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Volumn 427, Issue 4, 2015, Pages 966-981

Structural basis of dynamic membrane recognition by trans-Golgi network specific FAPP proteins

Author keywords

lipid microdomains; membrane trafficking; nuclear magnetic resonance spectroscopy; phosphoinositide recognition; pleckstrin homology domain

Indexed keywords

FAPP PROTEIN; LIPOSOME; PHOSPHATIDYLINOSITIDE; PROTEIN; UNCLASSIFIED DRUG; GLYCOSPHINGOLIPID; PHOSPHATIDYLINOSITOL 4-PHOSPHATE; PLEKHA3 PROTEIN, HUMAN; PLEKHA8 PROTEIN, HUMAN; POLYPHOSPHOINOSITIDE; PROTEIN BINDING; SIGNAL TRANSDUCING ADAPTOR PROTEIN;

EID: 84922237862     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2014.12.023     Document Type: Article
Times cited : (31)

References (75)
  • 1
    • 2342478588 scopus 로고    scopus 로고
    • Signaling with phosphoinositides: Better than binary
    • M. Overduin, M.L. Cheever, and T.G. Kutateladze Signaling with phosphoinositides: better than binary Mol Interv 1 2001 150 159
    • (2001) Mol Interv , vol.1 , pp. 150-159
    • Overduin, M.1    Cheever, M.L.2    Kutateladze, T.G.3
  • 2
    • 2342661960 scopus 로고    scopus 로고
    • Phosphoinositides in constitutive membrane traffic
    • M.G. Roth Phosphoinositides in constitutive membrane traffic Physiol Rev 84 2004 699 730
    • (2004) Physiol Rev , vol.84 , pp. 699-730
    • Roth, M.G.1
  • 3
    • 0015950912 scopus 로고
    • Cholera toxin: Interaction of subunits with ganglioside GM1
    • S.V. Heyningen Cholera toxin: interaction of subunits with ganglioside GM1 Science 183 1974 656 657
    • (1974) Science , vol.183 , pp. 656-657
    • Heyningen, S.V.1
  • 4
    • 0023821674 scopus 로고
    • 2 +-dependent phospholipid- (and membrane-) binding proteins
    • 2 +-dependent phospholipid- (and membrane-) binding proteins Biochemistry 27 1988 6645 6653
    • (1988) Biochemistry , vol.27 , pp. 6645-6653
    • Klee, C.B.1
  • 6
    • 1442317538 scopus 로고    scopus 로고
    • Embo JBAR domains as sensors of membrane curvature: The amphiphysin BAR structure
    • B.J. Peter, H.M. Kent, I.G. Mills, Y. Vallis, P.J. Butler, and P.R. Evans Embo JBAR domains as sensors of membrane curvature: the amphiphysin BAR structure Science 303 2004 495 499
    • (2004) Science , vol.303 , pp. 495-499
    • Peter, B.J.1    Kent, H.M.2    Mills, I.G.3    Vallis, Y.4    Butler, P.J.5    Evans, P.R.6
  • 8
    • 84859175189 scopus 로고    scopus 로고
    • Structural basis of membrane bending by the N-BAR protein endophilin
    • C. Mim, H. Cui, J.A. Gawronski-Salerno, A. Frost, E. Lyman, and G.A. Voth Structural basis of membrane bending by the N-BAR protein endophilin Cell 149 2012 137 145
    • (2012) Cell , vol.149 , pp. 137-145
    • Mim, C.1    Cui, H.2    Gawronski-Salerno, J.A.3    Frost, A.4    Lyman, E.5    Voth, G.A.6
  • 10
    • 0030033414 scopus 로고    scopus 로고
    • Myristoylation-facilitated binding of the G protein ARF1GDP to membrane phospholipids is required for its activation by a soluble nucleotide exchange factor
    • M. Franco, P. Chardin, M. Chabre, and S. Paris Myristoylation-facilitated binding of the G protein ARF1GDP to membrane phospholipids is required for its activation by a soluble nucleotide exchange factor J Biol Chem 271 1996 1573 1578
    • (1996) J Biol Chem , vol.271 , pp. 1573-1578
    • Franco, M.1    Chardin, P.2    Chabre, M.3    Paris, S.4
  • 12
    • 20144375061 scopus 로고    scopus 로고
    • An acylation cycle regulates localization and activity of palmitoylated Ras isoforms
