gene SMN. Hum. Mol. Genet. 9:2000;259-265.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 259-265
    • Lorson, C.L.1    Androphy, E.J.2
  • 6
    • 0036544654 scopus 로고    scopus 로고
    • Disruption of an SF2/ASF-dependent exonic splicing enhancer in SMN2 causes spinal muscular atrophy in the absence of SMN1
    • Cartegni L., Krainer A.R. Disruption of an SF2/ASF-dependent exonic splicing enhancer in SMN2 causes spinal muscular atrophy in the absence of SMN1. Nat. Genet. 30:2002;377-384.
    • (2002) Nat. Genet. , vol.30 , pp. 377-384
    • Cartegni, L.1    Krainer, A.R.2
  • 7
    • 0030931720 scopus 로고    scopus 로고
    • Inactivation of the survival motor neuron gene, a candidate gene for human spinal muscular atrophy, leads to massive cell death in early mouse embryos
    • Schrank B., et al. Inactivation of the survival motor neuron gene, a candidate gene for human spinal muscular atrophy, leads to massive cell death in early mouse embryos. Proc. Natl. Acad. Sci. U. S. A. 94:1997;9920-9925.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 9920-9925
    • Schrank, B.1
  • 8
    • 0031081575 scopus 로고    scopus 로고
    • Tudor domains in proteins that interact with RNA
    • Ponting C.P. Tudor domains in proteins that interact with RNA. Trends Biochem. Sci. 22:1997;51-52.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 51-52
    • Ponting, C.P.1
  • 9
    • 8544283791 scopus 로고    scopus 로고
    • The survival motor neuron protein in spinal muscular atrophy
    • Coovert D.D., et al. The survival motor neuron protein in spinal muscular atrophy. Hum. Mol. Genet. 6:1997;1205-1214.
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 1205-1214
    • Coovert, D.D.1
  • 10
    • 0029954338 scopus 로고    scopus 로고
    • A novel nuclear structure containing the survival of motor neurons protein
    • Liu Q., Dreyfuss G. A novel nuclear structure containing the survival of motor neurons protein. EMBO J. 15:1996;3555-3565.
    • (1996) EMBO J. , vol.15 , pp. 3555-3565
    • Liu, Q.1    Dreyfuss, G.2
  • 11
    • 0034641609 scopus 로고    scopus 로고
    • Characterization of a nuclear 20S complex containing the survival of motor neurons (SMN) protein and a specific subset of spliceosomal Sm proteins
    • Meister G., et al. Characterization of a nuclear 20S complex containing the survival of motor neurons (SMN) protein and a specific subset of spliceosomal Sm proteins. Hum. Mol. Genet. 9:2000;1977-1986.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 1977-1986
    • Meister, G.1
  • 12
    • 0033613150 scopus 로고    scopus 로고
    • SMN mutants of spinal muscular atrophy patients are defective in binding to snRNP proteins
    • Pellizzoni L., et al. SMN mutants of spinal muscular atrophy patients are defective in binding to snRNP proteins. Proc. Natl. Acad. Sci. U. S. A. 96:1999;11167-11172.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 11167-11172
    • Pellizzoni, L.1
  • 13
    • 0030931727 scopus 로고    scopus 로고
    • The spinal muscular atrophy disease gene product, SMN, and its associated protein SIP1 are in a complex with spliceosomal snRNP proteins
    • Liu Q., et al. The spinal muscular atrophy disease gene product, SMN, and its associated protein SIP1 are in a complex with spliceosomal snRNP proteins. Cell. 90:1997;1013-1021.
    • (1997) Cell , vol.90 , pp. 1013-1021
    • Liu, Q.1
  • 14
    • 0030928716 scopus 로고    scopus 로고
    • The SMN-SIP1 complex has an essential role in spliceosomal snRNP biogenesis
    • Fischer U., et al. The SMN-SIP1 complex has an essential role in spliceosomal snRNP biogenesis. Cell. 90:1997;1023-1029.
    • (1997) Cell , vol.90 , pp. 1023-1029
    • Fischer, U.1
  • 15
    • 0035370526 scopus 로고    scopus 로고
    • Spliceosomal UsnRNP biogenesis, structure and function
    • Will C.L., Luhrmann R. Spliceosomal UsnRNP biogenesis, structure and function. Curr. Opin. Cell Biol. 13:2001;290-301.
