메뉴 건너뛰기




Volumn 4, Issue , 2003, Pages

Domain analysis of the tubulin cofactor system: A model for tubulin folding and dimerization

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CHAPERONIN; COFACTOR A; COFACTOR B; COFACTOR C; COFACTOR D; COFACTOR E; COFACTOR PROTEIN; SPECTRIN; TUBULIN; UBIQUITIN; UNCLASSIFIED DRUG; FISH PROTEIN; FUNGAL PROTEIN; HELMINTH PROTEIN; PEPTIDE; SCHIZOSACCHAROMYCES POMBE PROTEIN; TUBULIN-SPECIFIC CHAPERONE C;

EID: 2942610866     PISSN: 14712105     EISSN: None     Source Type: Journal    
DOI: 10.1186/1471-2105-4-46     Document Type: Article
Times cited : (36)

References (71)
  • 2
    • 0027528871 scopus 로고
    • Two cofactors and cytoplasmic chaperonin are required for the folding of alpha-and beta-tubulin
    • Gao Y, Vainberg IE, Chow RL and Cowan NJ: Two cofactors and cytoplasmic chaperonin are required for the folding of alpha-and beta-tubulin. Mol Cell Biol 1993, 13:2478-2485.
    • (1993) Mol. Cell Biol. , vol.13 , pp. 2478-2485
    • Gao, Y.1    Vainberg, I.E.2    Chow, R.L.3    Cowan, N.J.4
  • 6
    • 0031817512 scopus 로고    scopus 로고
    • Identification of novel temperature-sensitive lethal alleles in essential beta-tubulin and nonessential alpha 2-tubulin genes as fission yeast polarity mutants
    • Radcliffe P, Hirata D, Childs D, Vardy L and Toda T: Identification of novel temperature-sensitive lethal alleles in essential beta-tubulin and nonessential alpha 2-tubulin genes as fission yeast polarity mutants. Mol Biol Cell 1998, 9:1757-1771.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1757-1771
    • Radcliffe, P.1    Hirata, D.2    Childs, D.3    Vardy, L.4    Toda, T.5
  • 7
    • 0033824583 scopus 로고    scopus 로고
    • The cofactor-dependent pathways for alpha- and beta-tubulins in microtubule biogenesis are functionally different in fission yeast
    • Radcliffe PA, Garcia MA and Toda T: The cofactor-dependent pathways for alpha- and beta-tubulins in microtubule biogenesis are functionally different in fission yeast. Genetics 2000, 156:93-103.
    • (2000) Genetics , vol.156 , pp. 93-103
    • Radcliffe, P.A.1    Garcia, M.A.2    Toda, T.3
  • 8
    • 0032824097 scopus 로고    scopus 로고
    • Functional dissection and hierarchy of tubulin-folding cofactor homologues in fission yeast
    • Radcliffe PA, Hirata D, Vardy L and Toda T: Functional dissection and hierarchy of tubulin-folding cofactor homologues in fission yeast. Mol Biol Cell 1999, 10:2987-3001.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2987-3001
    • Radcliffe, P.A.1    Hirata, D.2    Vardy, L.3    Toda, T.4
  • 9
    • 0033835874 scopus 로고    scopus 로고
    • Characterisation of fission yeast alp11 mutants defines three functional domains within tubulin-folding cofactor B
    • Radcliffe PA and Toda T: Characterisation of fission yeast alp11 mutants defines three functional domains within tubulin-folding cofactor B. Mol Gen Genet 2000, 263:752-760.
    • (2000) Mol. Gen. Genet. , vol.263 , pp. 752-760
    • Radcliffe, P.A.1    Toda, T.2
  • 10
    • 0030820735 scopus 로고    scopus 로고
    • Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors
    • Tian G, Lewis SA, Feierbach B, Stearns T, Rommelaere H, Ampe C and Cowan NJ: Tubulin subunits exist in an activated conformational state generated and maintained by protein cofactors. J Cell Biol 1997, 138:821-832.
    • (1997) J. Cell Biol. , vol.138 , pp. 821-832
    • Tian, G.1    Lewis, S.A.2    Feierbach, B.3    Stearns, T.4    Rommelaere, H.5    Ampe, C.6    Cowan, N.J.7
  • 11
    • 0029848951 scopus 로고    scopus 로고
    • Cofactor A is a molecular chaperone required for beta-tubulin folding: Functional and structural characterization
    • Melki R, Rommelaere H, Leguy R, Vandekerckhove J and Ampe C: Cofactor A is a molecular chaperone required for beta-tubulin folding: functional and structural characterization. Biochemistry 1996, 35:10422-10435.