    • O. Rocks, A. Peyker, M. Kahms, P.J. Verveer, C. Koerner, and M. Lumbierres An acylation cycle regulates localization and activity of palmitoylated Ras isoforms Science 307 2005 1746 1752
    • (2005) Science , vol.307 , pp. 1746-1752
    • Rocks, O.1    Peyker, A.2    Kahms, M.3    Verveer, P.J.4    Koerner, C.5    Lumbierres, M.6
  • 14
    • 0030882949 scopus 로고    scopus 로고
    • Altered regulation of cholesterol and cholesteryl ester synthesis in Chinese-hamster ovary cells overexpressing the oxysterol-binding protein is dependent on the pleckstrin homology domain
    • T.A. Lagace, D.M. Byers, H.W. Cook, and N.D. Ridgway Altered regulation of cholesterol and cholesteryl ester synthesis in Chinese-hamster ovary cells overexpressing the oxysterol-binding protein is dependent on the pleckstrin homology domain Biochem J 326 1997 205 213
    • (1997) Biochem J , vol.326 , pp. 205-213
    • Lagace, T.A.1    Byers, D.M.2    Cook, H.W.3    Ridgway, N.D.4
  • 17
    • 78649767884 scopus 로고
    • The intermembrane ceramide transport catalyzed by CERT is sensitive to the lipid environment
    • J. Tuuf, M.A. Kjellberg, J.G. Molotkovsky, K. Hanada, and P. Mattjus The intermembrane ceramide transport catalyzed by CERT is sensitive to the lipid environment Biochim Biophys Acta 2011 1808 229 235
    • (1808) Biochim Biophys Acta , vol.2011 , pp. 229-235
    • Tuuf, J.1    Kjellberg, M.A.2    Molotkovsky, J.G.3    Hanada, K.4    Mattjus, P.5
  • 18
    • 14844302797 scopus 로고    scopus 로고
    • A plasma membrane pool of phosphatidylinositol 4-phosphate is generated by phosphatidylinositol 4-kinase type-III alpha: Studies with the PH domains of the oxysterol binding protein and FAPP1
    • A. Balla, G. Tuymetova, A. Tsiomenko, P. Varnai, and T. Balla A plasma membrane pool of phosphatidylinositol 4-phosphate is generated by phosphatidylinositol 4-kinase type-III alpha: studies with the PH domains of the oxysterol binding protein and FAPP1 Mol Biol Cell 16 2005 1282 1295
    • (2005) Mol Biol Cell , vol.16 , pp. 1282-1295
    • Balla, A.1    Tuymetova, G.2    Tsiomenko, A.3    Varnai, P.4    Balla, T.5
  • 20
    • 84901650366 scopus 로고    scopus 로고
    • A novel probe for phosphatidylinositol 4-phosphate reveals multiple pools beyond the Golgi
    • G.R. Hammond, M.P. Machner, and T. Balla A novel probe for phosphatidylinositol 4-phosphate reveals multiple pools beyond the Golgi J Cell Biol 205 2014 113 126
    • (2014) J Cell Biol , vol.205 , pp. 113-126
    • Hammond, G.R.1    Machner, M.P.2    Balla, T.3
  • 22
    • 0032543562 scopus 로고    scopus 로고
    • The pleckstrin homology domain of oxysterol-binding protein recognises a determinant specific to Golgi membranes
    • T.P. Levine, and S. Munro The pleckstrin homology domain of oxysterol-binding protein recognises a determinant specific to Golgi membranes Curr Biol 8 1998 729 739
    • (1998) Curr Biol , vol.8 , pp. 729-739
    • Levine, T.P.1    Munro, S.2
  • 23
    • 84866904070 scopus 로고    scopus 로고
    • Structural basis for the Golgi-association by the pleckstrin homology domain of the ceramide trafficking protein CERT
    • T. Sugiki, K. Takeuchi, T. Yamaji, T. Takano, Y. Tokunaga, and K. Kumagai Structural basis for the Golgi-association by the pleckstrin homology domain of the ceramide trafficking protein CERT J Biol Chem 287 2012 33706 33778
    • (2012) J Biol Chem , vol.287 , pp. 33706-33778
    • Sugiki, T.1    Takeuchi, K.2    Yamaji, T.3    Takano, T.4    Tokunaga, Y.5    Kumagai, K.6
