메뉴 건너뛰기




Volumn 20, Issue 5, 2011, Pages 867-879

Apparent structural differences at the tetramerization region of erythroid and nonerythroid beta spectrin as discriminated by phage displayed scFvs

Author keywords

Affinity difference; Beta spectrin; Erythroid and nonerythroid; Scfv; Structural difference

Indexed keywords

FODRIN; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY; SPECTRIN; SPECTRIN BETA SUBUNIT; UNCLASSIFIED DRUG;

EID: 79954544076     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.617     Document Type: Article
Times cited : (3)

References (66)
  • 1
    • 38049048081 scopus 로고    scopus 로고
    • Organizing the fluid membrane bilayer: Diseases linked to spectrin and ankyrin
    • Bennett V, Healy J (2008) Organizing the fluid membrane bilayer: diseases linked to spectrin and ankyrin. Trends Mol Med 14:28-36.
    • (2008) Trends Mol Med , vol.14 , pp. 28-36
    • Bennett, V.1    Healy, J.2
  • 2
    • 0034958883 scopus 로고    scopus 로고
    • Spectrin and ankyrin-based pathways: Metazoan inventions for integrating cells into tissues
    • Bennett V, Baines AJ (2001) Spectrin and ankyrinbased pathways: metazoan inventions for integrating cells into tissues. Physiol Rev 81:1353-1392. (Pubitemid 32606672)
    • (2001) Physiological Reviews , vol.81 , Issue.3 , pp. 1353-1392
    • Bennett, V.1    Baines, A.J.2
  • 3
    • 17444415361 scopus 로고    scopus 로고
    • Spectrin, alpha-actinin, and dystrophin
    • Broderick M, Winder S (2005) Spectrin, alpha-actinin, and dystrophin. Adv Protein Chem 70:203-246.
    • (2005) Adv Protein Chem , vol.70 , pp. 203-246
    • Broderick, M.1    Winder, S.2
  • 4
    • 0028110108 scopus 로고
    • Brain α erythroid spectrin: Identification, compartmentalization, and β spectrin associations
    • DOI 10.1016/0006-8993(94)91267-X
    • Clark MB, Ma Y, Bloom ML, Barker JE, Zagon IS, Zimmer WE, Goodman SR (1994) Brain α erythroid spectrin: identification, compartmentalization, and β spectrin associations. Brain Res 663:223-236. (Pubitemid 24339036)
    • (1994) Brain Research , vol.663 , Issue.2 , pp. 223-236
    • Clark, M.B.1    Ma, Y.2    Bloom, M.L.3    Barker, J.E.4    Zagon, I.S.5    Zimmer, W.E.6    Goodman, S.R.7
  • 5
    • 0027525225 scopus 로고
    • The 270 kDa splice variant of erythrocyte β-spectrin (βIΣ2) segregates in vivo and in vitro to specific domains of cerebellar neurons
    • Malchiodi-Albedi F, Ceccarini M, Winkelmann JC, Morrow JS, Petrucci TC (1993) The 270 kDa splice variant of erythrocyte β-spectrin (β1∑2) segregates in vivo and in vitro to specific domains of cerebellar neurons. J Cell Sci 106:67-78. (Pubitemid 23286779)
    • (1993) Journal of Cell Science , vol.106 , Issue.1 , pp. 67-78
    • Malchiodi-Albedi, F.1    Ceccarini, M.2    Winkelmann, J.C.3    Morrow, J.S.4    Petrucci, T.C.5
  • 6
    • 0024343759 scopus 로고
    • Presence of erythroid and nonerythroid spectrin transcripts in human lens and cerebellum
    • Yoon SH, Skalka H, Prchal JT (1989) Presence of erythroid and nonerythroid spectrin transcripts in human lens and cerebellum. Invest Ophthalmol Visual Sci 30: 1860-1866. (Pubitemid 19215011)
    • (1989) Investigative Ophthalmology and Visual Science , vol.30 , Issue.8 , pp. 1860-1866
    • Yoon, S.-H.1    Skalka, H.2    Prchal, J.T.3
  • 7
    • 0027301038 scopus 로고
    • Erythroid and nonerythroid spectrins