    • (1996) Biochemistry , vol.35 , pp. 10422-10435
    • Melki, R.1    Rommelaere, H.2    Leguy, R.3    Vandekerckhove, J.4    Ampe, C.5
  • 13
    • 0032472940 scopus 로고    scopus 로고
    • Essential role of tubulin-folding cofactor D in microtubule assembly and its association with microtubules in fission yeast
    • Hirata D, Masuda H, Eddison M and Toda T: Essential role of tubulin-folding cofactor D in microtubule assembly and its association with microtubules in fission yeast. Embo J 1998, 17:658-666.
    • (1998) Embo J. , vol.17 , pp. 658-666
    • Hirata, D.1    Masuda, H.2    Eddison, M.3    Toda, T.4
  • 14
    • 0032770140 scopus 로고    scopus 로고
    • Stolp, a fission yeast protein similar to tubulin folding cofactor E, plays an essential role in mitotic microtubule assembly
    • Grishchuk EL and McIntosh JR: Stolp, a fission yeast protein similar to tubulin folding cofactor E, plays an essential role in mitotic microtubule assembly. J Cell Sci 1999, 112 ( Pt 12):1979-1988.
    • (1999) J. Cell Sci. , vol.112 , Issue.PART 12 , pp. 1979-1988
    • Grishchuk, E.L.1    McIntosh, J.R.2
  • 15
    • 0025057481 scopus 로고
    • Yeast mutants sensitive to antimicrotubule drugs define three genes that affect microtubule function
    • Stearns T, Hoyt MA and Botstein D: Yeast mutants sensitive to antimicrotubule drugs define three genes that affect microtubule function. Genetics 1990, 124:251-262.
    • (1990) Genetics , vol.124 , pp. 251-262
    • Stearns, T.1    Hoyt, M.A.2    Botstein, D.3
  • 16
    • 0026345831 scopus 로고
    • The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes
    • Ursic D and Culbertson MR: The yeast homolog to mouse Tcp-1 affects microtubule-mediated processes. Mol Cell Biol 1991, 11:2629-2640.
    • (1991) Mol. Cell Biol. , vol.11 , pp. 2629-2640
    • Ursic, D.1    Culbertson, M.R.2
  • 17
    • 0029164636 scopus 로고
    • Rbl2p, a yeast protein that binds to beta-tubulin and participates in microtubule function in vivo
    • Archer JE, Vega LR and Solomon F: Rbl2p, a yeast protein that binds to beta-tubulin and participates in microtubule function in vivo. Cell 1995, 82:425-434.
    • (1995) Cell , vol.82 , pp. 425-434
    • Archer, J.E.1    Vega, L.R.2    Solomon, F.3
  • 18
    • 0034729382 scopus 로고    scopus 로고
    • ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin
    • Bhamidipati A, Lewis SA and Cowan NJ: ADP ribosylation factor-like protein 2 (Arl2) regulates the interaction of tubulin-folding cofactor D with native tubulin. J Cell Biol 2000, 149:1087-1096.
    • (2000) J. Cell Biol. , vol.149 , pp. 1087-1096
    • Bhamidipati, A.1    Lewis, S.A.2    Cowan, N.J.3
  • 19
    • 0033588020 scopus 로고    scopus 로고
    • Tubulin folding cofactors as GTPase-activating proteins. GTP hydrolysis and the assembly of the alpha/beta-tubulin heterodimer
    • Tian G, Bhamidipati A, Cowan NJ and Lewis SA: Tubulin folding cofactors as GTPase-activating proteins. GTP hydrolysis and the assembly of the alpha/beta-tubulin heterodimer. J Biol Chem 1999, 274:24054-24058.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24054-24058
    • Tian, G.1    Bhamidipati, A.2    Cowan, N.J.3    Lewis, S.A.4
  • 21
    • 1842568392 scopus 로고    scopus 로고
    • Functional evolution of two subtly different (similar) folds
    • Agrawal V and Kishan RK: Functional evolution of two subtly different (similar) folds. BMC Struct Biol 2001, 1:5.
    • (2001) BMC Struct. Biol. , vol.1 , pp. 5
    • Agrawal, V.1    Kishan, R.K.2
  • 22
    • 0033549896 scopus 로고    scopus 로고
    • Ubiquitin pathway: Another link in the polyubiquitin chain?
