메뉴 건너뛰기




Volumn 25, Issue 2, 2018, Pages 139-146

Cryo-EM structure of the exocyst complex

Author keywords

[No Author keywords available]

Indexed keywords

EXOCYST; SACCHAROMYCES CEREVISIAE PROTEIN; CROSS LINKING REAGENT; PROTEIN BINDING; VESICULAR TRANSPORT PROTEIN;

EID: 85042767185     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/s41594-017-0016-2     Document Type: Article
Times cited : (111)

References (74)
  • 1
    • 0033130103 scopus 로고    scopus 로고
    • Transport-vesicle targeting: Tethers before SNAREs
    • Pfeffer, S. R. Transport-vesicle targeting: tethers before SNAREs. Nat. Cell. Biol. 1, E17-E22 (1999).
    • (1999) Nat. Cell. Biol. , vol.1 , pp. E17-E22
    • Pfeffer, S.R.1
  • 3
    • 0036629335 scopus 로고    scopus 로고
    • Vesicle tethering complexes in membrane traffic
    • Whyte, J. R. & Munro, S. Vesicle tethering complexes in membrane traffic. J. Cell. Sci. 115, 2627-2637 (2002).
    • (2002) J. Cell. Sci. , vol.115 , pp. 2627-2637
    • Whyte, J.R.1    Munro, S.2
  • 4
    • 33644816187 scopus 로고    scopus 로고
    • Role of tethering factors in secretory membrane traffic
    • Sztul, E. & Lupashin, V. Role of tethering factors in secretory membrane traffic. Am. J. Physiol. Cell. Physiol. 290, C11-C26 (2006).
    • (2006) Am. J. Physiol. Cell. Physiol. , vol.290 , pp. C11-C26
    • Sztul, E.1    Lupashin, V.2
  • 5
    • 78049368534 scopus 로고    scopus 로고
    • Tethering factors as organizers of intracellular vesicular traffic
    • Yu, I. M. & Hughson, F. M. Tethering factors as organizers of intracellular vesicular traffic. Annu. Rev. Cell. Dev. Biol. 26, 137-156 (2010).
    • (2010) Annu. Rev. Cell. Dev. Biol. , vol.26 , pp. 137-156
    • Yu, I.M.1    Hughson, F.M.2
  • 6
    • 78149306025 scopus 로고    scopus 로고
    • Multisubunit tethering complexes and their role in membrane fusion
    • Bröcker, C., Engelbrecht-Vandré, S. & Ungermann, C. Multisubunit tethering complexes and their role in membrane fusion. Curr. Biol. 20, R943-R952 (2010).
    • (2010) Curr. Biol. , vol.20 , pp. R943-R952
    • Bröcker, C.1    Engelbrecht-Vandré, S.2    Ungermann, C.3
  • 7
    • 0029045404 scopus 로고
    • Sec6, Sec8, and Sec15 are components of a multisubunit complex which localizes to small bud tips in Saccharomyces cerevisiae
    • TerBush, D. R. & Novick, P. Sec6, Sec8, and Sec15 are components of a multisubunit complex which localizes to small bud tips in Saccharomyces cerevisiae. J. Cell. Biol. 130, 299-312 (1995).
    • (1995) J. Cell. Biol. , vol.130 , pp. 299-312
    • TerBush, D.R.1    Novick, P.2
  • 8
    • 0029843493 scopus 로고    scopus 로고
    • The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae
    • TerBush, D. R., Maurice, T., Roth, D. & Novick, P. The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae. EMBO J. 15, 6483-6494 (1996).
    • (1996) EMBO J. , vol.15 , pp. 6483-6494
    • TerBush, D.R.1    Maurice, T.2    Roth, D.3    Novick, P.4
  • 9
    • 67949106616 scopus 로고    scopus 로고
    • The exocyst complex in polarized exocytosis
    • He, B. & Guo, W. The exocyst complex in polarized exocytosis. Curr. Opin. Cell. Biol. 21, 537-542 (2009).
