메뉴 건너뛰기




Volumn 109, Issue 50, 2012, Pages

Structure of the formin-interaction domain of the actin nucleation-promoting factor Bud6

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; BUD6 PROTEIN; DIMER; G ACTIN; PROTEIN; UNCLASSIFIED DRUG;

EID: 84870875953     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1203035109     Document Type: Article
Times cited : (28)

References (63)
  • 1
    • 60749122102 scopus 로고    scopus 로고
    • Actin nucleation and elongation factors: Mechanisms and interplay
    • Chesarone MA, Goode BL (2009) Actin nucleation and elongation factors: Mechanisms and interplay. Curr Opin Cell Biol 21(1):28-37.
    • (2009) Curr Opin Cell Biol , vol.21 , Issue.1 , pp. 28-37
    • Chesarone, M.A.1    Goode, B.L.2
  • 2
    • 70450245305 scopus 로고    scopus 로고
    • Actin filament nucleation and elongation factors - Structure-function relationships
    • Dominguez R (2009) Actin filament nucleation and elongation factors - Structure-function relationships. Crit Rev Biochem Mol Biol 44(6):351-366.
    • (2009) Crit Rev Biochem Mol Biol , vol.44 , Issue.6 , pp. 351-366
    • Dominguez, R.1
  • 3
    • 77949834455 scopus 로고    scopus 로고
    • A nucleator arms race: Cellular control of actin assembly
    • Campellone KG, Welch MD (2010) A nucleator arms race: Cellular control of actin assembly. Nat Rev Mol Cell Biol 11(4):237-251.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , Issue.4 , pp. 237-251
    • Campellone, K.G.1    Welch, M.D.2
  • 4
    • 34248154652 scopus 로고    scopus 로고
    • Mechanism and function of formins in the control of actin assembly
    • Goode BL, Eck MJ (2007) Mechanism and function of formins in the control of actin assembly. Annu Rev Biochem 76:593-627.
    • (2007) Annu Rev Biochem , vol.76 , pp. 593-627
    • Goode, B.L.1    Eck, M.J.2
  • 5
    • 0034896467 scopus 로고    scopus 로고
    • Thermodynamics and kinetics of actin filament nucleation
    • Sept D, McCammon JA (2001) Thermodynamics and kinetics of actin filament nucleation. Biophys J 81(2):667-674. (Pubitemid 32721442)
    • (2001) Biophysical Journal , vol.81 , Issue.2 , pp. 667-674
    • Sept, D.1    McCammon, J.A.2
  • 8
    • 80051977000 scopus 로고    scopus 로고
    • Structural and biochemical characterization of two binding sites for nucleation-promoting factor WASp-VCA on Arp2/3 complex
    • Ti SC, Jurgenson CT, Nolen BJ, Pollard TD (2011) Structural and biochemical characterization of two binding sites for nucleation-promoting factor WASp-VCA on Arp2/3 complex. Proc Natl Acad Sci USA 108(33):E463-E471.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.33
    • Ti, S.C.1    Jurgenson, C.T.2    Nolen, B.J.3    Pollard, T.D.4
  • 11
    • 72949110575 scopus 로고    scopus 로고
    • Unleashing formins to remodel the actin and microtubule cytoskeletons
    • Chesarone MA, DuPage AG, Goode BL (2010) Unleashing formins to remodel the actin and microtubule cytoskeletons. Nat Rev Mol Cell Biol 11(1):62-74.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , Issue.1 , pp. 62-74
    • Chesarone, M.A.1    DuPage, A.G.2    Goode, B.L.3
  • 12
    • 1542269073 scopus 로고    scopus 로고
    • Crystal structures of a formin homology-2 domain reveal a tethered dimer architecture
    • DOI 10.1016/S0092-8674(04)00210-7, PII S0092867404002107
    • Xu Y, et al. (2004) Crystal structures of a Formin Homology-2 domain reveal a tethered dimer architecture. Cell 116(5):711-723. (Pubitemid 38326729)
    • (2004) Cell , vol.116 , Issue.5 , pp. 711-723
    • Xu, Y.1    Moseley, J.B.2    Sagot, I.3    Poy, F.4    Pellman, D.5    Goode, B.L.6    Eck, M.J.7
  • 13
    • 13444280218 scopus 로고    scopus 로고
    • Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain
    • DOI 10.1038/nature03251
    • Otomo T, et al. (2005) Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain. Nature 433(7025):488-494. (Pubitemid 40204299)
    • (2005) Nature , vol.433 , Issue.7025 , pp. 488-494
    • Otomo, T.1    Tomchick, D.R.2    Otomo, C.3    Panchal, S.C.4    Machius, M.5    Rosen, M.K.6
  • 14
    • 78650988290 scopus 로고    scopus 로고
    • Rotational movement of the formin mDia1 along the double helical strand of an actin filament
    • Mizuno H, et al. (2011) Rotational movement of the formin mDia1 along the double helical strand of an actin filament. Science 331(6013):80-83.
