메뉴 건너뛰기




Volumn 92, Issue 6, 2014, Pages 555-563

Discovery of novel membrane binding structures and functions

Author keywords

Bilayer insertion; Lipid site identification; Membrane interaction interface; Peripheral membrane protein; Phospholipid interaction; Protein structure annotation

Indexed keywords

BIOLOGICAL MEMBRANES; LIPID BILAYERS; MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHOSPHOLIPIDS; PROTEINS;

EID: 84911371378     PISSN: 08298211     EISSN: 12086002     Source Type: Journal    
DOI: 10.1139/bcb-2014-0074     Document Type: Article
Times cited : (45)

References (66)
  • 1
    • 0027955787 scopus 로고
    • Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins
    • 8289329
    • Abagyan R. Totrov M. 1994. Biased probability Monte Carlo conformational searches and electrostatic calculations for peptides and proteins. J. Mol. Biol. 235 (3): 983-1002. 10.1006/jmbi.1994.1052. 8289329.
    • (1994) J. Mol. Biol. , vol.235 , Issue.3 , pp. 983-1002
    • Abagyan, R.1    Totrov, M.2
  • 2
    • 0028304890 scopus 로고
    • Recognition of distantly related proteins through energy calculations
    • 8090707
    • Abagyan R. Frishman D. Argos P. 1994. Recognition of distantly related proteins through energy calculations. Proteins, 19 (2): 132-140. 10.1002/prot.340190206. 8090707.
    • (1994) Proteins , vol.19 , Issue.2 , pp. 132-140
    • Abagyan, R.1    Frishman, D.2    Argos, P.3
  • 3
    • 0036373119 scopus 로고    scopus 로고
    • 1H, 15N and 13C assignments of full length human ADP ribosylation factor 1 (ARF1) using triple resonance connectivities and dipolar couplings
    • 12238602
    • Amor J.C. Seidel R.D. III Tian F. Kahn R.A. Prestegard J.H. 2002. 1H, 15N and 13C assignments of full length human ADP ribosylation factor 1 (ARF1) using triple resonance connectivities and dipolar couplings. J. Biomol. NMR, 23 (3): 253-254. 10.1023/A:1019839607202. 12238602.
    • (2002) J. Biomol. NMR , vol.23 , Issue.3 , pp. 253-254
    • Amor, J.C.1    Tian, F.2    Kahn, R.A.3    Prestegard, J.H.4
  • 4
    • 84890875112 scopus 로고    scopus 로고
    • ALIX and the multivesicular endosome: ALIX in Wonderland
    • 24287454
    • Bissig C. Gruenberg J. 2014. ALIX and the multivesicular endosome: ALIX in Wonderland. Trends Cell Biol. 24 (1): 19-25. 10.1016/j.tcb.2013.10.009. 24287454.
    • (2014) Trends Cell Biol. , vol.24 , Issue.1 , pp. 19-25
    • Bissig, C.1    Gruenberg, J.2
  • 5
    • 84878368479 scopus 로고    scopus 로고
    • Viral infection controlled by a calcium-dependent lipid-binding module in ALIX. Dev
    • 23664863
    • Bissig C. Lenoir M. Velluz M.C. Kufareva I. Abagyan R. Overduin M. Gruenberg J. 2013. Viral infection controlled by a calcium-dependent lipid-binding module in ALIX. Dev. Cell, 25 (4): 364-373. 10.1016/j.devcel.2013.04.003. 23664863.
    • (2013) Cell , vol.25 , Issue.4 , pp. 364-373
    • Bissig, C.1    Lenoir, M.2    Velluz, M.C.3    Kufareva, I.4    Abagyan, R.5    Overduin, M.6    Gruenberg, J.7
  • 6
    • 6344284704 scopus 로고    scopus 로고
    • Interfacial binding of bee venom secreted phospholipase A2 to membranes occurs predominantly by a nonelectrostatic mechanism
    • 15491136
    • Bollinger J.G. Diraviyam K. Ghomashchi F. Murray D. Gelb M.H. 2004. Interfacial binding of bee venom secreted phospholipase A2 to membranes occurs predominantly by a nonelectrostatic mechanism. Biochemistry, 43 (42): 13293-13304. 10.1021/bi049390i. 15491136.
    • (2004) Biochemistry , vol.43 , Issue.42 , pp. 13293-13304
    • Bollinger, J.G.1    Diraviyam, K.2    Ghomashchi, F.3    Murray, D.4    Gelb, M.H.5
  • 7
    • 17944367436 scopus 로고    scopus 로고
    • The crystal structure of the PX domain from p40(phox) bound to phosphatidylinositol 3-phosphate
    • 11684018
    • Bravo J. Karathanassis D. Pacold C.M. Pacold M.E. Ellson C.D. Anderson K.E. et al 2001. The crystal structure of the PX domain from p40(phox) bound to phosphatidylinositol 3-phosphate. Mol. Cell, 8 (4): 829-839. 10.1016/S1097-2765(01)00372-0. 11684018.
    • (2001) Mol. Cell , vol.8 , Issue.4 , pp. 829-839
    • Bravo, J.1    Karathanassis, D.2    Pacold, C.M.3    Pacold, M.E.4    Ellson, C.D.5    Anderson, K.E.6
  • 8
    • 0000049034 scopus 로고    scopus 로고
    • Lipid binding ridge on loops 2 and 3 of the C2A domain of synaptotagmin i as revealed by NMR spectroscopy
    • 9748232
    • Chae Y.K. Abildgaard F. Chapman E.R. Markley J.L. 1998. Lipid binding ridge on loops 2 and 3 of the C2A domain of synaptotagmin I as revealed by NMR spectroscopy. J. Biol. Chem. 273 (40): 25659-25663. 10.1074/jbc.273.40.25659. 9748232.