    • (2009) Curr. Opin. Cell. Biol. , vol.21 , pp. 537-542
    • He, B.1    Guo, W.2
  • 10
    • 84939543428 scopus 로고    scopus 로고
    • The exocyst at a glance
    • Wu, B. & Guo, W. The exocyst at a glance. J. Cell. Sci. 128, 2957-2964 (2015).
    • (2015) J. Cell. Sci. , vol.128 , pp. 2957-2964
    • Wu, B.1    Guo, W.2
  • 11
    • 85010423721 scopus 로고    scopus 로고
    • Sec3 promotes the initial binary t-SNARE complex assembly and membrane fusion
    • Yue, P. et al. Sec3 promotes the initial binary t-SNARE complex assembly and membrane fusion. Nat. Commun. 8, 14236 (2017).
    • (2017) Nat. Commun. , vol.8 , pp. 14236
    • Yue, P.1
  • 12
    • 84862268931 scopus 로고    scopus 로고
    • Exorcising the exocyst complex
    • Heider, M. R. & Munson, M. Exorcising the exocyst complex. Traffic 13, 898-907 (2012).
    • (2012) Traffic , vol.13 , pp. 898-907
    • Heider, M.R.1    Munson, M.2
  • 13
    • 33745841364 scopus 로고    scopus 로고
    • The exocyst defrocked, a framework of rods revealed
    • Munson, M. & Novick, P. The exocyst defrocked, a framework of rods revealed. Nat. Struct. Mol. Biol. 13, 577-581 (2006).
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 577-581
    • Munson, M.1    Novick, P.2
  • 14
    • 0032904433 scopus 로고    scopus 로고
    • Targeting vesicles to specific sites on the plasma membrane: The role of the sec6/8 complex
    • Hsu, S. C., Hazuka, C. D., Foletti, D. L. & Scheller, R. H. Targeting vesicles to specific sites on the plasma membrane: the role of the sec6/8 complex. Trends Cell. Biol. 9, 150-153 (1999).
    • (1999) Trends Cell. Biol. , vol.9 , pp. 150-153
    • Hsu, S.C.1    Hazuka, C.D.2    Foletti, D.L.3    Scheller, R.H.4
  • 15
    • 84954386257 scopus 로고    scopus 로고
    • Subunit connectivity, assembly determinants and architecture of the yeast exocyst complex
    • Heider, M. R. et al. Subunit connectivity, assembly determinants and architecture of the yeast exocyst complex. Nat. Struct. Mol. Biol. 23, 59-66 (2016).
    • (2016) Nat. Struct. Mol. Biol. , vol.23 , pp. 59-66
    • Heider, M.R.1
  • 16
    • 78549285917 scopus 로고    scopus 로고
    • Molecular organization of the COG vesicle tethering complex
    • Lees, J. A., Yip, C. K., Walz, T. & Hughson, F. M. Molecular organization of the COG vesicle tethering complex. Nat. Struct. Mol. Biol. 17, 1292-1297 (2010).
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 1292-1297
    • Lees, J.A.1    Yip, C.K.2    Walz, T.3    Hughson, F.M.4
  • 18
    • 85010677165 scopus 로고    scopus 로고
    • The in vivo architecture of the exocyst provides structural basis for exocytosis
    • Picco, A. et al. The in vivo architecture of the exocyst provides structural basis for exocytosis. Cell 168, 400-412.e18 (2017).
    • (2017) Cell , vol.168 , pp. 400e18-412e18
    • Picco, A.1
  • 19
    • 84966320565 scopus 로고    scopus 로고
    • Increasing the depth of mass-spectrometry-based structural analysis of protein complexes through the use of multiple cross-linkers
    • Ding, Y. H. et al. Increasing the depth of mass-spectrometry-based structural analysis of protein complexes through the use of multiple cross-linkers. Anal. Chem. 88, 4461-4469 (2016).