    • (2011) Science , vol.331 , Issue.6013 , pp. 80-83
    • Mizuno, H.1
  • 15
    • 31044433924 scopus 로고    scopus 로고
    • Control of the assembly of ATP- and ADP-actin by formins and profilin
    • DOI 10.1016/j.cell.2005.11.038, PII S009286740501398X
    • Kovar DR, Harris ES, Mahaffy R, Higgs HN, Pollard TD (2006) Control of the assembly of ATP- and ADP-actin by formins and profilin. Cell 124(2):423-435. (Pubitemid 43121988)
    • (2006) Cell , vol.124 , Issue.2 , pp. 423-435
    • Kovar, D.R.1    Harris, E.S.2    Mahaffy, R.3    Higgs, H.N.4    Pollard, T.D.5
  • 16
    • 31044443763 scopus 로고    scopus 로고
    • Model of formin-associated actin filament elongation
    • DOI 10.1016/j.molcel.2006.01.016, PII S1097276506000384
    • Vavylonis D, Kovar DR, O'Shaughnessy B, Pollard TD (2006) Model of formin-associated actin filament elongation. Mol Cell 21(4):455-466. (Pubitemid 43228002)
    • (2006) Molecular Cell , vol.21 , Issue.4 , pp. 455-466
    • Vavylonis, D.1    Kovar, D.R.2    O'Shaughnessy, B.3    Pollard, T.D.4
  • 17
    • 0037458002 scopus 로고    scopus 로고
    • Mechanism of formin-induced nucleation of actin filaments
    • DOI 10.1021/bi026520j
    • Pring M, Evangelista M, Boone C, Yang C, Zigmond SH (2003) Mechanism of formin-induced nucleation of actin filaments. Biochemistry 42(2):486-496. (Pubitemid 36105767)
    • (2003) Biochemistry , vol.42 , Issue.2 , pp. 486-496
    • Pring, M.1    Evangelista, M.2    Boone, C.3    Yang, C.4    Zigmond, S.H.5
  • 18
    • 79952363769 scopus 로고    scopus 로고
    • The formin DAD domain plays dual roles in autoinhibition and actin nucleation
    • Gould CJ, et al. (2011) The formin DAD domain plays dual roles in autoinhibition and actin nucleation. Curr Biol 21(5):384-390.
    • (2011) Curr Biol , vol.21 , Issue.5 , pp. 384-390
    • Gould, C.J.1
  • 19
    • 33748745132 scopus 로고    scopus 로고
    • INF2 is a WASP homology 2 motif-containing formin that severs actin filaments and accelerates both polymerization and depolymerization
    • DOI 10.1074/jbc.M604666200
    • Chhabra ES, Higgs HN (2006) INF2 Is a WASP homology 2 motif-containing formin that severs actin filaments and accelerates both polymerization and depolymerization. J Biol Chem 9(36):26754-26767. (Pubitemid 44401884)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.36 , pp. 26754-26767
    • Chhabra, E.S.1    Higgs, H.N.2
  • 20
    • 84856279315 scopus 로고    scopus 로고
    • The C terminus of formin FMNL3 accelerates actin polymerization and contains a WH2 domain-like sequence that binds both monomers and filament barbed ends
    • Heimsath EG, Jr., Higgs HN (2012) The C terminus of formin FMNL3 accelerates actin polymerization and contains a WH2 domain-like sequence that binds both monomers and filament barbed ends. J Biol Chem 287(5):3087-3098.