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 290-301
    • Will, C.L.1    Luhrmann, R.2
  • 16
    • 0020338524 scopus 로고
    • U2 RNA shares a structural domain with U1, U4, and U5 RNAs
    • Branlant C., et al. U2 RNA shares a structural domain with U1, U4, and U5 RNAs. EMBO J. 1:1982;1259-1265.
    • (1982) EMBO J. , vol.1 , pp. 1259-1265
    • Branlant, C.1
  • 17
    • 0036238278 scopus 로고    scopus 로고
    • Hypermethylation of the cap structure of both yeast snRNAs and snoRNAs requires a conserved methyltransferase that is localized to the nucleolus
    • Mouaikel J., et al. Hypermethylation of the cap structure of both yeast snRNAs and snoRNAs requires a conserved methyltransferase that is localized to the nucleolus. Mol. Cell. 9:2002;891-901.
    • (2002) Mol. Cell , vol.9 , pp. 891-901
    • Mouaikel, J.1
  • 18
    • 0032567036 scopus 로고    scopus 로고
    • A novel function for SMN, the spinal muscular atrophy disease gene product, in pre-mRNA splicing
    • Pellizzoni L., et al. A novel function for SMN, the spinal muscular atrophy disease gene product, in pre-mRNA splicing. Cell. 95:1998;615-624.
    • (1998) Cell , vol.95 , pp. 615-624
    • Pellizzoni, L.1
  • 19
    • 0242683460 scopus 로고    scopus 로고
    • Essential role for the tudor domain of SMN in spliceosomal U snRNP assembly: Implications for spinal muscular atrophy
    • Buhler D., et al. Essential role for the tudor domain of SMN in spliceosomal U snRNP assembly: implications for spinal muscular atrophy. Hum. Mol. Genet. 8:1999;2351-2357.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 2351-2357
    • Buhler, D.1
  • 20
    • 0033552589 scopus 로고    scopus 로고
    • Gemin3: A novel DEAD box protein that interacts with SMN, the spinal muscular atrophy gene product, and is a component of gems
    • Charroux B., et al. Gemin3: A novel DEAD box protein that interacts with SMN, the spinal muscular atrophy gene product, and is a component of gems. J. Cell Biol. 147:1999;1181-1194.
    • (1999) J. Cell Biol. , vol.147 , pp. 1181-1194
    • Charroux, B.1
  • 21
    • 0036510395 scopus 로고    scopus 로고
    • Purification of native survival of motor neurons complexes and identification of Gemin6 as a novel component
    • Pellizzoni L., et al. Purification of native survival of motor neurons complexes and identification of Gemin6 as a novel component. J. Biol. Chem. 277:2002;7540-7545.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7540-7545
    • Pellizzoni, L.1
  • 22
    • 0037085390 scopus 로고    scopus 로고
    • Gemin5, a novel WD repeat protein component of the SMN complex that binds Sm proteins
    • Gubitz A.K., et al. Gemin5, a novel WD repeat protein component of the SMN complex that binds Sm proteins. J. Biol. Chem. 277:2002;5631-5636.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5631-5636
    • Gubitz, A.K.1
  • 23
    • 0011459688 scopus 로고    scopus 로고
    • Identification and characterization of Gemin7, a novel component of the SMN complex
    • in press
    • Baccon, J. et al. Identification and characterization of Gemin7, a novel component of the SMN complex. J. Biol. Chem. (in press)
    • J. Biol. Chem.
    • Baccon, J.1
  • 24
    • 0031800695 scopus 로고    scopus 로고
    • SMN oligomerization defect correlates with spinal muscular atrophy severity
    • Lorson C.L., et al. SMN oligomerization defect correlates with spinal muscular atrophy severity. Nat. Genet. 19:1998;63-66.
    • (1998) Nat. Genet. , vol.19 , pp. 63-66
    • Lorson, C.L.1
  • 25
    • 0035735484 scopus 로고    scopus 로고
    • A multiprotein complex mediates the ATP-dependent assembly of spliceosomal U snRNPs
    • Meister G., et al. A multiprotein complex mediates the ATP-dependent assembly of spliceosomal U snRNPs. Nat. Cell Biol. 3:2001;945-949.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 945-949
    • Meister, G.1
  • 26
    • 0035846546 scopus 로고    scopus 로고
    • Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln
    • Meister G., et al. Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln. Curr. Biol. 11:2001;1990-1994.