    • (2016) Anal. Chem. , vol.88 , pp. 4461-4469
    • Ding, Y.H.1
  • 20
    • 84887212464 scopus 로고    scopus 로고
    • Conservation of helical bundle structure between the exocyst subunits
    • Croteau, N. J., Furgason, M. L., Devos, D. & Munson, M. Conservation of helical bundle structure between the exocyst subunits. PLoS. One 4, e4443 (2009).
    • (2009) PLoS. One , vol.4 , pp. e4443
    • Croteau, N.J.1    Furgason, M.L.2    Devos, D.3    Munson, M.4
  • 21
    • 84865305431 scopus 로고    scopus 로고
    • Structures and mechanisms of vesicle coat components and multisubunit tethering complexes
    • Jackson, L. P., Kümmel, D., Reinisch, K. M. & Owen, D. J. Structures and mechanisms of vesicle coat components and multisubunit tethering complexes. Curr. Opin. Cell. Biol. 24, 475-483 (2012).
    • (2012) Curr. Opin. Cell. Biol. , vol.24 , pp. 475-483
    • Jackson, L.P.1    Kümmel, D.2    Reinisch, K.M.3    Owen, D.J.4
  • 22
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution
    • Sutton, R. B., Fasshauer, D., Jahn, R. & Brunger, A. T. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution. Nature 395, 347-353 (1998).
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 23
    • 0032548828 scopus 로고    scopus 로고
    • Sec3p is a spatial landmark for polarized secretion in budding yeast
    • Finger, F. P., Hughes, T. E. & Novick, P. Sec3p is a spatial landmark for polarized secretion in budding yeast. Cell 92, 559-571 (1998).
    • (1998) Cell , vol.92 , pp. 559-571
    • Finger, F.P.1    Hughes, T.E.2    Novick, P.3
  • 24
    • 0035067186 scopus 로고    scopus 로고
    • Spatial regulation of the exocyst complex by Rho1 GTPase
    • Guo, W., Tamanoi, F. & Novick, P. Spatial regulation of the exocyst complex by Rho1 GTPase. Nat. Cell. Biol. 3, 353-360 (2001).
    • (2001) Nat. Cell. Biol. , vol.3 , pp. 353-360
    • Guo, W.1    Tamanoi, F.2    Novick, P.3
  • 25
    • 38349030651 scopus 로고    scopus 로고
    • Membrane association and functional regulation of Sec3 by phospholipids and Cdc42
    • Zhang, X. et al. Membrane association and functional regulation of Sec3 by phospholipids and Cdc42. J. Cell. Biol. 180, 145-158 (2008).
    • (2008) J. Cell. Biol. , vol.180 , pp. 145-158
    • Zhang, X.1
  • 26
    • 76349093365 scopus 로고    scopus 로고
    • Structural basis for the Rho-and phosphoinositidedependent localization of the exocyst subunit Sec3
    • Yamashita, M. et al. Structural basis for the Rho-and phosphoinositidedependent localization of the exocyst subunit Sec3. Nat. Struct. Mol. Biol. 17, 180-186 (2010).
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 180-186
    • Yamashita, M.1
  • 27
    • 77951227637 scopus 로고    scopus 로고
    • Structure-function study of the N-terminal domain of exocyst subunit Sec3
    • Baek, K. et al. Structure-function study of the N-terminal domain of exocyst subunit Sec3. J. Biol. Chem. 285, 10424-10433 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 10424-10433
    • Baek, K.1
  • 28
    • 10344263403 scopus 로고    scopus 로고
    • Vesicles carry most exocyst subunits to exocytic sites marked by the remaining two subunits, Sec3p and Exo70p
    • Boyd, C., Hughes, T., Pypaert, M. & Novick, P. Vesicles carry most exocyst subunits to exocytic sites marked by the remaining two subunits, Sec3p and Exo70p. J. Cell. Biol. 167, 889-901 (2004).