  • 24
    • 0034737658 scopus 로고    scopus 로고
    • Phosphoinositide-dependent activation of the ADP-ribosylation factor GTPase-activating protein ASAP1. Evidence for the pleckstrin homology domain functioning as an allosteric site
    • J.L. Kam, K. Miura, T.R. Jackson, J. Gruschus, P. Roller, and S. Stauffer Phosphoinositide-dependent activation of the ADP-ribosylation factor GTPase-activating protein ASAP1. Evidence for the pleckstrin homology domain functioning as an allosteric site J Biol Chem 275 2000 9653 9663
    • (2000) J Biol Chem , vol.275 , pp. 9653-9663
    • Kam, J.L.1    Miura, K.2    Jackson, T.R.3    Gruschus, J.4    Roller, P.5    Stauffer, S.6
  • 25
    • 33749505651 scopus 로고    scopus 로고
    • Cooperation of phosphoinositides and BAR domain proteins in endosomal tubulation
    • N. Shinozaki-Narikawa, T. Kodama, and Y. Shibasaki Cooperation of phosphoinositides and BAR domain proteins in endosomal tubulation Traffic 7 2006 1539 1550
    • (2006) Traffic , vol.7 , pp. 1539-1550
    • Shinozaki-Narikawa, N.1    Kodama, T.2    Shibasaki, Y.3
  • 26
    • 0032515042 scopus 로고    scopus 로고
    • Specificity and promiscuity in phosphoinositide binding by pleckstrin homology domains
    • J.M. Kavran, D.E. Klein, A. Lee, M. Falasca, S.J. Isakoff, and E.Y. Skolnik Specificity and promiscuity in phosphoinositide binding by pleckstrin homology domains J Biol Chem 273 1998 30497 30508
    • (1998) J Biol Chem , vol.273 , pp. 30497-30508
    • Kavran, J.M.1    Klein, D.E.2    Lee, A.3    Falasca, M.4    Isakoff, S.J.5    Skolnik, E.Y.6
  • 27
    • 77950370938 scopus 로고    scopus 로고
    • Structural basis of wedging the Golgi membrane by FAPP pleckstrin homology domains
    • M. Lenoir, U. Coskun, M. Grzybek, X. Cao, S.B. Buschhorn, and J. James Structural basis of wedging the Golgi membrane by FAPP pleckstrin homology domains EMBO Rep 11 2010 279 284
    • (2010) EMBO Rep , vol.11 , pp. 279-284
    • Lenoir, M.1    Coskun, U.2    Grzybek, M.3    Cao, X.4    Buschhorn, S.B.5    James, J.6
  • 28
    • 0037197804 scopus 로고    scopus 로고
    • Targeting of Golgi-specific pleckstrin homology domains involves both PtdIns 4-kinase-dependent and -independent components
    • T.P. Levine, and S. Munro Targeting of Golgi-specific pleckstrin homology domains involves both PtdIns 4-kinase-dependent and -independent components Curr Biol 12 2002 695 704
    • (2002) Curr Biol , vol.12 , pp. 695-704
    • Levine, T.P.1    Munro, S.2
  • 29
    • 33845487091 scopus 로고    scopus 로고
    • FAPP2, cilium formation, and compartmentalization of the apical membrane in polarized Madin-Darby canine kidney (MDCK) cells
    • O.V. Vieira, K. Gaus, P. Verkade, J. Fullekrug, W.L. Vaz, and K. Simons FAPP2, cilium formation, and compartmentalization of the apical membrane in polarized Madin-Darby canine kidney (MDCK) cells Proc Natl Acad Sci USA 103 2006 18556 18561
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 18556-18561
    • Vieira, O.V.1    Gaus, K.2    Verkade, P.3    Fullekrug, J.4    Vaz, W.L.5    Simons, K.6
  • 30
    • 84883742330 scopus 로고    scopus 로고
    • Vesicular and non-vesicular transport feed distinct glycosylation pathways in the Golgi
    • G. D'Angelo, T. Uemura, C.C. Chuang, E. Polishchuk, M. Santoro, and H. Ohvo-Rekila Vesicular and non-vesicular transport feed distinct glycosylation pathways in the Golgi Nature 501 2013 116 120
    • (2013) Nature , vol.501 , pp. 116-120