    • (2001) Curr. Biol. , vol.11 , pp. 1990-1994
    • Meister, G.1
  • 27
    • 0035197005 scopus 로고    scopus 로고
    • The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins
    • Friesen W.J., et al. The methylosome, a 20S complex containing JBP1 and pICln, produces dimethylarginine-modified Sm proteins. Mol. Cell. Biol. 21:2001;8289-8300.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 8289-8300
    • Friesen, W.J.1
  • 28
    • 0033018469 scopus 로고    scopus 로고
    • PICln inhibits snRNP biogenesis by binding core spliceosomal proteins
    • Pu W.T., et al. pICln inhibits snRNP biogenesis by binding core spliceosomal proteins. Mol. Cell. Biol. 19:1999;4113-4120.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4113-4120
    • Pu, W.T.1
  • 29
    • 0028144541 scopus 로고
    • Molecular characterization of a swelling-induced chloride conductance regulatory protein, pICln
    • Krapivinsky G.B., et al. Molecular characterization of a swelling-induced chloride conductance regulatory protein, pICln. Cell. 76:1994;439-448.
    • (1994) Cell , vol.76 , pp. 439-448
    • Krapivinsky, G.B.1
  • 30
    • 0034693140 scopus 로고    scopus 로고
    • PRMT3 is a distinct member of the protein arginine N-methyltransferase family. Conferral of substrate specificity by a zinc-finger domain
    • Frankel A., Clarke S. PRMT3 is a distinct member of the protein arginine N-methyltransferase family. Conferral of substrate specificity by a zinc-finger domain. J. Biol. Chem. 275:2000;32974-32982.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32974-32982
    • Frankel, A.1    Clarke, S.2
  • 31
    • 0035854372 scopus 로고    scopus 로고
    • State of the arg: Protein methylation at arginine comes of age
    • McBride A.E., Silver P.A. State of the arg: protein methylation at arginine comes of age. Cell. 106:2001;5-8.
    • (2001) Cell , vol.106 , pp. 5-8
    • McBride, A.E.1    Silver, P.A.2
  • 32
    • 0035980018 scopus 로고    scopus 로고
    • PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins
    • Branscombe T.L., et al. PRMT5 (Janus kinase-binding protein 1) catalyzes the formation of symmetric dimethylarginine residues in proteins. J. Biol. Chem. 276:2001;32971-32976.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32971-32976
    • Branscombe, T.L.1
  • 33
    • 0034595798 scopus 로고    scopus 로고
    • The C-terminal RG dipeptide repeats of the spliceosomal Sm proteins D1 and D3 contain symmetrical dimethylarginines, which form a major B-cell epitope for anti-Sm autoantibodies
    • Brahms H., et al. The C-terminal RG dipeptide repeats of the spliceosomal Sm proteins D1 and D3 contain symmetrical dimethylarginines, which form a major B-cell epitope for anti-Sm autoantibodies. J. Biol. Chem. 275:2000;17122-17129.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17122-17129
    • Brahms, H.1
  • 34
    • 0035947239 scopus 로고    scopus 로고
    • SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets
    • Friesen W.J., et al. SMN, the product of the spinal muscular atrophy gene, binds preferentially to dimethylarginine-containing protein targets. Mol. Cell. 7:2001;1111-1117.
    • (2001) Mol. Cell , vol.7 , pp. 1111-1117
    • Friesen, W.J.1
  • 35
    • 0035171131 scopus 로고    scopus 로고
    • Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B′ and the Sm-like protein LSm4, and their interaction with the SMN protein
    • Brahms H., et al. Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B′ and the Sm-like protein LSm4, and their interaction with the SMN protein. RNA. 7:2001;1-12.
    • (2001) RNA , vol.7 , pp. 1-12
    • Brahms, H.1
  • 36
    • 0036500546 scopus 로고    scopus 로고
    • Sequence-specific interaction of U1 snRNA with the SMN complex
    • Yong J., et al. Sequence-specific interaction of U1 snRNA with the SMN complex. EMBO J. 21:2002;1188-1196.