    • (2004) J. Cell. Biol. , vol.167 , pp. 889-901
    • Boyd, C.1    Hughes, T.2    Pypaert, M.3    Novick, P.4
  • 29
    • 84911361850 scopus 로고    scopus 로고
    • The role of Sec3p in secretory vesicle targeting and exocyst complex assembly
    • Luo, G., Zhang, J. & Guo, W. The role of Sec3p in secretory vesicle targeting and exocyst complex assembly. Mol. Biol. Cell. 25, 3813-3822 (2014).
    • (2014) Mol. Biol. Cell. , vol.25 , pp. 3813-3822
    • Luo, G.1    Zhang, J.2    Guo, W.3
  • 30
    • 34648823113 scopus 로고    scopus 로고
    • Exo70 interacts with phospholipids and mediates the targeting of the exocyst to the plasma membrane
    • He, B., Xi, F., Zhang, X., Zhang, J. & Guo, W. Exo70 interacts with phospholipids and mediates the targeting of the exocyst to the plasma membrane. EMBO J. 26, 4053-4065 (2007).
    • (2007) EMBO J. , vol.26 , pp. 4053-4065
    • He, B.1    Xi, F.2    Zhang, X.3    Zhang, J.4    Guo, W.5
  • 31
    • 35848947444 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate mediates the targeting of the exocyst to the plasma membrane for exocytosis in mammalian cells
    • Liu, J., Zuo, X., Yue, P. & Guo, W. Phosphatidylinositol 4,5-bisphosphate mediates the targeting of the exocyst to the plasma membrane for exocytosis in mammalian cells. Mol. Biol. Cell. 18, 4483-4492 (2007).
    • (2007) Mol. Biol. Cell. , vol.18 , pp. 4483-4492
    • Liu, J.1    Zuo, X.2    Yue, P.3    Guo, W.4
  • 32
    • 33744933711 scopus 로고    scopus 로고
    • The structure of the exocyst subunit Sec6p defines a conserved architecture with diverse roles
    • Sivaram, M. V., Furgason, M. L., Brewer, D. N. & Munson, M. The structure of the exocyst subunit Sec6p defines a conserved architecture with diverse roles. Nat. Struct. Mol. Biol. 13, 555-556 (2006).
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 555-556
    • Sivaram, M.V.1    Furgason, M.L.2    Brewer, D.N.3    Munson, M.4
  • 33
    • 21844443829 scopus 로고    scopus 로고
    • Exo84 and Sec5 are competitive regulatory Sec6/8 effectors to the RalA GTPase
    • Jin, R. et al. Exo84 and Sec5 are competitive regulatory Sec6/8 effectors to the RalA GTPase. EMBO J. 24, 2064-2074 (2005).
    • (2005) EMBO J. , vol.24 , pp. 2064-2074
    • Jin, R.1
  • 34
    • 0038602702 scopus 로고    scopus 로고
    • Structural basis of the interaction between RalA and Sec5, a subunit of the sec6/8 complex
    • Fukai, S., Matern, H. T., Jagath, J. R., Scheller, R. H. & Brunger, A. T. Structural basis of the interaction between RalA and Sec5, a subunit of the sec6/8 complex. EMBO J. 22, 3267-3278 (2003).
    • (2003) EMBO J. , vol.22 , pp. 3267-3278
    • Fukai, S.1    Matern, H.T.2    Jagath, J.R.3    Scheller, R.H.4    Brunger, A.T.5
  • 35
    • 27144456598 scopus 로고    scopus 로고
    • Sec15 interacts with Rab11 via a novel domain and affects Rab11 localization in vivo
    • Wu, S., Mehta, S. Q., Pichaud, F., Bellen, H. J. & Quiocho, F. A. Sec15 interacts with Rab11 via a novel domain and affects Rab11 localization in vivo. Nat. Struct. Mol. Biol. 12, 879-885 (2005).