    • (1998) J. Biol. Chem. , vol.273 , Issue.40 , pp. 25659-25663
    • Chae, Y.K.1    Abildgaard, F.2    Chapman, E.R.3    Markley, J.L.4
  • 9
    • 4644348988 scopus 로고    scopus 로고
    • Crystallographic identification of Ca2+ and Sr2+ coordination sites in synaptotagmin i C2B domain
    • 15340165
    • Cheng Y. Sequeira S.M. Malinina L. Tereshko V. Sollner T.H. Patel D.J. 2004. Crystallographic identification of Ca2+ and Sr2+ coordination sites in synaptotagmin I C2B domain. Protein Sci. 13 (10): 2665-2672. 10.1110/ps.04832604. 15340165.
    • (2004) Protein Sci. , vol.13 , Issue.10 , pp. 2665-2672
    • Cheng, Y.1    Sequeira, S.M.2    Malinina, L.3    Tereshko, V.4    Sollner, T.H.5    Patel, D.J.6
  • 10
    • 20544475665 scopus 로고    scopus 로고
    • Membrane-protein interactions in cell signaling and membrane trafficking
    • 15869386
    • Cho W. Stahelin R.V. 2005. Membrane-protein interactions in cell signaling and membrane trafficking. Annu. Rev. Biophys. Biomol. Struct. 34: 119-151. 10.1146/annurev.biophys.33.110502.133337. 15869386.
    • (2005) Annu. Rev. Biophys. Biomol. Struct. , vol.34 , pp. 119-151
    • Cho, W.1    Stahelin, R.V.2
  • 11
    • 0033617291 scopus 로고    scopus 로고
    • Crystal structure of human cytosolic phospholipase A2 reveals a novel topology and catalytic mechanism
    • 10319815
    • Dessen A. Tang J. Schmidt H. Stahl M. Clark J.D. Seehra J. Somers W.S. 1999. Crystal structure of human cytosolic phospholipase A2 reveals a novel topology and catalytic mechanism. Cell, 97 (3): 349-360. 10.1016/S0092-8674(00)80744-8. 10319815.
    • (1999) Cell , vol.97 , Issue.3 , pp. 349-360
    • Dessen, A.1    Tang, J.2    Schmidt, H.3    Stahl, M.4    Clark, J.D.5    Seehra, J.6    Somers, W.S.7
  • 12
    • 0035930332 scopus 로고    scopus 로고
    • Multivalent endosome targeting by homodimeric EEA1
    • 11741531
    • Dumas J.J. Merithew E. Sudharshan E. Rajamani D. Hayes S. Lawe D. et al 2001. Multivalent endosome targeting by homodimeric EEA1. Mol. Cell, 8 (5): 947-958. 10.1016/S1097-2765(01)00385-9. 11741531.
    • (2001) Mol. Cell , vol.8 , Issue.5 , pp. 947-958
    • Dumas, J.J.1    Merithew, E.2    Sudharshan, E.3    Rajamani, D.4    Hayes, S.5    Lawe, D.6
  • 13
    • 0035968172 scopus 로고    scopus 로고
    • The omega-loop region of the human prothrombin gamma-carboxyglutamic acid domain penetrates anionic phospholipid membranes
    • 11312259
    • Falls L.A. Furie B.C. Jacobs M. Furie B. Rigby A.C. 2001. The omega-loop region of the human prothrombin gamma-carboxyglutamic acid domain penetrates anionic phospholipid membranes. J. Biol. Chem. 276 (26): 23895-23902. 10.1074/jbc.M008332200. 11312259.
    • (2001) J. Biol. Chem. , vol.276 , Issue.26 , pp. 23895-23902
    • Falls, L.A.1    Furie, B.C.2    Jacobs, M.3    Furie, B.4    Rigby, A.C.5
  • 14
    • 0037205478 scopus 로고    scopus 로고
    • Role of tryptophan residues in interfacial binding of phosphatidylinositol-specific phospholipase C
    • 11912206
    • Feng J. Wehbi H. Roberts M.F. 2002. Role of tryptophan residues in interfacial binding of phosphatidylinositol-specific phospholipase C. J. Biol. Chem. 277 (22): 19867-19875. 10.1074/jbc.M200938200. 11912206.
    • (2002) J. Biol. Chem. , vol.277 , Issue.22 , pp. 19867-19875
    • Feng, J.1    Wehbi, H.2    Roberts, M.F.3
  • 15
    • 10844235653 scopus 로고    scopus 로고
    • Optimal docking area: A new method for predicting protein-protein interaction sites
    • 15495260
    • Fernandez-Recio J. Totrov M. Skorodumov C. Abagyan R. 2005. Optimal docking area: a new method for predicting protein-protein interaction sites. Proteins, 58 (1): 134-143. 10.1002/prot.20285. 15495260.
    • (2005) Proteins , vol.58 , Issue.1 , pp. 134-143
    • Fernandez-Recio, J.1    Totrov, M.2    Skorodumov, C.3    Abagyan, R.4
  • 16
    • 33847355934 scopus 로고    scopus 로고
    • Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding
    • 17350572
    • Fisher R.D. Chung H.Y. Zhai Q. Robinson H. Sundquist W.I. Hill C.P. 2007. Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding. Cell, 128 (5): 841-852. 10.1016/j.cell.2007.01.035. 17350572.