    • D'Angelo, G.1    Uemura, T.2    Chuang, C.C.3    Polishchuk, E.4    Santoro, M.5    Ohvo-Rekila, H.6
  • 32
    • 0035793903 scopus 로고    scopus 로고
    • Structural mechanism of endosome docking by the FYVE domain
    • T. Kutateladze, and M. Overduin Structural mechanism of endosome docking by the FYVE domain Science 291 2001 1793 1796
    • (2001) Science , vol.291 , pp. 1793-1796
    • Kutateladze, T.1    Overduin, M.2
  • 34
    • 3142655870 scopus 로고    scopus 로고
    • Structural basis of membrane targeting by the Phox homology domain of cytokine-independent survival kinase (CISK-PX)
    • Y. Xing, D. Liu, R. Zhang, A. Joachimiak, Z. Songyang, and W. Xu Structural basis of membrane targeting by the Phox homology domain of cytokine-independent survival kinase (CISK-PX) J Biol Chem 279 2004 30662 30669
    • (2004) J Biol Chem , vol.279 , pp. 30662-30669
    • Xing, Y.1    Liu, D.2    Zhang, R.3    Joachimiak, A.4    Songyang, Z.5    Xu, W.6
  • 35
    • 0242385346 scopus 로고    scopus 로고
    • Separation of liquid phases in giant vesicles of ternary mixtures of phospholipids and cholesterol
    • S.L. Veatch, and S.L. Keller Separation of liquid phases in giant vesicles of ternary mixtures of phospholipids and cholesterol Biophys J 85 2003 3074 3083
    • (2003) Biophys J , vol.85 , pp. 3074-3083
    • Veatch, S.L.1    Keller, S.L.2
  • 36
    • 18444366155 scopus 로고    scopus 로고
    • Role of curvature and phase transition in lipid sorting and fission of membrane tubules
    • A. Roux, D. Cuvelier, P. Nassoy, J. Prost, P. Bassereau, and B. Goud Role of curvature and phase transition in lipid sorting and fission of membrane tubules EMBO J 24 2005 1537 1545
    • (2005) EMBO J , vol.24 , pp. 1537-1545
    • Roux, A.1    Cuvelier, D.2    Nassoy, P.3    Prost, J.4    Bassereau, P.5    Goud, B.6
  • 37
    • 29144531904 scopus 로고    scopus 로고
    • Seeing spots: Complex phase behavior in simple membranes
    • S.L. Veatch, and S.L. Keller Seeing spots: complex phase behavior in simple membranes Biochim Biophys Acta 1746 2005 172 185
    • (2005) Biochim Biophys Acta , vol.1746 , pp. 172-185
    • Veatch, S.L.1    Keller, S.L.2
  • 38
    • 58149185333 scopus 로고    scopus 로고
    • Lipid lateral diffusion and membrane heterogeneity
    • G. Lindblom, and G. Oradd Lipid lateral diffusion and membrane heterogeneity Biochim Biophys Acta 1788 2009 234 244
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 234-244
    • Lindblom, G.1    Oradd, G.2
  • 39
    • 0035845497 scopus 로고    scopus 로고
    • Partitioning of Thy-1, GM1, and cross-linked phospholipid analogs into lipid rafts reconstituted in supported model membrane monolayers
    • C. Dietrich, Z.N. Volovyk, M. Levi, N.L. Thompson, and K. Jacobson Partitioning of Thy-1, GM1, and cross-linked phospholipid analogs into lipid rafts reconstituted in supported model membrane monolayers Proc Natl Acad Sci USA 98 2001 10642 10647
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10642-10647
    • Dietrich, C.1    Volovyk, Z.N.2    Levi, M.3    Thompson, N.L.4    Jacobson, K.5
  • 41
    • 0034125920 scopus 로고    scopus 로고
    • Partitioning of amphiphiles between coexisting ordered and disordered phases in two-phase lipid bilayer membranes
    • R.M. Mesquita, E. Melo, T.E. Thompson, and W.L. Vaz Partitioning of amphiphiles between coexisting ordered and disordered phases in two-phase lipid bilayer membranes Biophys J 78 2000 3019 3025
    • (2000) Biophys J , vol.78 , pp. 3019-3025