    • (2012) J Biol Chem , vol.287 , Issue.5 , pp. 3087-3098
    • Heimsath Jr., E.G.1    Higgs, H.N.2
  • 21
    • 35349021033 scopus 로고    scopus 로고
    • Regulatory interactions between two actin nucleators, Spire and Cappuccino
    • DOI 10.1083/jcb.200706196
    • Quinlan ME, Hilgert S, Bedrossian A, Mullins RD, Kerkhoff E (2007) Regulatory interactions between two actin nucleators, Spire and Cappuccino. J Cell Biol 179(1):117-128. (Pubitemid 47606688)
    • (2007) Journal of Cell Biology , vol.179 , Issue.1 , pp. 117-128
    • Quinlan, M.E.1    Hilgert, S.2    Bedrossian, A.3    Mullins, R.D.4    Kerkhoff, E.5
  • 22
    • 77954422924 scopus 로고    scopus 로고
    • Adenomatous polyposis coli protein nucleates actin assembly and synergizes with the formin mDia1
    • Okada K, et al. (2010) Adenomatous polyposis coli protein nucleates actin assembly and synergizes with the formin mDia1. J Cell Biol 189(7):1087-1096.
    • (2010) J Cell Biol , vol.189 , Issue.7 , pp. 1087-1096
    • Okada, K.1
  • 24
    • 0030989560 scopus 로고    scopus 로고
    • Aip3p/bud6p, a yeast actin-interacting protein that is involved in morphogenesis and the selection of bipolar budding sites
    • Amberg DC, Zahner JE, Mulholland JW, Pringle JR, Botstein D (1997) Aip3p/Bud6p, a yeast actin-interacting protein that is involved in morphogenesis and the selection of bipolar budding sites. Mol Biol Cell 8(4):729-753. (Pubitemid 27176179)
    • (1997) Molecular Biology of the Cell , vol.8 , Issue.4 , pp. 729-753
    • Amberg, D.C.1    Zahner, J.E.2    Mulholland, J.W.3    Pringle, J.R.4    Botstein, D.5
  • 25
    • 2942668708 scopus 로고    scopus 로고
    • Regulation of a formin complex by the microtubule plus end protein tea1p
    • DOI 10.1083/jcb.200403090
    • Feierbach B, Verde F, Chang F (2004) Regulation of a formin complex by the microtubule plus end protein tea1p. J Cell Biol 165(5):697-707. (Pubitemid 38765771)
    • (2004) Journal of Cell Biology , vol.165 , Issue.5 , pp. 697-707
    • Feierbach, B.1    Verde, F.2    Chang, F.3
  • 26
    • 22344453326 scopus 로고    scopus 로고
    • Septin-dependent compartmentalization of the endoplasmic reticulum during yeast polarized growth
    • DOI 10.1083/jcb.200412143
    • Luedeke C, et al. (2005) Septin-dependent compartmentalization of the endoplasmic reticulum during yeast polarized growth. J Cell Biol 169(6):897-908. (Pubitemid 41002866)
    • (2005) Journal of Cell Biology , vol.169 , Issue.6 , pp. 897-908
    • Luedeke, C.1    Frei, S.B.2    Sbalzarini, I.3    Schwarz, H.4    Spang, A.5    Barral, Y.6
  • 27
    • 49649106438 scopus 로고    scopus 로고
    • A mechanism for asymmetric segregation of age during yeast budding
    • Shcheprova Z, Baldi S, Frei SB, Gonnet G, Barral Y (2008) A mechanism for asymmetric segregation of age during yeast budding. Nature 454(7205):728-734.
    • (2008) Nature , vol.454 , Issue.7205 , pp. 728-734
    • Shcheprova, Z.1    Baldi, S.2    Frei, S.B.3    Gonnet, G.4    Barral, Y.5
  • 28
    • 0033996103 scopus 로고    scopus 로고
    • The secretory pathway mediates localization of the cell polarity regulator Aip3p/Bud6p
    • Jin H, Amberg DC (2000) The secretory pathway mediates localization of the cell polarity regulator Aip3p/Bud6p. Mol Biol Cell 11(2):647-661. (Pubitemid 30112172)
    • (2000) Molecular Biology of the Cell , vol.11 , Issue.2 , pp. 647-661
    • Jin, H.1    Amberg, D.C.2
  • 29
    • 59549103134 scopus 로고    scopus 로고
    • Dissecting the involvement of formins in Bud6p-mediated cortical capture of microtubules in S. cerevisiae
    • Delgehyr N, Lopes CS, Moir CA, Huisman SM, Segal M (2008) Dissecting the involvement of formins in Bud6p-mediated cortical capture of microtubules in S. cerevisiae. J Cell Sci 121(Pt 22):3803-3814.