    • (2007) Cell , vol.128 , Issue.5 , pp. 841-852
    • Fisher, R.D.1    Chung, H.Y.2    Zhai, Q.3    Robinson, H.4    Sundquist, W.I.5    Hill, C.P.6
  • 18
    • 0037150098 scopus 로고    scopus 로고
    • Membrane orientation and position of the C2 domain from cPLA2 by site-directed spin labeling
    • 12009889
    • Frazier A.A. Wisner M.A. Malmberg N.J. Victor K.G. Fanucci G.E. Nalefski E.A. et al 2002. Membrane orientation and position of the C2 domain from cPLA2 by site-directed spin labeling. Biochemistry, 41 (20): 6282-6292. 10.1021/bi0160821. 12009889.
    • (2002) Biochemistry , vol.41 , Issue.20 , pp. 6282-6292
    • Frazier, A.A.1    Wisner, M.A.2    Malmberg, N.J.3    Victor, K.G.4    Fanucci, G.E.5    Nalefski, E.A.6
  • 19
    • 0037435606 scopus 로고    scopus 로고
    • Membrane-bound orientation and position of the synaptotagmin i C2A domain by site-directed spin labeling
    • 12515543
    • Frazier A.A. Roller C.R. Havelka J.J. Hinderliter A. Cafiso D.S. 2003. Membrane-bound orientation and position of the synaptotagmin I C2A domain by site-directed spin labeling. Biochemistry, 42 (1): 96-105. 10.1021/bi0268145. 12515543.
    • (2003) Biochemistry , vol.42 , Issue.1 , pp. 96-105
    • Frazier, A.A.1    Roller, C.R.2    Havelka, J.J.3    Hinderliter, A.4    Cafiso, D.S.5
  • 20
    • 0032510696 scopus 로고    scopus 로고
    • Interfacial recognition by bee venom phospholipase A2: Insights into nonelectrostatic molecular determinants by charge reversal mutagenesis
    • 9578553
    • Ghomashchi F. Lin Y. Hixon M.S. Yu B.Z. Annand R. Jain M.K. Gelb M.H. 1998. Interfacial recognition by bee venom phospholipase A2: insights into nonelectrostatic molecular determinants by charge reversal mutagenesis. Biochemistry, 37 (19): 6697-6710. 10.1021/bi972525i. 9578553.
    • (1998) Biochemistry , vol.37 , Issue.19 , pp. 6697-6710
    • Ghomashchi, F.1    Lin, Y.2    Hixon, M.S.3    Yu, B.Z.4    Annand, R.5    Jain, M.K.6    Gelb, M.H.7
  • 21
    • 79956320991 scopus 로고    scopus 로고
    • Molecular basis of phosphatidylinositol 4-phosphate and ARF1 GTPase recognition by the FAPP1 pleckstrin homology (PH) domain
    • 21454700
    • He J. Scott J.L. Heroux A. Roy S. Lenoir M. Overduin M. et al 2011. Molecular basis of phosphatidylinositol 4-phosphate and ARF1 GTPase recognition by the FAPP1 pleckstrin homology (PH) domain. J. Biol. Chem. 286 (21): 18650-18657. 10.1074/jbc.M111.233015. 21454700.
    • (2011) J. Biol. Chem. , vol.286 , Issue.21 , pp. 18650-18657
    • He, J.1    Scott, J.L.2    Heroux, A.3    Roy, S.4    Lenoir, M.5    Overduin, M.6
  • 22
    • 0345448246 scopus 로고    scopus 로고
    • The F-G loop region of cytochrome P450scc (CYP11A1) interacts with the phospholipid membrane
    • 14637024
    • Headlam M.J. Wilce M.C. Tuckey R.C. 2003. The F-G loop region of cytochrome P450scc (CYP11A1) interacts with the phospholipid membrane. Biochim. Biophys. Acta, 1617 (1-2): 96-108. 10.1016/j.bbamem.2003.09.007. 14637024.
    • (2003) Biochim. Biophys. Acta , vol.1617 , Issue.12 , pp. 96-108
    • Headlam, M.J.1    Wilce, M.C.2    Tuckey, R.C.3
  • 23
    • 0029740871 scopus 로고    scopus 로고
    • Crystal structure of phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with glucosaminyl(alpha 1->6)-D-myo-inositol, an essential fragment of GPI anchors
    • 8755729
    • Heinz D.W. Ryan M. Smith M.P. Weaver L.H. Keana J.F. Griffith O.H. 1996. Crystal structure of phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with glucosaminyl(alpha 1->6)-D-myo-inositol, an essential fragment of GPI anchors. Biochemistry, 35 (29): 9496-9504. 10.1021/bi9606105. 8755729.
    • (1996) Biochemistry , vol.35 , Issue.29 , pp. 9496-9504
    • Heinz, D.W.1    Ryan, M.2    Smith, M.P.3    Weaver, L.H.4    Keana, J.F.5    Griffith, O.H.6
  • 24
    • 0041819513 scopus 로고    scopus 로고
    • Structural basis of membrane binding by Gla domains of vitamin K-dependent proteins
    • 12923575
    • Huang M. Rigby A.C. Morelli X. Grant M.A. Huang G. Furie B. et al 2003. Structural basis of membrane binding by Gla domains of vitamin K-dependent proteins. Nat. Struct. Biol. 10 (9): 751-756. 10.1038/nsb971. 12923575.