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 879-885
    • Wu, S.1    Mehta, S.Q.2    Pichaud, F.3    Bellen, H.J.4    Quiocho, F.A.5
  • 36
    • 28544432477 scopus 로고    scopus 로고
    • The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif
    • Dong, G., Hutagalung, A. H., Fu, C., Novick, P. & Reinisch, K. M. The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif. Nat. Struct. Mol. Biol. 12, 1094-1100 (2005).
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 1094-1100
    • Dong, G.1    Hutagalung, A.H.2    Fu, C.3    Novick, P.4    Reinisch, K.M.5
  • 37
    • 30344435606 scopus 로고    scopus 로고
    • Crystal structure of the S cerevisiae exocyst component Exo70p
    • Hamburger, Z. A., Hamburger, A. E., West, A. P. Jr. & Weis, W. I. Crystal structure of the S. cerevisiae exocyst component Exo70p. J. Mol. Biol. 356, 9-21 (2006).
    • (2006) J. Mol. Biol. , vol.356 , pp. 9-21
    • Hamburger, Z.A.1    Hamburger, A.E.2    West, A.P.3    Weis, W.I.4
  • 38
    • 34447276935 scopus 로고    scopus 로고
    • The crystal structure of mouse Exo70 reveals unique features of the mammalian exocyst
    • Moore, B. A., Robinson, H. H. & Xu, Z. The crystal structure of mouse Exo70 reveals unique features of the mammalian exocyst. J. Mol. Biol. 371, 410-421 (2007).
    • (2007) J. Mol. Biol. , vol.371 , pp. 410-421
    • Moore, B.A.1    Robinson, H.H.2    Xu, Z.3
  • 39
    • 84953280683 scopus 로고    scopus 로고
    • Endosidin2 targets conserved exocyst complex subunit EXO70 to inhibit exocytosis
    • Zhang, C. et al. Endosidin2 targets conserved exocyst complex subunit EXO70 to inhibit exocytosis. Proc. Natl Acad. Sci. USA 113, E41-E50 (2016).
    • (2016) Proc. Natl Acad. Sci. USA , vol.113 , pp. E41-E50
    • Zhang, C.1
  • 40
    • 85010058347 scopus 로고    scopus 로고
    • Crystal structure of Sec10, a subunit of the exocyst complex
    • Chen, J. et al. Crystal structure of Sec10, a subunit of the exocyst complex. Sci. Rep. 7, 40909 (2017).
    • (2017) Sci. Rep. , vol.7 , pp. 40909
    • Chen, J.1
  • 41
    • 0035489304 scopus 로고    scopus 로고
    • The Sec34/35 Golgi transport complex is related to the exocyst, defining a family of complexes involved in multiple steps of membrane traffic
    • Whyte, J. R. & Munro, S. The Sec34/35 Golgi transport complex is related to the exocyst, defining a family of complexes involved in multiple steps of membrane traffic. Dev. Cell. 1, 527-537 (2001).
    • (2001) Dev. Cell. , vol.1 , pp. 527-537
    • Whyte, J.R.1    Munro, S.2
  • 42
    • 84984653623 scopus 로고    scopus 로고
    • An endosomal tether undergoes an entropic collapse to bring vesicles together
    • Murray, D. H. et al. An endosomal tether undergoes an entropic collapse to bring vesicles together. Nature 537, 107-111 (2016).
    • (2016) Nature , vol.537 , pp. 107-111
    • Murray, D.H.1
  • 43
    • 0036608158 scopus 로고    scopus 로고
    • Ras family therapy: Rab, Rho and Ral talk to the exocyst
    • Novick, P. & Guo, W. Ras family therapy: Rab, Rho and Ral talk to the exocyst. Trends Cell. Biol. 12, 247-249 (2002).