    • Mesquita, R.M.1    Melo, E.2    Thompson, T.E.3    Vaz, W.L.4
  • 42
    • 0035964342 scopus 로고    scopus 로고
    • Electrostatics of nanosystems: Application to microtubules and the ribosome
    • N.A. Baker, D. Sept, S. Joseph, M.J. Holst, and J.A. McCammon Electrostatics of nanosystems: application to microtubules and the ribosome Proc Natl Acad Sci USA 98 2001 10037 10041
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10037-10041
    • Baker, N.A.1    Sept, D.2    Joseph, S.3    Holst, M.J.4    McCammon, J.A.5
  • 44
    • 38349035977 scopus 로고    scopus 로고
    • Lipid interaction networks of peripheral membrane proteins revealed by data-driven micelle docking
    • F. Dancea, K. Kami, and M. Overduin Lipid interaction networks of peripheral membrane proteins revealed by data-driven micelle docking Biophys J 94 2008 515 524
    • (2008) Biophys J , vol.94 , pp. 515-524
    • Dancea, F.1    Kami, K.2    Overduin, M.3
  • 45
    • 27544456339 scopus 로고    scopus 로고
    • A simple method to predict protein flexibility using secondary chemical shifts
    • M.V. Berjanskii, and D.S. Wishart A simple method to predict protein flexibility using secondary chemical shifts J Am Chem Soc 127 2005 14970 14971
    • (2005) J Am Chem Soc , vol.127 , pp. 14970-14971
    • Berjanskii, M.V.1    Wishart, D.S.2
  • 48
    • 79956320991 scopus 로고    scopus 로고
    • Molecular basis of phosphatidylinositol 4-phosphate and ARF1 GTPase recognition by the FAPP1 pleckstrin homology (PH) domain
    • J. He, J.L. Scott, A. Heroux, S. Roy, M. Lenoir, and M. Overduin Molecular basis of phosphatidylinositol 4-phosphate and ARF1 GTPase recognition by the FAPP1 pleckstrin homology (PH) domain J Biol Chem 286 2011 18650 18657
    • (2011) J Biol Chem , vol.286 , pp. 18650-18657
    • He, J.1    Scott, J.L.2    Heroux, A.3    Roy, S.4    Lenoir, M.5    Overduin, M.6
  • 50
    • 84869040414 scopus 로고    scopus 로고
    • Curvature, lipid packing, and electrostatics of membrane organelles: Defining cellular territories in determining specificity
    • J. Bigay, and B. Antonny Curvature, lipid packing, and electrostatics of membrane organelles: defining cellular territories in determining specificity Dev Cell 23 2012 886 895
    • (2012) Dev Cell , vol.23 , pp. 886-895
    • Bigay, J.1    Antonny, B.2
  • 51
    • 84896691337 scopus 로고    scopus 로고
    • Interaction of Fapp1 with Arf1 and PI4P at a Membrane Surface: An Example of Coincidence Detection
    • Y. Liu, R.A. Kahn, and J.H. Prestegard Interaction of Fapp1 with Arf1 and PI4P at a Membrane Surface: An Example of Coincidence Detection Structure 22 2014 421 430
    • (2014) Structure , vol.22 , pp. 421-430
    • Liu, Y.1    Kahn, R.A.2    Prestegard, J.H.3
  • 53
    • 33744728346 scopus 로고    scopus 로고
    • Oxysterol-binding protein and vesicle-associated membrane protein-associated protein are required for sterol-dependent activation of the ceramide transport protein
    • R.J. Perry, and N.D. Ridgway Oxysterol-binding protein and vesicle-associated membrane protein-associated protein are required for sterol-dependent activation of the ceramide transport protein Mol Biol Cell 17 2006 2604 2616
    • (2006) Mol Biol Cell , vol.17 , pp. 2604-2616
    • Perry, R.J.1    Ridgway, N.D.2
  • 54
    • 77954204064 scopus 로고    scopus 로고
    • Regulation of oxysterol-binding protein Golgi localization through protein kinase D-mediated phosphorylation