    • (2008) J Cell Sci , vol.121 , Issue.PART 22 , pp. 3803-3814
    • Delgehyr, N.1    Lopes, C.S.2    Moir, C.A.3    Huisman, S.M.4    Segal, M.5
  • 30
    • 80655149440 scopus 로고    scopus 로고
    • Mechanism and cellular function of Bud6 as an actin nucleation-promoting factor
    • Graziano BR, et al. (2011) Mechanism and cellular function of Bud6 as an actin nucleation-promoting factor. Mol Biol Cell 22(21):4016-4028.
    • (2011) Mol Biol Cell , vol.22 , Issue.21 , pp. 4016-4028
    • Graziano, B.R.1
  • 31
    • 23044510466 scopus 로고    scopus 로고
    • Differential activities and regulation of Saccharomyces cerevisiae formin proteins Bni1 and Bnr1 by Bud6
    • DOI 10.1074/jbc.M503094200
    • Moseley JB, Goode BL (2005) Differential activities and regulation of Saccharomyces cerevisiae formin proteins Bni1 and Bnr1 by Bud6. J Biol Chem 280(30):28023-28033. (Pubitemid 41076920)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.30 , pp. 28023-28033
    • Moseley, J.B.1    Goode, B.L.2
  • 32
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • DOI 10.1006/jmbi.1993.1489
    • Holm L, Sander C (1993) Protein structure comparison by alignment of distance matrices. J Mol Biol 233(1):123-138. (Pubitemid 23288916)
    • (1993) Journal of Molecular Biology , vol.233 , Issue.1 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 34
    • 0035252931 scopus 로고    scopus 로고
    • Coiled coils: A highly versatile protein folding motif
    • DOI 10.1016/S0962-8924(00)01898-5, PII S0962892400018985
    • Burkhard P, Stetefeld J, Strelkov SV (2001) Coiled coils: A highly versatile protein folding motif. Trends Cell Biol 11(2):82-88. (Pubitemid 32144755)
    • (2001) Trends in Cell Biology , vol.11 , Issue.2 , pp. 82-88
    • Burkhard, P.1    Stetefeld, J.2    Strelkov, S.V.3
  • 35
    • 0035853291 scopus 로고    scopus 로고
    • SOCKET: A program for identifying and analysing coiled-coil motifs within protein structures
    • DOI 10.1006/jmbi.2001.4545
    • Walshaw J, Woolfson DN (2001) Socket: A program for identifying and analysing coiled-coil motifs within protein structures. J Mol Biol 307(5):1427-1450. (Pubitemid 33027651)
    • (2001) Journal of Molecular Biology , vol.307 , Issue.5 , pp. 1427-1450
    • Walshaw, J.1    Woolfson, D.N.2
  • 36
    • 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, Gibson TJ (1994) CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22(22):4673-4680. (Pubitemid 24354800)
    • (1994) Nucleic Acids Research , vol.22 , Issue.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 37
    • 77954257799 scopus 로고    scopus 로고
    • ConSurf 2010: Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids
    • Ashkenazy H, Erez E, Martz E, Pupko T, Ben-Tal N (2010) ConSurf 2010: Calculating evolutionary conservation in sequence and structure of proteins and nucleic acids. Nucleic Acids Res 38(Web Server issue):W529-W533.
    • (2010) Nucleic Acids Res , vol.38 , Issue.WEB SERVER ISSUE
    • Ashkenazy, H.1    Erez, E.2    Martz, E.3    Pupko, T.4    Ben-Tal, N.5
  • 39
    • 55549131537 scopus 로고    scopus 로고
    • The Diaphanous-related Formin FHOD1 associates with ROCK1 and promotes Src-dependent plasma membrane blebbing
    • Hannemann S, et al. (2008) The Diaphanous-related Formin FHOD1 associates with ROCK1 and promotes Src-dependent plasma membrane blebbing. J Biol Chem 283 (41):27891-27903.
    • (2008) J Biol Chem , vol.283 , Issue.41 , pp. 27891-27903
    • Hannemann, S.1
  • 40
    • 79952836685 scopus 로고    scopus 로고
    • Crystal structure of a coiled-coil domain from human ROCK I
    • Tu D, et al. (2011) Crystal structure of a coiled-coil domain from human ROCK I. PLoS ONE 6(3):e18080.