    • Dubiel W and Gordon C: Ubiquitin pathway: another link in the polyubiquitin chain? Curr Biol 1999, 9:R554-7.
    • (1999) Curr. Biol. , vol.9
    • Dubiel, W.1    Gordon, C.2
  • 24
    • 0037065732 scopus 로고    scopus 로고
    • Structural studies of the interaction between ubiquitin family proteins and proteasome subunit S5a
    • Walters KJ, Kleijnen MF, Goh AM, Wagner G and Howley PM: Structural studies of the interaction between ubiquitin family proteins and proteasome subunit S5a. Biochemistry 2002, 41:1767-1777.
    • (2002) Biochemistry , vol.41 , pp. 1767-1777
    • Walters, K.J.1    Kleijnen, M.F.2    Goh, A.M.3    Wagner, G.4    Howley, P.M.5
  • 26
    • 0021272595 scopus 로고
    • Erythrocyte spectrin is comprised of many homologous triple helical segments
    • Speicher DW and Marchesi VT: Erythrocyte spectrin is comprised of many homologous triple helical segments. Nature 1984, 311:177-180.
    • (1984) Nature , vol.311 , pp. 177-180
    • Speicher, D.W.1    Marchesi, V.T.2
  • 27
    • 0026510756 scopus 로고
    • Analysis of the three-alpha-helix motif in the spectrin superfamily of proteins
    • Parry DA, Dixon TW and Cohen C: Analysis of the three-alpha-helix motif in the spectrin superfamily of proteins. Biophys J 1992, 61:858-867.
    • (1992) Biophys. J. , vol.61 , pp. 858-867
    • Parry, D.A.1    Dixon, T.W.2    Cohen, C.3
  • 29
    • 0033588277 scopus 로고    scopus 로고
    • Structure of the alpha-actinin rod: Molecular basis for cross-linking of actin filaments
    • Djinovic-Carugo K, Young P, Gautel M and Saraste M: Structure of the alpha-actinin rod: molecular basis for cross-linking of actin filaments. Cell 1999, 98:537-546.
    • (1999) Cell , vol.98 , pp. 537-546
    • Djinovic-Carugo, K.1    Young, P.2    Gautel, M.3    Saraste, M.4
  • 30
    • 0025995618 scopus 로고
    • Ankyrin binds to the 15th repetitive unit of erythroid and nonerythroid beta-spectrin
    • Kennedy SP, Warren SL, Forget BG and Morrow JS: Ankyrin binds to the 15th repetitive unit of erythroid and nonerythroid beta-spectrin. J Cell Biol 1991, 115:267-277.
    • (1991) J. Cell Biol. , vol.115 , pp. 267-277
    • Kennedy, S.P.1    Warren, S.L.2    Forget, B.G.3    Morrow, J.S.4
  • 31
    • 0026806912 scopus 로고
    • Ankyrins. Adaptors between diverse plasma membrane proteins and the cytoplasm
    • Bennett V: Ankyrins. Adaptors between diverse plasma membrane proteins and the cytoplasm. J Biol Chem 1992, 267:8703-8706.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8703-8706
    • Bennett, V.1
  • 32
    • 0032561199 scopus 로고    scopus 로고
    • A cluster of basic repeats in the dystrophin rod domain binds F-actin through an electrostatic interaction
    • Amann KJ, Renley BA and Ervasti JM: A cluster of basic repeats in the dystrophin rod domain binds F-actin through an electrostatic interaction. J Biol Chem 1998, 273:28419-28423.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28419-28423
    • Amann, K.J.1    Renley, B.A.2    Ervasti, J.M.3
  • 33
    • 0037138385 scopus 로고    scopus 로고
    • The spectrin repeat: A structural platform for cytoskeletal protein assemblies
    • Djinovic-Carugo K, Gautel M, Ylanne J and Young P: The spectrin repeat: a structural platform for cytoskeletal protein assemblies. FEBS Lett 2002, 513:119-123.
    • (2002) FEBS Lett. , vol.513 , pp. 119-123
    • Djinovic-Carugo, K.1    Gautel, M.2    Ylanne, J.3    Young, P.4
  • 34
    • 0034609746 scopus 로고    scopus 로고
    • Actin cytoskeleton: Putting a CAP on actin polymerization
    • Stevenson VA and Theurkauf WE: Actin cytoskeleton: putting a CAP on actin polymerization. Curr Biol 2000, 10:R695-7.