    • (2002) Trends Cell. Biol. , vol.12 , pp. 247-249
    • Novick, P.1    Guo, W.2
  • 44
    • 0001647625 scopus 로고    scopus 로고
    • Exocytosis: The many masters of the exocyst
    • Lipschutz, J. H. & Mostov, K. E. Exocytosis: the many masters of the exocyst. Curr. Biol. 12, R212-R214 (2002).
    • (2002) Curr. Biol. , vol.12 , pp. R212-R214
    • Lipschutz, J.H.1    Mostov, K.E.2
  • 45
    • 0036141393 scopus 로고    scopus 로고
    • The exocyst is a Ral effector complex
    • Moskalenko, S. et al. The exocyst is a Ral effector complex. Nat. Cell. Biol. 4, 66-72 (2002).
    • (2002) Nat. Cell. Biol. , vol.4 , pp. 66-72
    • Moskalenko, S.1
  • 46
    • 0346154744 scopus 로고    scopus 로고
    • Ral GTPases regulate exocyst assembly through dual subunit interactions
    • Moskalenko, S. et al. Ral GTPases regulate exocyst assembly through dual subunit interactions. J. Biol. Chem. 278, 51743-51748 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 51743-51748
    • Moskalenko, S.1
  • 47
    • 0036141434 scopus 로고    scopus 로고
    • The exocyst complex binds the small GTPase RalA to mediate filopodia formation
    • Sugihara, K. et al. The exocyst complex binds the small GTPase RalA to mediate filopodia formation. Nat. Cell. Biol. 4, 73-78 (2002).
    • (2002) Nat. Cell. Biol. , vol.4 , pp. 73-78
    • Sugihara, K.1
  • 48
    • 84880620028 scopus 로고    scopus 로고
    • Mitotic phosphorylation of Exo84 disrupts exocyst assembly and arrests cell growth
    • Luo, G., Zhang, J., Luca, F. C. & Guo, W. Mitotic phosphorylation of Exo84 disrupts exocyst assembly and arrests cell growth. J. Cell. Biol. 202, 97-111 (2013).
    • (2013) J. Cell. Biol. , vol.202 , pp. 97-111
    • Luo, G.1    Zhang, J.2    Luca, F.C.3    Guo, W.4
  • 49
    • 84971224778 scopus 로고    scopus 로고
    • Oncogenic BRAF-mediated melanoma cell invasion
    • Lu, H. et al. Oncogenic BRAF-mediated melanoma cell invasion. Cell. Rep. 15, 2012-2024 (2016).
    • (2016) Cell. Rep. , vol.15 , pp. 2012-2024
    • Lu, H.1
  • 50
    • 84860913399 scopus 로고    scopus 로고
    • ERK1/2 regulate exocytosis through direct phosphorylation of the exocyst component Exo70
    • Ren, J. & Guo, W. ERK1/2 regulate exocytosis through direct phosphorylation of the exocyst component Exo70. Dev. Cell. 22, 967-978 (2012).
    • (2012) Dev. Cell. , vol.22 , pp. 967-978
    • Ren, J.1    Guo, W.2
  • 51
    • 84866117936 scopus 로고    scopus 로고
    • Identification of cross-linked peptides from complex samples
    • Yang, B. et al. Identification of cross-linked peptides from complex samples. Nat. Methods 9, 904-906 (2012).
    • (2012) Nat. Methods , vol.9 , pp. 904-906
    • Yang, B.1
  • 52
    • 80355128077 scopus 로고    scopus 로고
    • Single particle electron microscopy reconstruction of the exosome complex using the random conical tilt method
    • Liu, X. & Wang, H. W. Single particle electron microscopy reconstruction of the exosome complex using the random conical tilt method. J. Vis. Exp. 49, 2574 (2011).