    • (2011) PLoS ONE , vol.6 , Issue.3
    • Tu, D.1
  • 42
    • 0036144567 scopus 로고    scopus 로고
    • Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast
    • DOI 10.1038/ncb718
    • Evangelista M, Pruyne D, Amberg DC, Boone C, Bretscher A (2002) Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast. Nat Cell Biol 4(1):32-41. (Pubitemid 34071978)
    • (2002) Nature Cell Biology , vol.4 , Issue.1 , pp. 32-41
    • Evangelista, M.1    Pruyne, D.2    Amberg, D.C.3    Boone, C.4    Bretscher, A.5
  • 43
    • 66349133039 scopus 로고    scopus 로고
    • New players in actin polymerization - WH2-domain-containing actin nucleators
    • Qualmann B, Kessels MM (2009) New players in actin polymerization - WH2-domain-containing actin nucleators. Trends Cell Biol 19(6):276-285.
    • (2009) Trends Cell Biol , vol.19 , Issue.6 , pp. 276-285
    • Qualmann, B.1    Kessels, M.M.2
  • 44
    • 55049090663 scopus 로고    scopus 로고
    • Hierarchical regulation of WASP/WAVE proteins
    • Padrick SB, et al. (2008) Hierarchical regulation of WASP/WAVE proteins. Mol Cell 32(3):426-438.
    • (2008) Mol Cell , vol.32 , Issue.3 , pp. 426-438
    • Padrick, S.B.1
  • 46
    • 84858967947 scopus 로고    scopus 로고
    • Multiple forms of Spire-actin complexes and their functional consequences
    • Chen CK, Sawaya MR, Phillips ML, Reisler E, Quinlan ME (2012) Multiple forms of Spire-actin complexes and their functional consequences. J Biol Chem 287(13):10684-10692.
    • (2012) J Biol Chem , vol.287 , Issue.13 , pp. 10684-10692
    • Chen, C.K.1    Sawaya, M.R.2    Phillips, M.L.3    Reisler, E.4    Quinlan, M.E.5
  • 47
    • 34848873760 scopus 로고    scopus 로고
    • Capu and Spire Assemble a Cytoplasmic Actin Mesh that Maintains Microtubule Organization in the Drosophila Oocyte
    • DOI 10.1016/j.devcel.2007.09.003, PII S1534580707003437
    • Dahlgaard K, Raposo AA, Niccoli T, St Johnston D (2007) Capu and Spire assemble a cytoplasmic actin mesh that maintains microtubule organization in the Drosophila oocyte. Dev Cell 13(4):539-553. (Pubitemid 47500810)
    • (2007) Developmental Cell , vol.13 , Issue.4 , pp. 539-553
    • Dahlgaard, K.1    Raposo, A.A.S.F.2    Niccoli, T.3    St, J.D.4
  • 48
    • 67650757497 scopus 로고    scopus 로고
    • A novel role for an APC2-Diaphanous complex in regulating actin organization in Drosophila
    • Webb RL, Zhou MN, McCartney BM (2009) A novel role for an APC2-Diaphanous complex in regulating actin organization in Drosophila. Development 136(8):1283-1293.
    • (2009) Development , vol.136 , Issue.8 , pp. 1283-1293
    • Webb, R.L.1    Zhou, M.N.2    McCartney, B.M.3
  • 49
    • 84861196154 scopus 로고    scopus 로고
    • Stabilization of actin filaments prevents germinal vesicle breakdown and affects microtubule organization in Xenopus oocytes
    • Okada I, Fujiki S, Iwase S, Abe H (2012) Stabilization of actin filaments prevents germinal vesicle breakdown and affects microtubule organization in Xenopus oocytes. Cytoskeleton (Hoboken) 69(5):312-323.
    • (2012) Cytoskeleton (Hoboken) , vol.69 , Issue.5 , pp. 312-323
    • Okada, I.1    Fujiki, S.2    Iwase, S.3    Abe, H.4
  • 50
    • 84861708449 scopus 로고    scopus 로고
    • Rocket launcher mechanism of collaborative actin assembly defined by single-molecule imaging
    • Breitsprecher D, et al. (2012) Rocket launcher mechanism of collaborative actin assembly defined by single-molecule imaging. Science 336(6085):1164-1168.