    • (2000) Curr. Biol. , vol.10
    • Stevenson, V.A.1    Theurkauf, W.E.2
  • 36
    • 0033150672 scopus 로고    scopus 로고
    • Topological characteristics of helical repeat proteins
    • Groves MR and Barford D: Topological characteristics of helical repeat proteins. Curr Opin Struct Biol 1999, 9:383-389.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 383-389
    • Groves, M.R.1    Barford, D.2
  • 37
    • 0033534405 scopus 로고    scopus 로고
    • The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs
    • Groves MR, Hanlon N, Turowski P, Hemmings BA and Barford D: The structure of the protein phosphatase 2A PR65/A subunit reveals the conformation of its 15 tandemly repeated HEAT motifs. Cell 1999, 96:99-110.
    • (1999) Cell , vol.96 , pp. 99-110
    • Groves, M.R.1    Hanlon, N.2    Turowski, P.3    Hemmings, B.A.4    Barford, D.5
  • 38
    • 0029392854 scopus 로고
    • HEAT repeats in the Huntington's disease protein
    • Andrade MA and Bork P: HEAT repeats in the Huntington's disease protein. Nat Genet 1995, 11:115-116.
    • (1995) Nat. Genet. , vol.11 , pp. 115-116
    • Andrade, M.A.1    Bork, P.2
  • 39
    • 0028890381 scopus 로고
    • Saccharomyces cerevisiae kinesin- and dynein-related proteins required for anaphase chromosome segregation
    • Saunders WS, Koshland D, Eshel D, Gibbons IR and Hoyt MA: Saccharomyces cerevisiae kinesin- and dynein-related proteins required for anaphase chromosome segregation. J Cell Biol 1995, 128:617-624.
    • (1995) J. Cell Biol. , vol.128 , pp. 617-624
    • Saunders, W.S.1    Koshland, D.2    Eshel, D.3    Gibbons, I.R.4    Hoyt, M.A.5
  • 40
    • 0026728755 scopus 로고
    • Two Saccharomyces cerevisiae kinesin-related gene products required for mitotic spindle assembly
    • Hoyt MA, He L, Loo KK and Saunders WS: Two Saccharomyces cerevisiae kinesin-related gene products required for mitotic spindle assembly. J Cell Biol 1992, 118:109-120.
    • (1992) J. Cell Biol. , vol.118 , pp. 109-120
    • Hoyt, M.A.1    He, L.2    Loo, K.K.3    Saunders, W.S.4
  • 41
    • 0026638269 scopus 로고
    • Kinesin-related proteins required for structural integrity of the mitotic spindle
    • Saunders WS and Hoyt MA: Kinesin-related proteins required for structural integrity of the mitotic spindle. Cell 1992, 70:451-458.
    • (1992) Cell , vol.70 , pp. 451-458
    • Saunders, W.S.1    Hoyt, M.A.2
  • 43
    • 0034678076 scopus 로고    scopus 로고
    • Tubulin folding cofactor D is a microtubule destabilizing protein
    • Martin L, Fanarraga ML, Aloria K and Zabala JC: Tubulin folding cofactor D is a microtubule destabilizing protein. FEBS Lett 2000, 470:93-95.
    • (2000) FEBS Lett. , vol.470 , pp. 93-95
    • Martin, L.1    Fanarraga, M.L.2    Aloria, K.3    Zabala, J.C.4
  • 44
    • 0032478536 scopus 로고    scopus 로고
    • Structural diversity of leucine-rich repeat proteins
    • Kajava AV: Structural diversity of leucine-rich repeat proteins. J Mol Biol 1998, 277:519-527.
    • (1998) J. Mol. Biol. , vol.277 , pp. 519-527
    • Kajava, A.V.1
  • 47
    • 0037177814 scopus 로고    scopus 로고
    • Functional overlap between retinitis pigmentosa 2 protein and the tubulin-specific chaperone cofactor C
    • Bartolini F, Bhamidipati A, Thomas S, Schwahn U, Lewis SA and Cowan NJ: Functional overlap between retinitis pigmentosa 2 protein and the tubulin-specific chaperone cofactor C. J Biol Chem 2002, 277:14629-14634.