    • (2003) Nat. Struct. Biol. , vol.10 , Issue.9 , pp. 751-756
    • Huang, M.1    Rigby, A.C.2    Morelli, X.3    Grant, M.A.4    Huang, G.5    Furie, B.6
  • 25
    • 0036791737 scopus 로고    scopus 로고
    • Binding of the PX domain of p47(phox) to phosphatidylinositol 3,4-bisphosphate and phosphatidic acid is masked by an intramolecular interaction
    • 12356722
    • Karathanassis D. Stahelin R.V. Bravo J. Perisic O. Pacold C.M. Cho W. Williams R.L. 2002. Binding of the PX domain of p47(phox) to phosphatidylinositol 3,4-bisphosphate and phosphatidic acid is masked by an intramolecular interaction. EMBO J. 21 (19): 5057-5068. 10.1093/emboj/cdf519. 12356722.
    • (2002) EMBO J. , vol.21 , Issue.19 , pp. 5057-5068
    • Karathanassis, D.1    Stahelin, R.V.2    Bravo, J.3    Perisic, O.4    Pacold, C.M.5    Cho, W.6    Williams, R.L.7
  • 26
    • 0026784217 scopus 로고
    • Comparative analysis of normal and growth-retarded placentas with phosphorus nuclear magnetic resonance spectroscopy
    • 1497068
    • Kay H.H. Hawkins S.R. Gordon J.D. Wang Y. Ribeiro A.A. Spicer L.D. 1992. Comparative analysis of normal and growth-retarded placentas with phosphorus nuclear magnetic resonance spectroscopy. Am. J. Obstet. Gynecol. 167 (2): 548-553. 10.1016/S0002-9378(11)91451-3. 1497068.
    • (1992) Am. J. Obstet. Gynecol. , vol.167 , Issue.2 , pp. 548-553
    • Kay, H.H.1    Hawkins, S.R.2    Gordon, J.D.3    Wang, Y.4    Ribeiro, A.A.5    Spicer, L.D.6
  • 27
    • 0347298574 scopus 로고    scopus 로고
    • C2 domain of protein kinase C alpha: Elucidation of the membrane docking surface by site-directed fluorescence and spin labeling
    • 12564928
    • Kohout S.C. Corbalan-Garcia S. Gomez-Fernandez J.C. Falke J.J. 2003. C2 domain of protein kinase C alpha: elucidation of the membrane docking surface by site-directed fluorescence and spin labeling. Biochemistry, 42 (5): 1254-1265. 10.1021/bi026596f. 12564928.
    • (2003) Biochemistry , vol.42 , Issue.5 , pp. 1254-1265
    • Kohout, S.C.1    Corbalan-Garcia, S.2    Gomez-Fernandez, J.C.3    Falke, J.J.4
  • 28
    • 33947360625 scopus 로고    scopus 로고
    • PIER: Protein interface recognition for structural proteomics
    • 17299750
    • Kufareva I. Budagyan L. Raush E. Totrov M. Abagyan R. 2007. PIER: protein interface recognition for structural proteomics. Proteins, 67 (2): 400-417. 10.1002/prot.21233. 17299750.
    • (2007) Proteins , vol.67 , Issue.2 , pp. 400-417
    • Kufareva, I.1    Budagyan, L.2    Raush, E.3    Totrov, M.4    Abagyan, R.5
  • 29
    • 0033626262 scopus 로고    scopus 로고
    • Sequence-specific 1H, 15N and 13C resonance assignments of the EEA1 FYVE domain
    • 10909872
    • Kutateladze T.G. Overduin M. 2000. Sequence-specific 1H, 15N and 13C resonance assignments of the EEA1 FYVE domain. J. Biomol. NMR, 17 (1): 89-90. 10909872.
    • (2000) J. Biomol. NMR , vol.17 , Issue.1 , pp. 89-90
    • Kutateladze, T.G.1    Overduin, M.2
  • 31
    • 0038281249 scopus 로고    scopus 로고
    • Phosphoinositide recognition domains
    • 12694559
    • Lemmon M.A. 2003. Phosphoinositide recognition domains. Traffic, 4 (4): 201-213. 10.1034/j.1600-0854.2004.00071.x. 12694559.
    • (2003) Traffic , vol.4 , Issue.4 , pp. 201-213
    • Lemmon, M.A.1
  • 32
    • 84872115717 scopus 로고    scopus 로고
    • Pleckstrin homology (PH) domains and phosphoinositides
    • 17233582
    • Lemmon M.A. 2007. Pleckstrin homology (PH) domains and phosphoinositides. Biochem. Soc. Symp. 74: 81-93. 10.1042/BSS0740081. 17233582.
    • (2007) Biochem. Soc. Symp. , vol.74 , pp. 81-93
    • Lemmon, M.A.1
  • 33
    • 77950370938 scopus 로고    scopus 로고
    • Structural basis of wedging the Golgi membrane by FAPP pleckstrin homology domains
    • 20300118
    • Lenoir M. Coskun U. Grzybek M. Cao X. Buschhorn S.B. James J. et al 2010. Structural basis of wedging the Golgi membrane by FAPP pleckstrin homology domains. EMBO Rep. 11 (4): 279-284. 10.1038/embor.2010.28. 20300118.
    • (2010) EMBO Rep. , vol.11 , Issue.4 , pp. 279-284
    • Lenoir, M.1    Coskun, U.2    Grzybek, M.3    Cao, X.4    Buschhorn, S.B.5    James, J.6
  • 34
    • 0032549181 scopus 로고    scopus 로고
    • Docking phospholipase A2 on membranes using electrostatic potential-modulated spin relaxation magnetic resonance
    • 9506941
    • Lin Y. Nielsen R. Murray D. Hubbell W.L. Mailer C. Robinson B.H. Gelb M.H. 1998. Docking phospholipase A2 on membranes using electrostatic potential-modulated spin relaxation magnetic resonance. Science, 279 (5358): 1925-1929. 10.1126/science.279.5358.1925. 9506941.