    • (2002) EMBO J , vol.21 , pp. 1188-1196
    • Yong, J.1
  • 37
    • 0035929237 scopus 로고    scopus 로고
    • Opening of the clamp: An intimate view of an ATP-driven biological machine
    • Ellison V., Stillman B. Opening of the clamp: an intimate view of an ATP-driven biological machine. Cell. 106:2001;655-660.
    • (2001) Cell , vol.106 , pp. 655-660
    • Ellison, V.1    Stillman, B.2
  • 38
    • 0035477247 scopus 로고    scopus 로고
    • Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new 14 kDa Sm D1-like protein
    • Pillai R. S., et al. Purified U7 snRNPs lack the Sm proteins D1 and D2 but contain Lsm10, a new 14 kDa Sm D1-like protein. EMBO J. 20:2001;5470-5479.
    • (2001) EMBO J. , vol.20 , pp. 5470-5479
    • Pillai R., S.1
  • 39
    • 0033569743 scopus 로고    scopus 로고
    • A doughnut-shaped heteromer of human Sm-like proteins binds to the 3′-end of U6 snRNA, thereby facilitating U4/U6 duplex formation in vitro
    • Achsel T., et al. A doughnut-shaped heteromer of human Sm-like proteins binds to the 3′-end of U6 snRNA, thereby facilitating U4/U6 duplex formation in vitro. EMBO J. 18:1999;5789-5802.
    • (1999) EMBO J. , vol.18 , pp. 5789-5802
    • Achsel, T.1
  • 40
    • 0033564627 scopus 로고    scopus 로고
    • Sm and Sm-like proteins assemble in two related complexes of deep evolutionary origin
    • Salgado-Garrido J., et al. Sm and Sm-like proteins assemble in two related complexes of deep evolutionary origin. EMBO J. 18:1999;3451-3462.
    • (1999) EMBO J. , vol.18 , pp. 3451-3462
    • Salgado-Garrido, J.1
  • 41
    • 0035341325 scopus 로고    scopus 로고
    • RNA binding in an Sm core domain: X-ray structure and functional analysis of an archaeal Sm protein complex
    • Toro I., et al. RNA binding in an Sm core domain: X-ray structure and functional analysis of an archaeal Sm protein complex. EMBO J. 20:2001;2293-2303.
    • (2001) EMBO J. , vol.20 , pp. 2293-2303
    • Toro, I.1
  • 42
    • 0034714380 scopus 로고    scopus 로고
    • Specific sequences of the Sm and Sm-like (Lsm) proteins mediate their interaction with the spinal muscular atrophy disease gene product (SMN)
    • Friesen W.J., Dreyfuss G. Specific sequences of the Sm and Sm-like (Lsm) proteins mediate their interaction with the spinal muscular atrophy disease gene product (SMN). J. Biol. Chem. 275:2000;26370-26375.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26370-26375
    • Friesen, W.J.1    Dreyfuss, G.2
  • 43
    • 0035914360 scopus 로고    scopus 로고
    • Direct interaction of the spinal muscular atrophy disease protein SMN with the small nucleolar RNA-associated protein fibrillarin
    • Jones K.W., et al. Direct interaction of the spinal muscular atrophy disease protein SMN with the small nucleolar RNA-associated protein fibrillarin. J. Biol. Chem. 276:2001;38645-38651.
    • (2001) J. Biol. Chem. , vol.276 , pp. 38645-38651
    • Jones, K.W.1
  • 44
    • 0035943003 scopus 로고    scopus 로고
    • The survival of motor neurons (SMN) protein interacts with the snoRNP proteins fibrillarin and GAR1
    • Pellizzoni L., et al. The survival of motor neurons (SMN) protein interacts with the snoRNP proteins fibrillarin and GAR1. Curr. Biol. 11:2001;1079-1088.
    • (2001) Curr. Biol. , vol.11 , pp. 1079-1088
    • Pellizzoni, L.1
  • 45
    • 0036342369 scopus 로고    scopus 로고
    • The DnaK chaperone system facilitates 30S ribosomal subunit assembly
    • Maki J.A., et al. The DnaK chaperone system facilitates 30S ribosomal subunit assembly. Mol. Cell. 10:2002;129-138.