    • (2011) J. Vis. Exp. , vol.49 , pp. 2574
    • Liu, X.1    Wang, H.W.2
  • 53
    • 84946482375 scopus 로고    scopus 로고
    • Aysnchronous data acquisition and on-The-fly analysis of dose fractionated cryo-EM images by UCSFImage
    • Li, X., Zheng, S., Agard, D. A. & Cheng, Y. Aysnchronous data acquisition and on-the-fly analysis of dose fractionated cryo-EM images by UCSFImage. J. Struct. Biol. 192, 74-78 (2015).
    • (2015) J. Struct. Biol. , vol.192 , pp. 74-78
    • Li, X.1    Zheng, S.2    Agard, D.A.3    Cheng, Y.4
  • 54
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM
    • Li, X. et al. Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nat. Methods 10, 584-590 (2013).
    • (2013) Nat. Methods , vol.10 , pp. 584-590
    • Li, X.1
  • 55
    • 84920942671 scopus 로고    scopus 로고
    • Beam-induced motion correction for sub-megadalton cryo-EM particles
    • Scheres, S. H. Beam-induced motion correction for sub-megadalton cryo-EM particles. eLife 3, e03665 (2014).
    • (2014) ELife , vol.3 , pp. e03665
    • Scheres, S.H.1
  • 56
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: An extensible image processing suite for electron microscopy
    • Tang, G. et al. EMAN2: an extensible image processing suite for electron microscopy. J. Struct. Biol. 157, 38-46 (2007).
    • (2007) J. Struct. Biol. , vol.157 , pp. 38-46
    • Tang, G.1
  • 57
    • 58049204808 scopus 로고    scopus 로고
    • SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs
    • Shaikh, T. R. et al. SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs. Nat. Protoc. 3, 1941-1974 (2008).
    • (2008) Nat. Protoc. , vol.3 , pp. 1941-1974
    • Shaikh, T.R.1
  • 58
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • Mindell, J. A. & Grigorieff, N. Accurate determination of local defocus and specimen tilt in electron microscopy. J. Struct. Biol. 142, 334-347 (2003).
    • (2003) J. Struct. Biol. , vol.142 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 59
    • 84868444740 scopus 로고    scopus 로고
    • RELION: Implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres, S. H. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J. Struct. Biol. 180, 519-530 (2012).
    • (2012) J. Struct. Biol. , vol.180 , pp. 519-530
    • Scheres, S.H.1
  • 60
    • 85014129582 scopus 로고    scopus 로고
    • MotionCor2: Anisotropic correction of beam-induced motion for improved cryo-electron microscopy
    • Zheng, S. Q. et al. MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy. Nat. Methods 14, 331-332 (2017).
    • (2017) Nat. Methods , vol.14 , pp. 331-332
    • Zheng, S.Q.1
  • 61
    • 84946481951 scopus 로고    scopus 로고
    • Automatic estimation and correction of anisotropic magnification distortion in electron microscopes
    • Grant, T. & Grigorieff, N. Automatic estimation and correction of anisotropic magnification distortion in electron microscopes. J. Struct. Biol. 192, 204-208 (2015).
    • (2015) J. Struct. Biol. , vol.192 , pp. 204-208
    • Grant, T.1    Grigorieff, N.2
  • 62
    • 84992045306 scopus 로고    scopus 로고
    • An algorithm for estimation and correction of anisotropic magnification distortion of cryo-EM images without need of pre-calibration
    • Yu, G. et al. An algorithm for estimation and correction of anisotropic magnification distortion of cryo-EM images without need of pre-calibration. J. Struct. Biol. 195, 207-215 (2016).
    • (2016) J. Struct. Biol. , vol.195 , pp. 207-215
    • Yu, G.1
  • 63
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-A visualization system for exploratory research and analysis
    • Pettersen, E. F. et al. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 64
    • 84894623755 scopus 로고    scopus 로고
    • Quantifying the local resolution of cryo-EM density maps
    • Kucukelbir, A., Sigworth, F. J. & Tagare, H. D. Quantifying the local resolution of cryo-EM density maps. Nat. Methods 11, 63-65 (2014).