    • (1998) Science , vol.279 , Issue.5358 , pp. 1925-1929
    • Lin, Y.1    Nielsen, R.2    Murray, D.3    Hubbell, W.L.4    Mailer, C.5    Robinson, B.H.6    Gelb, M.H.7
  • 35
    • 77954382701 scopus 로고    scopus 로고
    • Dynamic structure of membrane-anchored Arf GTP
    • 20601958
    • Liu Y. Kahn R.A. Prestegard J.H. 2010. Dynamic structure of membrane-anchored Arf GTP. Nat. Struct. Mol. Biol. 17 (7): 876-881. 10.1038/nsmb.1853. 20601958.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , Issue.7 , pp. 876-881
    • Liu, Y.1    Kahn, R.A.2    Prestegard, J.H.3
  • 36
    • 84896691337 scopus 로고    scopus 로고
    • Interaction of Fapp1 with Arf1 and PI4P at a membrane surface: An example of coincidence detection
    • 24462251
    • Liu Y. Kahn R.A. Prestegard J.H. 2014. Interaction of Fapp1 with Arf1 and PI4P at a membrane surface: an example of coincidence detection. Structure, 22 (3): 421-430. 10.1016/j.str.2013.12.011. 24462251.
    • (2014) Structure , vol.22 , Issue.3 , pp. 421-430
    • Liu, Y.1    Kahn, R.A.2    Prestegard, J.H.3
  • 37
    • 0036239041 scopus 로고    scopus 로고
    • The mirrored methionine sulfoxide reductases of Neisseria gonorrhoeae pilB
    • 11938352
    • Lowther W.T. Weissbach H. Etienne F. Brot N. Matthews B.W. 2002. The mirrored methionine sulfoxide reductases of Neisseria gonorrhoeae pilB. Nat. Struct. Biol. 9 (5): 348-352. 10.1038/nsb783. 11938352.
    • (2002) Nat. Struct. Biol. , vol.9 , Issue.5 , pp. 348-352
    • Lowther, W.T.1    Weissbach, H.2    Etienne, F.3    Brot, N.4    Matthews, B.W.5
  • 38
    • 0033604610 scopus 로고    scopus 로고
    • Crystal structures of the membrane-binding C2 domain of human coagulation factor v
    • 10586886
    • Macedo-Ribeiro S. Bode W. Huber R. Quinn-Allen M.A. Kim S.W. Ortel T.L. et al 1999. Crystal structures of the membrane-binding C2 domain of human coagulation factor V. Nature, 402 (6760): 434-439. 10.1038/46594. 10586886.
    • (1999) Nature , vol.402 , Issue.6760 , pp. 434-439
    • Macedo-Ribeiro, S.1    Bode, W.2    Huber, R.3    Quinn-Allen, M.A.4    Kim, S.W.5    Ortel, T.L.6
  • 39
    • 0034681262 scopus 로고    scopus 로고
    • Crystal structure of the VHS and FYVE tandem domains of Hrs, a protein involved in membrane trafficking and signal transduction
    • 10693761
    • Mao Y. Nickitenko A. Duan X. Lloyd T.E. Wu M.N. Bellen H. Quiocho F.A. 2000. Crystal structure of the VHS and FYVE tandem domains of Hrs, a protein involved in membrane trafficking and signal transduction. Cell, 100 (4): 447-456. 10.1016/S0092-8674(00)80680-7. 10693761.
    • (2000) Cell , vol.100 , Issue.4 , pp. 447-456
    • Mao, Y.1    Nickitenko, A.2    Duan, X.3    Lloyd, T.E.4    Wu, M.N.5    Bellen, H.6    Quiocho, F.A.7
  • 40
    • 0033612372 scopus 로고    scopus 로고
    • Crystal structure of a phosphatidylinositol 3-phosphate-specific membrane-targeting motif, the FYVE domain of Vps27p
    • 10367894
    • Misra S. Hurley J.H. 1999. Crystal structure of a phosphatidylinositol 3-phosphate-specific membrane-targeting motif, the FYVE domain of Vps27p. Cell, 97 (5): 657-666. 10.1016/S0092-8674(00)80776-X. 10367894.
    • (1999) Cell , vol.97 , Issue.5 , pp. 657-666
    • Misra, S.1    Hurley, J.H.2
  • 41
    • 0035977019 scopus 로고    scopus 로고
    • The role of electrostatic interactions in the regulation of the membrane association of G protein beta gamma heterodimers
    • 11557749
    • Murray D. McLaughlin S. Honig B. 2001. The role of electrostatic interactions in the regulation of the membrane association of G protein beta gamma heterodimers. J. Biol. Chem. 276 (48): 45153-45159. 10.1074/jbc.M101784200. 11557749.
    • (2001) J. Biol. Chem. , vol.276 , Issue.48 , pp. 45153-45159
    • Murray, D.1    McLaughlin, S.2    Honig, B.3
  • 42
    • 0036973429 scopus 로고    scopus 로고
    • Backbone 1H, 13C, and 15N resonance assignments of the von Willebrand factor A3 domain
    • 12522300
    • Nishida N. Miyazawa M. Sumikawa H. Sakakura M. Shimba N. Takahashi H. et al 2002. Backbone 1H, 13C, and 15N resonance assignments of the von Willebrand factor A3 domain. J. Biomol. NMR, 24 (4): 357-358. 10.1023/A:1021669129988. 12522300.