    • S. Nhek, M. Ngo, X. Yang, M.M. Ng, S.J. Field, and J.M. Asara Regulation of oxysterol-binding protein Golgi localization through protein kinase D-mediated phosphorylation Mol Biol Cell 21 2010 2327 2337
    • (2010) Mol Biol Cell , vol.21 , pp. 2327-2337
    • Nhek, S.1    Ngo, M.2    Yang, X.3    Ng, M.M.4    Field, S.J.5    Asara, J.M.6
  • 55
    • 84862637666 scopus 로고    scopus 로고
    • Phosphatidylinositol 4-kinase IIalpha is palmitoylated by Golgi-localized palmitoyltransferases in cholesterol-dependent manner
    • D. Lu, H.Q. Sun, H. Wang, B. Barylko, Y. Fukata, and M. Fukata Phosphatidylinositol 4-kinase IIalpha is palmitoylated by Golgi-localized palmitoyltransferases in cholesterol-dependent manner J Biol Chem 287 2012 21856 21865
    • (2012) J Biol Chem , vol.287 , pp. 21856-21865
    • Lu, D.1    Sun, H.Q.2    Wang, H.3    Barylko, B.4    Fukata, Y.5    Fukata, M.6
  • 56
    • 0034789931 scopus 로고    scopus 로고
    • The organizing potential of sphingolipids in intracellular membrane transport
    • J.C. Holthuis, T. Pomorski, R.J. Raggers, H. Sprong, and G. Van Meer The organizing potential of sphingolipids in intracellular membrane transport Physiol Rev 81 2001 1689 1723
    • (2001) Physiol Rev , vol.81 , pp. 1689-1723
    • Holthuis, J.C.1    Pomorski, T.2    Raggers, R.J.3    Sprong, H.4    Van Meer, G.5
  • 58
    • 0345363228 scopus 로고    scopus 로고
    • Electrospray ionization tandem mass spectrometry (ESI-MS/MS) analysis of the lipid molecular species composition of yeast subcellular membranes reveals acyl chain-based sorting/remodeling of distinct molecular species en route to the plasma membrane
    • R. Schneiter, B. Brugger, R. Sandhoff, G. Zellnig, A. Leber, and M. Lampl Electrospray ionization tandem mass spectrometry (ESI-MS/MS) analysis of the lipid molecular species composition of yeast subcellular membranes reveals acyl chain-based sorting/remodeling of distinct molecular species en route to the plasma membrane J Cell Biol 146 1999 741 754
    • (1999) J Cell Biol , vol.146 , pp. 741-754
    • Schneiter, R.1    Brugger, B.2    Sandhoff, R.3    Zellnig, G.4    Leber, A.5    Lampl, M.6
  • 59
    • 66149094592 scopus 로고    scopus 로고
    • Segregation of sphingolipids and sterols during formation of secretory vesicles at the trans-Golgi network
    • R.W. Klemm, C.S. Ejsing, M.A. Surma, H.J. Kaiser, M.J. Gerl, and J.L. Sampaio Segregation of sphingolipids and sterols during formation of secretory vesicles at the trans-Golgi network J Cell Biol 185 2009 601 612
    • (2009) J Cell Biol , vol.185 , pp. 601-612
    • Klemm, R.W.1    Ejsing, C.S.2    Surma, M.A.3    Kaiser, H.J.4    Gerl, M.J.5    Sampaio, J.L.6
  • 60
    • 74849118341 scopus 로고    scopus 로고
    • Lipid rafts as a membrane-organizing principle
    • D. Lingwood, and K. Simons Lipid rafts as a membrane-organizing principle Science 327 2010 46 50
    • (2010) Science , vol.327 , pp. 46-50
    • Lingwood, D.1    Simons, K.2
  • 62
    • 84903316055 scopus 로고    scopus 로고
    • Validity and applicability of membrane model systems for studying interactions of peripheral membrane proteins with lipids
    • A. Czogalla, M. Grzybek, W. Jones, and Ü. Coskun Validity and applicability of membrane model systems for studying interactions of peripheral membrane proteins with lipids Biochim Biophys Acta Mol Cell Biol Lipids 1841 2014 1049 1059
    • (2014) Biochim Biophys Acta Mol Cell Biol Lipids , vol.1841 , pp. 1049-1059
    • Czogalla, A.1    Grzybek, M.2    Jones, W.3    Coskun Ü.4
  • 63
  • 64