    • (2002) Mol. Cell , vol.10 , pp. 129-138
    • Maki, J.A.1
  • 46
    • 0037162519 scopus 로고    scopus 로고
    • Gene targeting of Gemin2 in mice reveals a correlation between defects in the biogenesis of U snRNPs and motoneuron cell death
    • Jablonka S., et al. Gene targeting of Gemin2 in mice reveals a correlation between defects in the biogenesis of U snRNPs and motoneuron cell death. Proc. Natl. Acad. Sci. U. S. A. 99:2002;10126-10131.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 10126-10131
    • Jablonka, S.1
  • 47
    • 0033524941 scopus 로고    scopus 로고
    • Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs
    • Kambach C., et al. Crystal structures of two Sm protein complexes and their implications for the assembly of the spliceosomal snRNPs. Cell. 96:1999;375-387.
    • (1999) Cell , vol.96 , pp. 375-387
    • Kambach, C.1
  • 48
    • 0033516645 scopus 로고    scopus 로고
    • Characterisation of DP103, a novel DEAD box protein that binds to the Epstein-Barr virus nuclear proteins EBNA2 and EBNA3C
    • Grundhoff A.T., et al. Characterisation of DP103, a novel DEAD box protein that binds to the Epstein-Barr virus nuclear proteins EBNA2 and EBNA3C. J. Biol. Chem. 27:1999;19136-19144.
    • (1999) J. Biol. Chem. , vol.27 , pp. 19136-19144
    • Grundhoff, A.T.1
  • 49
    • 0034639998 scopus 로고    scopus 로고
    • Direct interaction of Smn with dp103, a putative RNA helicase: A role for Smn in transcription regulation?
    • Campbell L., et al. Direct interaction of Smn with dp103, a putative RNA helicase: a role for Smn in transcription regulation? Hum. Mol. Genet. 9:2000;1093-1100.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 1093-1100
    • Campbell, L.1
  • 50
    • 0034688999 scopus 로고    scopus 로고
    • Gemin4. A novel component of the SMN complex that is found in both gems and nucleoli
    • Charroux B., et al. Gemin4. A novel component of the SMN complex that is found in both gems and nucleoli. J. Cell Biol. 148:2000;1177-1186.
    • (2000) J. Cell Biol. , vol.148 , pp. 1177-1186
    • Charroux, B.1
  • 51
    • 0035171131 scopus 로고    scopus 로고
    • Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B′ and the Sm-like protein LSm4, and their interaction with the SMN protein
    • Brahms H., et al. Symmetrical dimethylation of arginine residues in spliceosomal Sm protein B/B′ and the Sm-like protein LSm4, and their interaction with the SMN protein. RNA. 7:2001;1531-1542.
    • (2001) RNA , vol.7 , pp. 1531-1542
    • Brahms, H.1
  • 52
    • 0035887042 scopus 로고    scopus 로고
    • Coilin forms the bridge between Cajal bodies and SMN, the spinal muscular atrophy protein
    • Hebert M.D., et al. Coilin forms the bridge between Cajal bodies and SMN, the spinal muscular atrophy protein. Genes Dev. 15:2001;2720-2729.
    • (2001) Genes Dev. , vol.15 , pp. 2720-2729
    • Hebert, M.D.1
  • 53
    • 0033621413 scopus 로고    scopus 로고
    • A role for polyproline motifs in the spinal muscular atrophy protein SMN. Profilins bind to and colocalize with SMN in nuclear gems
    • Giesemann T., et al. A role for polyproline motifs in the spinal muscular atrophy protein SMN. Profilins bind to and colocalize with SMN in nuclear gems. J. Biol. Chem. 274:1999;37908-37914.
    • (1999) J. Biol. Chem. , vol.274 , pp. 37908-37914
    • Giesemann, T.1
  • 54
    • 0035074529 scopus 로고    scopus 로고
    • Spinal muscular atrophy disrupts the interaction of ZPR1 with the SMN protein
    • Gangwani L., et al. Spinal muscular atrophy disrupts the interaction of ZPR1 with the SMN protein. Nat. Cell Biol. 3:2001;376-383.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 376-383
    • Gangwani, L.1
  • 55
    • 0035798635 scopus 로고    scopus 로고
    • Osteoclast-stimulating factor interacts with the spinal muscular atrophy gene product to stimulate osteoclast formation
    • Kurihara N., et al. Osteoclast-stimulating factor interacts with the spinal muscular atrophy gene product to stimulate osteoclast formation. J. Biol. Chem. 276:2001;41035-41039.