    • (2002) J. Biomol. NMR , vol.24 , Issue.4 , pp. 357-358
    • Nishida, N.1    Miyazawa, M.2    Sumikawa, H.3    Sakakura, M.4    Shimba, N.5    Takahashi, H.6
  • 43
    • 36849088540 scopus 로고    scopus 로고
    • Solution NMR of membrane proteins in bilayer mimics: Small is beautiful, but sometimes bigger is better
    • 17961504
    • Poget S.F. Girvin M.E. 2007. Solution NMR of membrane proteins in bilayer mimics: small is beautiful, but sometimes bigger is better. Biochim. Biophys. Acta, 1768 (12): 3098-3106. 10.1016/j.bbamem.2007.09.006. 17961504.
    • (2007) Biochim. Biophys. Acta , vol.1768 , Issue.12 , pp. 3098-3106
    • Poget, S.F.1    Girvin, M.E.2
  • 44
    • 0033604501 scopus 로고    scopus 로고
    • Structure of the C2 domain of human factor VIII at 1.5 A resolution
    • 10586887
    • Pratt K.P. Shen B.W. Takeshima K. Davie E.W. Fujikawa K. Stoddard B.L. 1999. Structure of the C2 domain of human factor VIII at 1.5 A resolution. Nature, 402 (6760): 439-442. 10.1038/46601. 10586887.
    • (1999) Nature , vol.402 , Issue.6760 , pp. 439-442
    • Pratt, K.P.1    Shen, B.W.2    Takeshima, K.3    Davie, E.W.4    Fujikawa, K.5    Stoddard, B.L.6
  • 45
    • 84874033425 scopus 로고    scopus 로고
    • Structural basis for recruitment and activation of the AP-1 clathrin adaptor complex by Arf1
    • 23415225
    • Ren X. Farias G.G. Canagarajah B.J. Bonifacino J.S. Hurley J.H. 2013. Structural basis for recruitment and activation of the AP-1 clathrin adaptor complex by Arf1. Cell, 152 (4): 755-767. 10.1016/j.cell.2012.12.042. 23415225.
    • (2013) Cell , vol.152 , Issue.4 , pp. 755-767
    • Ren, X.1    Farias, G.G.2    Canagarajah, B.J.3    Bonifacino, J.S.4    Hurley, J.H.5
  • 46
    • 79955030496 scopus 로고    scopus 로고
    • Toward a definition of the complete proteome of plant peroxisomes: Where experimental proteomics must be complemented by bioinformatics
    • 21472859
    • Reumann S. 2011. Toward a definition of the complete proteome of plant peroxisomes: Where experimental proteomics must be complemented by bioinformatics. Proteomics, 11 (9): 1764-1779. 10.1002/pmic.201000681. 21472859.
    • (2011) Proteomics , vol.11 , Issue.9 , pp. 1764-1779
    • Reumann, S.1
  • 47
    • 0035971244 scopus 로고    scopus 로고
    • Identification of the collagen-binding site of the von Willebrand factor A3-domain
    • 11098050
    • Romijn R.A. Bouma B. Wuyster W. Gros P. Kroon J. Sixma J.J. Huizinga E.G. 2001. Identification of the collagen-binding site of the von Willebrand factor A3-domain. J. Biol. Chem. 276 (13): 9985-9991. 10.1074/jbc.M006548200. 11098050.
    • (2001) J. Biol. Chem. , vol.276 , Issue.13 , pp. 9985-9991
    • Romijn, R.A.1    Bouma, B.2    Wuyster, W.3    Gros, P.4    Kroon, J.5    Sixma, J.J.6    Huizinga, E.G.7
  • 48
    • 11844254393 scopus 로고    scopus 로고
    • Membrane-bound orientation and position of the synaptotagmin C2B domain determined by site-directed spin labeling
    • 15628842
    • Rufener E. Frazier A.A. Wieser C.M. Hinderliter A. Cafiso D.S. 2005. Membrane-bound orientation and position of the synaptotagmin C2B domain determined by site-directed spin labeling. Biochemistry, 44 (1): 18-28. 10.1021/bi048370d. 15628842.
    • (2005) Biochemistry , vol.44 , Issue.1 , pp. 18-28
    • Rufener, E.1    Frazier, A.A.2    Wieser, C.M.3    Hinderliter, A.4    Cafiso, D.S.5
  • 49
    • 0032742855 scopus 로고    scopus 로고
    • PI transfer protein: The specific recognition of phospholipids and its functions
    • 10570254
    • Sha B. Luo M. 1999. PI transfer protein: the specific recognition of phospholipids and its functions. Biochim. Biophys. Acta, 1441 (2-3): 268-277. 10.1016/S1388-1981(99)00162-6. 10570254.
    • (1999) Biochim. Biophys. Acta , vol.1441 , Issue.23 , pp. 268-277
    • Sha, B.1    Luo, M.2
  • 50
    • 0032576758 scopus 로고    scopus 로고
    • Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol-transfer protein
    • 9461221
    • Sha B. Phillips S.E. Bankaitis V.A. Luo M. 1998. Crystal structure of the Saccharomyces cerevisiae phosphatidylinositol-transfer protein. Nature, 391 (6666): 506-510. 10.1038/35179. 9461221.