    • 0033932033 scopus 로고    scopus 로고
    • A correlation between lipid domain shape and binary phospholipid mixture composition in free standing bilayers: A two-photon fluorescence microscopy study
    • L.A. Bagatolli, and E. Gratton A correlation between lipid domain shape and binary phospholipid mixture composition in free standing bilayers: A two-photon fluorescence microscopy study Biophys J 79 2000 434 447
    • (2000) Biophys J , vol.79 , pp. 434-447
    • Bagatolli, L.A.1    Gratton, E.2
  • 65
    • 33748929006 scopus 로고    scopus 로고
    • Thermofluor-based high-throughput stability optimization of proteins for structural studies
    • U.B. Ericsson, B.M. Hallberg, G.T. Detitta, N. Dekker, and P. Nordlund Thermofluor-based high-throughput stability optimization of proteins for structural studies Anal Biochem 357 2006 289 298
    • (2006) Anal Biochem , vol.357 , pp. 289-298
    • Ericsson, U.B.1    Hallberg, B.M.2    Detitta, G.T.3    Dekker, N.4    Nordlund, P.5
  • 66
    • 33845553743 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results
    • G. Lipari, and A. Szabo Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 2. Analysis of experimental results J Am Chem Soc 104 1982 4559 4570
    • (1982) J Am Chem Soc , vol.104 , pp. 4559-4570
    • Lipari, G.1    Szabo, A.2
  • 67
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
    • G. Lipari, and A. Szabo Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity J Am Chem Soc 104 1982 4546 4559
    • (1982) J Am Chem Soc , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 69
    • 44049118502 scopus 로고
    • Pulse sequences for removal of the effects of cross correlation between dipolar and chemical-shift anisotropy relaxation mechanisms on the measurement of heteronuclear T1 and T2 values in proteins
    • L.E. Kay, L.K. Nicholson, F. Delaglio, A. Bax, and D.A. Torchia Pulse sequences for removal of the effects of cross correlation between dipolar and chemical-shift anisotropy relaxation mechanisms on the measurement of heteronuclear T1 and T2 values in proteins J Magn Reson 97 1992 359 375
    • (1992) J Magn Reson , vol.97 , pp. 359-375
    • Kay, L.E.1    Nicholson, L.K.2    Delaglio, F.3    Bax, A.4    Torchia, D.A.5
  • 70
    • 0028941877 scopus 로고
    • Backbone dynamics of Escherichia coli ribonuclease HI: Correlations with structure and function in an active enzyme
    • A.M. Mandel, M. Akke, and A.G. Palmer Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme J Mol Biol 246 1995 144 163
    • (1995) J Mol Biol , vol.246 , pp. 144-163
    • Mandel, A.M.1    Akke, M.2    Palmer, A.G.3
  • 71
    • 0038068865 scopus 로고    scopus 로고
    • FAST-Modelfree: A program for rapid automated analysis of solution NMR spin-relaxation data
    • R. Cole, and J.P. Loria FAST-Modelfree: a program for rapid automated analysis of solution NMR spin-relaxation data J Biomol NMR 26 2003 203 213
    • (2003) J Biomol NMR , vol.26 , pp. 203-213
    • Cole, R.1    Loria, J.P.2
  • 72
  • 73
    • 19444382397 scopus 로고    scopus 로고
    • The CCPN data model for NMR spectroscopy: Development of a software pipeline
    • W.F. Vranken, W. Boucher, T.J. Stevens, R.H. Fogh, A. Pajon, and M. Llinas The CCPN data model for NMR spectroscopy: development of a software pipeline Proteins 59 2005 687 696
    • (2005) Proteins , vol.59 , pp. 687-696
    • Vranken, W.F.1    Boucher, W.2    Stevens, T.J.3    Fogh, R.H.4    Pajon, A.5    Llinas, M.6


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