    • (2002) J. Biol. Chem. , vol.277 , pp. 14629-14634
    • Bartolini, F.1    Bhamidipati, A.2    Thomas, S.3    Schwahn, U.4    Lewis, S.A.5    Cowan, N.J.6
  • 48
    • 0029804024 scopus 로고    scopus 로고
    • Pat1: A topoisomerase II-associated protein required for faithful chromosome transmission in Saccharomyces cerevisiae
    • Wang X, Watt PM, Louis EJ, Borts RH and Hickson ID: Pat1: a topoisomerase II-associated protein required for faithful chromosome transmission in Saccharomyces cerevisiae. Nucleic Acids Res 1996, 24:4791-4797.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 4791-4797
    • Wang, X.1    Watt, P.M.2    Louis, E.J.3    Borts, R.H.4    Hickson, I.D.5
  • 49
    • 0035003652 scopus 로고    scopus 로고
    • Picture story. The great divide
    • Konforti B: Picture story. The great divide. Nat Struct Biol 2001, 8:488.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 488
    • Konforti, B.1
  • 51
    • 0033997036 scopus 로고    scopus 로고
    • Comparison of sequence profiles. Strategies for structural predictions using sequence information
    • Rychlewski L, Jaroszewski L, Li W and Godzik A: Comparison of sequence profiles. Strategies for structural predictions using sequence information. Protein Sci 2000, 9:232-241.
    • (2000) Protein Sci. , vol.9 , pp. 232-241
    • Rychlewski, L.1    Jaroszewski, L.2    Li, W.3    Godzik, A.4
  • 52
    • 0034780030 scopus 로고    scopus 로고
    • Pcons: A neural-network-based consensus predictor that improves fold recognition
    • Lundstrom J, Rychlewski L, Bujnicki J and Elofsson A: Pcons: a neural-network-based consensus predictor that improves fold recognition. Protein Sci 2001, 10:2354-2362.
    • (2001) Protein Sci. , vol.10 , pp. 2354-2362
    • Lundstrom, J.1    Rychlewski, L.2    Bujnicki, J.3    Elofsson, A.4
  • 53
    • 0033654768 scopus 로고    scopus 로고
    • Hybrid fold recognition: Combining sequence derived properties with evolutionary information
    • Fischer D: Hybrid fold recognition: combining sequence derived properties with evolutionary information. Pac Symp Biocomput 2000:119-130.
    • (2000) Pac. Symp. Biocomput. , pp. 119-130
    • Fischer, D.1
  • 54
    • 0033537993 scopus 로고    scopus 로고
    • GenTHREADER: An efficient and reliable protein fold recognition method for genomic sequences
    • Jones DT: GenTHREADER: an efficient and reliable protein fold recognition method for genomic sequences. J Mol Biol 1999, 287:797-815.
    • (1999) J. Mol. Biol. , vol.287 , pp. 797-815
    • Jones, D.T.1
  • 55
    • 0032438987 scopus 로고    scopus 로고
    • Hidden Markov models for detecting remote protein homologies
    • Karplus K, Barrett C and Hughey R: Hidden Markov models for detecting remote protein homologies. Bioinformatics 1998, 14:846-856.
    • (1998) Bioinformatics , vol.14 , pp. 846-856
    • Karplus, K.1    Barrett, C.2    Hughey, R.3
  • 56
    • 0034595501 scopus 로고    scopus 로고
    • Enhanced genome annotation using structural profiles in the program 3DPSSM
    • Kelley LA, MacCallum RM and Sternberg MJ: Enhanced genome annotation using structural profiles in the program 3DPSSM. J Mol Biol 2000, 299:499-520.
    • (2000) J. Mol. Biol. , vol.299 , pp. 499-520
    • Kelley, L.A.1    MacCallum, R.M.2    Sternberg, M.J.3
  • 57
    • 0035967880 scopus 로고    scopus 로고
    • FUGUE: Sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties
    • Shi J, Blundell TL and Mizuguchi K: FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J Mol Biol 2001, 310:243-257.
    • (2001) J. Mol. Biol. , vol.310 , pp. 243-257
    • Shi, J.1    Blundell, T.L.2    Mizuguchi, K.3
  • 59
    • 0035698724 scopus 로고    scopus 로고
    • LiveBench-2: Large-scale automated evaluation of protein structure prediction servers
    • Bujnicki JM, Elofsson A, Fischer D and Rychlewski L: LiveBench-2: large-scale automated evaluation of protein structure prediction servers. Proteins 2001, Suppl 5:184-191.
    • (2001) Proteins , Issue.SUPPL. 5 , pp. 184-191
    • Bujnicki, J.M.1    Elofsson, A.2    Fischer, D.3    Rychlewski, L.4
  • 60
    • 0037880509 scopus 로고    scopus 로고
    • The 2002 olympic games of protein structure prediction
    • Fischer D and Rychlewski L: The 2002 olympic games of protein structure prediction. Protein Eng 2003, 16:157-160.