    • (1998) Nature , vol.391 , Issue.6666 , pp. 506-510
    • Sha, B.1    Phillips, S.E.2    Bankaitis, V.A.3    Luo, M.4
  • 51
    • 0037162478 scopus 로고    scopus 로고
    • The outer membrane localization of the Neisseria gonorrhoeae MsrA/B is involved in survival against reactive oxygen species
    • 12096194
    • Skaar E.P. Tobiason D.M. Quick J. Judd R.C. Weissbach H. Etienne F. et al 2002. The outer membrane localization of the Neisseria gonorrhoeae MsrA/B is involved in survival against reactive oxygen species. Proc. Natl. Acad. Sci. U.S.A. 99 (15): 10108-10113. 10.1073/pnas.152334799. 12096194.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , Issue.15 , pp. 10108-10113
    • Skaar, E.P.1    Tobiason, D.M.2    Quick, J.3    Judd, R.C.4    Weissbach, H.5    Etienne, F.6
  • 52
    • 33644869406 scopus 로고    scopus 로고
    • Paratope determination of the antithrombotic antibody 82D6A3 based on the crystal structure of its complex with the von Willebrand factor A3-domain
    • 16314412
    • Staelens S. Hadders M.A. Vauterin S. Platteau C. De Maeyer M. Vanhoorelbeke K. et al 2006. Paratope determination of the antithrombotic antibody 82D6A3 based on the crystal structure of its complex with the von Willebrand factor A3-domain. J. Biol. Chem. 281 (4): 2225-2231. 10.1074/jbc.M508191200. 16314412.
    • (2006) J. Biol. Chem. , vol.281 , Issue.4 , pp. 2225-2231
    • Staelens, S.1    Hadders, M.A.2    Vauterin, S.3    Platteau, C.4    De Maeyer, M.5    Vanhoorelbeke, K.6
  • 53
    • 0037135529 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-phosphate induces the membrane penetration of the FYVE domains of Vps27p and Hrs
    • 12006563
    • Stahelin R.V. Long F. Diraviyam K. Bruzik K.S. Murray D. Cho W. 2002. Phosphatidylinositol 3-phosphate induces the membrane penetration of the FYVE domains of Vps27p and Hrs. J. Biol. Chem. 277 (29): 26379-26388. 10.1074/jbc.M201106200. 12006563.
    • (2002) J. Biol. Chem. , vol.277 , Issue.29 , pp. 26379-26388
    • Stahelin, R.V.1    Long, F.2    Diraviyam, K.3    Bruzik, K.S.4    Murray, D.5    Cho, W.6
  • 54
    • 0037853270 scopus 로고    scopus 로고
    • Membrane binding mechanisms of the PX domains of NADPH oxidase p40phox and p47phox
    • 12556460
    • Stahelin R.V. Burian A. Bruzik K.S. Murray D. Cho W. 2003. Membrane binding mechanisms of the PX domains of NADPH oxidase p40phox and p47phox. J. Biol. Chem. 278 (16): 14469-14479. 10.1074/jbc.M212579200. 12556460.
    • (2003) J. Biol. Chem. , vol.278 , Issue.16 , pp. 14469-14479
    • Stahelin, R.V.1    Burian, A.2    Bruzik, K.S.3    Murray, D.4    Cho, W.5
  • 55
    • 0028986240 scopus 로고
    • Structure of the first C2 domain of synaptotagmin I: A novel Ca2+/phospholipid-binding fold
    • 7697723
    • Sutton R.B. Davletov B.A. Berghuis A.M. Sudhof T.C. Sprang S.R. 1995. Structure of the first C2 domain of synaptotagmin I: a novel Ca2+/phospholipid-binding fold. Cell, 80 (6): 929-938. 10.1016/0092-8674(95)90296-1. 7697723.
    • (1995) Cell , vol.80 , Issue.6 , pp. 929-938
    • Sutton, R.B.1    Davletov, B.A.2    Berghuis, A.M.3    Sudhof, T.C.4    Sprang, S.R.5
  • 56
    • 9244229075 scopus 로고    scopus 로고
    • 1H, 13C and 15N resonance assignment of the methionine sulfoxide reductase B from Neisseria meningitidis
    • 15557807
    • Thureau A. Olry A. Coudevylle N. Azza S. Boschi-Muller S. Branlant G. Cung M.T. 2004. 1H, 13C and 15N resonance assignment of the methionine sulfoxide reductase B from Neisseria meningitidis. J. Biomol. NMR, 30 (2): 223-224. 10.1023/B:JNMR.0000048851.95591.80. 15557807.
    • (2004) J. Biomol. NMR , vol.30 , Issue.2 , pp. 223-224
    • Thureau, A.1    Olry, A.2    Coudevylle, N.3    Azza, S.4    Boschi-Muller, S.5    Branlant, G.6    Cung, M.T.7
  • 57
    • 33845277313 scopus 로고    scopus 로고
    • Structure of Arabidopsis thaliana At1g77540 protein, a minimal acetyltransferase from the COG2388 family
    • 17128971
    • Tyler R.C. Bitto E. Berndsen C.E. Bingman C.A. Singh S. Lee M.S. et al 2006. Structure of Arabidopsis thaliana At1g77540 protein, a minimal acetyltransferase from the COG2388 family. Biochemistry, 45 (48): 14325-14336. 10.1021/bi0612059. 17128971.
    • (2006) Biochemistry , vol.45 , Issue.48 , pp. 14325-14336
    • Tyler, R.C.1    Bitto, E.2    Berndsen, C.E.3    Bingman, C.A.4    Singh, S.5    Lee, M.S.6
  • 58
    • 0033571223 scopus 로고    scopus 로고
    • Ca(2+) bridges the C2 membrane-binding domain of protein kinase Calpha directly to phosphatidylserine
    • 10562545
    • Verdaguer N. Corbalan-Garcia S. Ochoa W.F. Fita I. Gomez-Fernandez J.C. 1999. Ca(2+) bridges the C2 membrane-binding domain of protein kinase Calpha directly to phosphatidylserine. EMBO J. 18 (22): 6329-6338. 10.1093/emboj/18.22.6329. 10562545.