    • (2014) Nat. Methods , vol.11 , pp. 63-65
    • Kucukelbir, A.1    Sigworth, F.J.2    Tagare, H.D.3
  • 65
    • 84866078359 scopus 로고    scopus 로고
    • Prevention of overfitting in cryo-EM structure determination
    • Scheres, S. H. & Chen, S. Prevention of overfitting in cryo-EM structure determination. Nat. Methods 9, 853-854 (2012).
    • (2012) Nat. Methods , vol.9 , pp. 853-854
    • Scheres, S.H.1    Chen, S.2
  • 66
    • 0032780181 scopus 로고    scopus 로고
    • Situs: A package for docking crystal structures into low-resolution maps from electron microscopy
    • Wriggers, W., Milligan, R. A. & McCammon, J. A. Situs: a package for docking crystal structures into low-resolution maps from electron microscopy. J. Struct. Biol. 125, 185-195 (1999).
    • (1999) J. Struct. Biol. , vol.125 , pp. 185-195
    • Wriggers, W.1    Milligan, R.A.2    McCammon, J.A.3
  • 67
    • 84904815625 scopus 로고    scopus 로고
    • SWISS-MODEL: Modelling protein tertiary and quaternary structure using evolutionary information
    • Biasini, M. et al. SWISS-MODEL: modelling protein tertiary and quaternary structure using evolutionary information. Nucleic Acids Res. 42, W252-W258 (2014).
    • (2014) Nucleic Acids Res. , vol.42 , pp. W252-W258
    • Biasini, M.1
  • 68
    • 84930074657 scopus 로고    scopus 로고
    • The Phyre2 web portal for protein modeling, prediction and analysis
    • Kelley, L. A., Mezulis, S., Yates, C. M., Wass, M. N. & Sternberg, M. J. The Phyre2 web portal for protein modeling, prediction and analysis. Nat. Protoc. 10, 845-858 (2015).
    • (2015) Nat. Protoc. , vol.10 , pp. 845-858
    • Kelley, L.A.1    Mezulis, S.2    Yates, C.M.3    Wass, M.N.4    Sternberg, M.J.5
  • 70
    • 85022179318 scopus 로고    scopus 로고
    • Modeling protein excited-state structures from over-length chemical cross-links
    • Ding, Y. H. et al. Modeling protein excited-state structures from over-length chemical cross-links. J. Biol. Chem. 292, 1187-1196 (2017).
    • (2017) J. Biol. Chem. , vol.292 , pp. 1187-1196
    • Ding, Y.H.1
  • 71
    • 84866095385 scopus 로고    scopus 로고
    • Structural probing of a protein phosphatase 2 A network by chemical cross-linking and mass spectrometry
    • Herzog, F. et al. Structural probing of a protein phosphatase 2 A network by chemical cross-linking and mass spectrometry. Science 337, 1348-1352 (2012).
    • (2012) Science , vol.337 , pp. 1348-1352
    • Herzog, F.1
  • 72
    • 84907323467 scopus 로고    scopus 로고
    • Molecular architecture of the 40SeIF1eIF3 translation initiation complex
    • Erzberger, J. P. et al. Molecular architecture of the 40SeIF1eIF3 translation initiation complex. Cell 158, 1123-1135 (2014).
    • (2014) Cell , vol.158 , pp. 1123-1135
    • Erzberger, J.P.1
  • 73
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66, 213-221 (2010).
    • (2010) Acta Crystallogr. D Biol. Crystallogr. , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 74
    • 74549178560 scopus 로고    scopus 로고
    • MolProbity: All-atom structure validation for macromolecular crystallography
    • Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D. Biol. Crystallogr. 66, 12-21 (2010).
    • (2010) Acta Crystallogr. D. Biol. Crystallogr. , vol.66 , pp. 12-21
    • Chen, V.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.