    • (2003) Protein Eng. , vol.16 , pp. 157-160
    • Fischer, D.1    Rychlewski, L.2
  • 61
    • 0025398721 scopus 로고
    • WHAT IF: A molecular modeling and drug design program
    • 29
    • Vriend G: WHAT IF: a molecular modeling and drug design program. J Mol Graph 1990, 8:52-6, 29.
    • (1990) J. Mol. Graph. , vol.8 , pp. 52-56
    • Vriend, G.1
  • 62
    • 0034974205 scopus 로고    scopus 로고
    • Design and implementation of a collaborative molecular graphics environment
    • 280-7
    • Tate JG, Moreland JL and Bourne PE: Design and implementation of a collaborative molecular graphics environment. J Mol Graph Model 2001, 19:280-7, 369-73.
    • (2001) J. Mol. Graph Model , vol.19 , pp. 369-373
    • Tate, J.G.1    Moreland, J.L.2    Bourne, P.E.3
  • 63
    • 0034924493 scopus 로고    scopus 로고
    • SWISS-PROT: Connecting biomolecular knowledge via a protein database
    • Gasteiger E, Jung E and Bairoch A: SWISS-PROT: connecting biomolecular knowledge via a protein database. Curr Issues Mol Biol 2001, 3:47-55.
    • (2001) Curr. Issues Mol. Biol. , vol.3 , pp. 47-55
    • Gasteiger, E.1    Jung, E.2    Bairoch, A.3
  • 64
    • 0036169928 scopus 로고    scopus 로고
    • Tolerating some redundancy significantly speeds up clustering of large protein databases
    • Li W, Jaroszewski L and Godzik A: Tolerating some redundancy significantly speeds up clustering of large protein databases. Bioinformatics 2002, 18:77-82.
    • (2002) Bioinformatics , vol.18 , pp. 77-82
    • Li, W.1    Jaroszewski, L.2    Godzik, A.3
  • 65
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG and Gibson TJ: CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994, 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 66
    • 0033588274 scopus 로고    scopus 로고
    • Structures of two repeats of spectrin suggest models of flexibility
    • Grum VL, Li D, MacDonald RI and Mondragon A: Structures of two repeats of spectrin suggest models of flexibility. Cell 1999, 98:523-535.
    • (1999) Cell , vol.98 , pp. 523-535
    • Grum, V.L.1    Li, D.2    MacDonald, R.I.3    Mondragon, A.4
  • 67
    • 2942605884 scopus 로고    scopus 로고
    • Crystal Structure of the Actin-Binding Domain of Cyclase Associated Protein (CAP) from Saccharomyces Cerevisiae
    • to be published
    • Roswarski DA, Fedorov AA, Dodatko T and Almo SC: Crystal Structure of the Actin-Binding Domain of Cyclase Associated Protein (CAP) from Saccharomyces Cerevisiae. to be published.
    • Roswarski, D.A.1    Fedorov, A.A.2    Dodatko, T.3    Almo, S.C.4
  • 68
    • 0034646565 scopus 로고    scopus 로고
    • Structural basis of recognition of monopartite and bipartite nuclear localization sequences by mammalian importin-alpha
    • Fontes MR, Teh T and Kobe B: Structural basis of recognition of monopartite and bipartite nuclear localization sequences by mammalian importin-alpha. J Mol Biol 2000, 297:1183-1194.
    • (2000) J. Mol. Biol. , vol.297 , pp. 1183-1194
    • Fontes, M.R.1    Teh, T.2    Kobe, B.3
  • 69
    • 0001506297 scopus 로고    scopus 로고
    • Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp
    • Chook YM and Blobel G: Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp. Nature 1999, 399:230-237.
    • (1999) Nature , vol.399 , pp. 230-237
    • Chook, Y.M.1    Blobel, G.2
  • 70
    • 2942574431 scopus 로고    scopus 로고
    • Solution Structure of the CAP-Gly Domain from Human Cylindromatosis Tumour-Suppressor Cyld
    • to be published
    • Saito K, Koshiba S, Kigawa T and Yokoyama S: Solution Structure of the CAP-Gly Domain from Human Cylindromatosis Tumour-Suppressor Cyld. to be published .
    • Saito, K.1    Koshiba, S.2    Kigawa, T.3    Yokoyama, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.