    • (2001) J. Biol. Chem. , vol.276 , pp. 41035-41039
    • Kurihara, N.1
  • 56
    • 0036566264 scopus 로고    scopus 로고
    • A novel association of the SMN protein with two major non-ribosomal nucleolar proteins and its implication in spinal muscular atrophy
    • Lefebvre S., et al. A novel association of the SMN protein with two major non-ribosomal nucleolar proteins and its implication in spinal muscular atrophy. Hum. Mol. Genet. 11:2002;1017-1027.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1017-1027
    • Lefebvre, S.1
  • 57
    • 0035825155 scopus 로고    scopus 로고
    • A functional interaction between the survival motor neuron complex and RNA polymerase II
    • Pellizzoni L., et al. A functional interaction between the survival motor neuron complex and RNA polymerase II. J. Cell Biol. 152:2001;75-86.
    • (2001) J. Cell Biol. , vol.152 , pp. 75-86
    • Pellizzoni, L.1
  • 58
    • 0035476679 scopus 로고    scopus 로고
    • SMN interacts with a novel family of hnRNP and spliceosomal proteins
    • Mourelatos Z., et al. SMN interacts with a novel family of hnRNP and spliceosomal proteins. EMBO J. 20:2001;5443-5452.
    • (2001) EMBO J. , vol.20 , pp. 5443-5452
    • Mourelatos, Z.1
  • 59
    • 0036154096 scopus 로고    scopus 로고
    • Specific interaction of Smn, the spinal muscular atrophy determining gene product, with hnRNP-R and gry-rbp/hnRNP-Q: A role for Smn in RNA processing in motor axons?
    • Rossoll W., et al. Specific interaction of Smn, the spinal muscular atrophy determining gene product, with hnRNP-R and gry-rbp/hnRNP-Q: a role for Smn in RNA processing in motor axons? Hum. Mol. Genet. 11:2002;93-105.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 93-105
    • Rossoll, W.1
  • 60
    • 0037098960 scopus 로고    scopus 로고
    • SMN, the spinal muscular atrophy protein, forms a pre-import snRNP complex with snurportin1 and importin-β
    • Narayanan U., et al. SMN, the spinal muscular atrophy protein, forms a pre-import snRNP complex with snurportin1 and importin-β Hum. Mol. Genet. 11:2002;1785-1795.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1785-1795
    • Narayanan, U.1
  • 61
    • 0035445710 scopus 로고    scopus 로고
    • Association of galectin-1 and galectin-3 with Gemin4 in complexes containing the SMN protein
    • Park J. W., et al. Association of galectin-1 and galectin-3 with Gemin4 in complexes containing the SMN protein. Nucleic Acids Res. 29:2001;3595-3602.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3595-3602
    • Park J., W.1
  • 62
    • 0032771012 scopus 로고    scopus 로고
    • Identification of survival motor neuron as a transcriptional activator-binding protein
    • Strasswimmer J., et al. Identification of survival motor neuron as a transcriptional activator-binding protein. Hum. Mol. Genet. 8:1999;1219-1226.
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 1219-1226
    • Strasswimmer, J.1
  • 63
    • 0036106046 scopus 로고    scopus 로고
    • Minute virus of mice small nonstructural protein NS2 interacts and colocalizes with the Smn protein
    • Young P.J., et al. Minute virus of mice small nonstructural protein NS2 interacts and colocalizes with the Smn protein. J. Virol. 76:2002;6364-6369.
    • (2002) J. Virol. , vol.76 , pp. 6364-6369
    • Young, P.J.1
  • 64
    • 0036197051 scopus 로고    scopus 로고
    • Minute virus of mice NS1 interacts with the SMN protein, and they colocalize in novel nuclear bodies induced by parvovirus infection
    • Young P.J., et al. Minute virus of mice NS1 interacts with the SMN protein, and they colocalize in novel nuclear bodies induced by parvovirus infection. J. Virol. 76:2002;3892-3904.
    • (2002) J. Virol. , vol.76 , pp. 3892-3904
    • Young, P.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.