    • (1999) EMBO J. , vol.18 , Issue.22 , pp. 6329-6338
    • Verdaguer, N.1    Corbalan-Garcia, S.2    Ochoa, W.F.3    Fita, I.4    Gomez-Fernandez, J.C.5
  • 59
    • 0035377312 scopus 로고    scopus 로고
    • Role of hydrophobic residues in the C1b domain of protein kinase C delta on ligand and phospholipid interactions
    • 11278612
    • Wang Q.J. Fang T.W. Nacro K. Marquez V.E. Wang S. Blumberg P.M. 2001. Role of hydrophobic residues in the C1b domain of protein kinase C delta on ligand and phospholipid interactions. J. Biol. Chem. 276 (22): 19580-19587. 10.1074/jbc.M010089200. 11278612.
    • (2001) J. Biol. Chem. , vol.276 , Issue.22 , pp. 19580-19587
    • Wang, Q.J.1    Fang, T.W.2    Nacro, K.3    Marquez, V.E.4    Wang, S.5    Blumberg, P.M.6
  • 60
    • 0034738973 scopus 로고    scopus 로고
    • Microsomal cytochrome P450 2C5: Comparison to microbial P450s and unique features
    • 11051563
    • Williams P.A. Cosme J. Sridhar V. Johnson E.F. McRee D.E. 2000. Microsomal cytochrome P450 2C5: comparison to microbial P450s and unique features. J. Inorg. Biochem. 81 (3): 183-190. 10.1016/S0162-0134(00)00102-1. 11051563.
    • (2000) J. Inorg. Biochem. , vol.81 , Issue.3 , pp. 183-190
    • Williams, P.A.1    Cosme, J.2    Sridhar, V.3    Johnson, E.F.4    McRee, D.E.5
  • 61
    • 0042667012 scopus 로고    scopus 로고
    • Structural analysis of lipid complexes of GM2-activator protein
    • 12909021
    • Wright C.S. Zhao Q. Rastinejad F. 2003. Structural analysis of lipid complexes of GM2-activator protein. J. Mol. Biol. 331 (4): 951-964. 10.1016/S0022-2836(03)00794-0. 12909021.
    • (2003) J. Mol. Biol. , vol.331 , Issue.4 , pp. 951-964
    • Wright, C.S.1    Zhao, Q.2    Rastinejad, F.3
  • 62
    • 3142655870 scopus 로고    scopus 로고
    • Structural basis of membrane targeting by the Phox homology domain of cytokine-independent survival kinase (CISK-PX)
    • 15126499
    • Xing Y. Liu D. Zhang R. Joachimiak A. Songyang Z. Xu W. 2004. Structural basis of membrane targeting by the Phox homology domain of cytokine-independent survival kinase (CISK-PX). J. Biol. Chem. 279 (29): 30662-30669. 10.1074/jbc.M404107200. 15126499.
    • (2004) J. Biol. Chem. , vol.279 , Issue.29 , pp. 30662-30669
    • Xing, Y.1    Liu, D.2    Zhang, R.3    Joachimiak, A.4    Songyang, Z.5    Xu, W.6
  • 63
    • 0032540860 scopus 로고    scopus 로고
    • Solution structure and membrane interactions of the C2 domain of cytosolic phospholipase A2
    • 9665851
    • Xu G.Y. McDonagh T. Yu H.A. Nalefski E.A. Clark J.D. Cumming D.A. 1998. Solution structure and membrane interactions of the C2 domain of cytosolic phospholipase A2. J. Mol. Biol. 280 (3): 485-500. 10.1006/jmbi.1998.1874. 9665851.
    • (1998) J. Mol. Biol. , vol.280 , Issue.3 , pp. 485-500
    • Xu, G.Y.1    McDonagh, T.2    Yu, H.A.3    Nalefski, E.A.4    Clark, J.D.5    Cumming, D.A.6
  • 64
    • 0030764306 scopus 로고    scopus 로고
    • NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein-lipid micelle interactions
    • 9271501
    • Xu R.X. Pawelczyk T. Xia T.H. Brown S.C. 1997. NMR structure of a protein kinase C-gamma phorbol-binding domain and study of protein-lipid micelle interactions. Biochemistry, 36 (35): 10709-10717. 10.1021/bi970833a. 9271501.
    • (1997) Biochemistry , vol.36 , Issue.35 , pp. 10709-10717
    • Xu, R.X.1    Pawelczyk, T.2    Xia, T.H.3    Brown, S.C.4
  • 65
    • 0028541866 scopus 로고
    • Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques
    • 7812156
    • Zhang O. Kay L.E. Olivier J.P. Forman-Kay J.D. 1994. Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques. J. Biomol. NMR, 4 (6): 845-858. 10.1007/BF00398413. 7812156.
    • (1994) J. Biomol. NMR , vol.4 , Issue.6 , pp. 845-858
    • Zhang, O.1    Kay, L.E.2    Olivier, J.P.3    Forman-Kay, J.D.4
  • 66
    • 10744227963 scopus 로고    scopus 로고
    • Crystal structure of the yeast Phox homology (PX) domain protein Grd19p complexed to phosphatidylinositol-3-phosphate
    • 14514667
    • Zhou C.Z. Li de La Sierra-Gallay I. Quevillon-Cheruel S. Collinet B. Minard P. Blondeau K. et al 2003. Crystal structure of the yeast Phox homology (PX) domain protein Grd19p complexed to phosphatidylinositol-3-phosphate. J. Biol. Chem. 278 (50): 50371-50376. 10.1074/jbc.M304392200. 14514667.
    • (2003) J. Biol. Chem. , vol.278 , Issue.50 , pp. 50371-50376
    • Zhou, C.Z.1    Li De La Sierra-Gallay, I.2    Quevillon-Cheruel, S.3    Collinet, B.4    Minard, P.5    Blondeau, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.