    • (2012) Science , vol.336 , Issue.6085 , pp. 1164-1168
    • Breitsprecher, D.1
  • 52
    • 0015218407 scopus 로고
    • The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin
    • Spudich JA, Watt S (1971) The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin. J Biol Chem 246(15):4866-4871.
    • (1971) J Biol Chem , vol.246 , Issue.15 , pp. 4866-4871
    • Spudich, J.A.1    Watt, S.2
  • 53
    • 0033576288 scopus 로고    scopus 로고
    • Influence of the C terminus of Wiskott-Aldrich syndrome protein (WASp) and the Arp2/3 complex on actin polymerization
    • Higgs HN, Blanchoin L, Pollard TD (1999) Influence of the C terminus of Wiskott-Aldrich syndrome protein (WASp) and the Arp2/3 complex on actin polymerization. Biochemistry 38(46):15212-15222. (Pubitemid 129520352)
    • (1999) Biochemistry , vol.38 , Issue.46 , pp. 15212-15222
    • Higgs, H.N.1    Blanchoin, L.2    Pollard, T.D.3
  • 54
    • 0020012723 scopus 로고
    • Methods to characterize actin filament networks
    • Pollard TD, Cooper JA (1982) Methods to characterize actin filament networks. Methods Enzymol 85 Pt B:211-233.
    • (1982) Methods Enzymol , vol.85 , Issue.PART B , pp. 211-233
    • Pollard, T.D.1    Cooper, J.A.2
  • 55
    • 32144457693 scopus 로고    scopus 로고
    • Formin proteins: Purification and measurement of effects on actin assembly
    • DOI 10.1016/S0076-6879(06)06016-2, PII S0076687906060162, 16, Regulators and Effectors of Small GTPases: Rho Family
    • Moseley JB, Maiti S, Goode BL (2006) Formin proteins: purification and measurement of effects on actin assembly. Methods Enzymol 406:215-234. (Pubitemid 43207442)
    • (2006) Methods in Enzymology , vol.406 , pp. 215-234
    • Moseley, J.B.1    Maiti, S.2    Goode, B.L.3
  • 56
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276:307-326. (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 57
    • 36549027357 scopus 로고    scopus 로고
    • Automated structure solution with autoSHARP
    • DOI 10.1385/1-59745-266-1:215, Macromolecular Crystallography Protocols, Volume 2: Structure Determination
    • Vonrhein C, Blanc E, Roversi P, Bricogne G (2007) Automated structure solution with autoSHARP. Methods Mol Biol 364:215-230. (Pubitemid 350183137)
    • (2007) Methods in Molecular Biology , vol.364 , pp. 215-230
    • Vonrhein, C.1    Blanc, E.2    Roversi, P.3    Bricogne, G.4
  • 58
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley P, Cowtan K (2004) Coot: Model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60(Pt 12 Pt 1):2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , Issue.PART 12 PART 1 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 59
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the Crystallography and NMR system
    • Brunger AT (2007) Version 1.2 of the Crystallography and NMR system. Nat Protoc 2(11):2728-2733.
    • (2007) Nat Protoc , vol.2 , Issue.11 , pp. 2728-2733
    • Brunger, A.T.1
  • 61
    • 0347383760 scopus 로고    scopus 로고
    • ARP/wARP and Automatic Interpretation of Protein Electron Density Maps
    • DOI 10.1016/S0076-6879(03)74011-7
    • Morris RJ, Perrakis A, Lamzin VS (2003) ARP/wARP and automatic interpretation of protein electron density maps. Methods Enzymol 374:229-244. (Pubitemid 37531812)
    • (2003) Methods in Enzymology , vol.374 , pp. 229-244
    • Morris, R.J.1    Perrakis, A.2    Lamzin, V.S.3
  • 62
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD, et al. (2010) PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66(Pt 2):213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , Issue.PART 2 , pp. 213-221
    • Adams, P.D.1
  • 63
    • 32144447240 scopus 로고    scopus 로고
    • Biochemical analysis of mammalian formin effects on actin dynamics
    • DOI 10.1016/S0076-6879(06)06015-0, PII S0076687906060150, 15, Regulators and Effectors of Small GTPases: Rho Family
    • Harris ES, Higgs HN (2006) Biochemical analysis of mammalian formin effects on actin dynamics. Methods Enzymol 406:190-214. (Pubitemid 43207441)
    • (2006) Methods in Enzymology , vol.406 , pp. 190-214
    • Harris, E.S.1    Higgs, H.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.