    • Winkelmann JC, Forget BG (1993) Erythroid and nonerythroid spectrins. Blood 81:3173-3185. (Pubitemid 23172896)
    • (1993) Blood , vol.81 , Issue.12 , pp. 3173-3185
    • Winkelmann, J.C.1    Forget, B.G.2
  • 8
    • 41549109490 scopus 로고    scopus 로고
    • Spectrin and ankyrin-based cytoskeletons at polarized domains in myelinated axons
    • DOI 10.3181/0709-MR-243
    • Susuki K, Rasband MN (2008) Spectrin and ankyrinbased cytoskeletons at polarized domains in myelinated axons. Exp Biol Med 233:394-400. (Pubitemid 351469294)
    • (2008) Experimental Biology and Medicine , vol.233 , Issue.4 , pp. 394-400
    • Susuki, K.1    Rasband, M.N.2
  • 9
    • 0022454882 scopus 로고
    • Brain spectrin (240/235) and brain spectrin (240/235E): Two distinct spectrin subtypes with different locations within mammalian neural cells
    • Riederer BM, Zagon IS, Goodman SR (1986) Brain spectrin (240/235) and brain spectrin (240/235E): two distinct spectrin subtypes with different locations within mammalian neural cells. J Cell Biol 102: 2088-2096.
    • (1986) J Cell Biol , vol.102 , pp. 2088-2096
    • Riederer, B.M.1    Zagon, I.S.2    Goodman, S.R.3
  • 10
    • 0034177578 scopus 로고    scopus 로고
    • The spectrin-based skeleton at the postsynaptic membrane of the neuromuscular junction
    • DOI 10.1002/(SICI)1097-0029(20000401)49:1<101::AID-JEMT11>3.0.CO;2- U
    • Kordeli E (2000) The spectrin-based skeleton at the postsynaptic membrane of the neuromuscular junction. Microsc Res Tech 49:101-107. (Pubitemid 30191914)
    • (2000) Microscopy Research and Technique , vol.49 , Issue.1 , pp. 101-107
    • Kordeli, E.1
  • 11
    • 33846274937 scopus 로고    scopus 로고
    • The molecular basis of hereditary red cell membrane disorders
    • DOI 10.1016/j.blre.2006.03.005, PII S0268960X06000257
    • Delaunay J (2007) The molecular basis of hereditary red cell membrane disorders. Blood Rev 21:1-20. (Pubitemid 46110925)
    • (2007) Blood Reviews , vol.21 , Issue.1 , pp. 1-20
    • Delaunay, J.1
  • 12
    • 0026470325 scopus 로고
    • Analysis of human red cell spectrin tetramer (head-to-head) assembly using complementary univalent peptides
    • DeSilva TM, Peng KC, Speicher KD, Speicher DW (1992) Analysis of human red cell spectrin tetramer (head-to-head) assembly using complementary univalent peptides. Biochemistry 31:10872-10878.
    • (1992) Biochemistry , vol.31 , pp. 10872-10878
    • DeSilva, T.M.1    Peng, K.C.2    Speicher, K.D.3    Speicher, D.W.4
  • 13
    • 0027419729 scopus 로고
    • Location of the human red cell spectrin tetramer binding site and detection of a related 'closed' hairpin loop dimer using proteolytic footprinting
    • Speicher DW, DeSilva TM, Speicher KD, Ursitt JA, Hembach P, Weglarz L (1993) Location of the human red cell spectrin tetramer binding site and detection of a related "closed" hairpin loop dimer using proteolytic footprinting. J Biol Chem 268:4227-4235. (Pubitemid 23072962)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.6 , pp. 4227-4235
    • Speicher, D.W.1    DeSilva, T.M.2    Speicher, K.D.3    Ursitti, J.A.4    Hembach, P.5    Weglarz, L.6
  • 14
    • 0141679134 scopus 로고    scopus 로고
    • Spectrin αII and βII isoforms interact with high affinity at the tetramerization site
    • DOI 10.1042/BJ20030507
    • Bignone PA, Baines AJ (2003) Spectrin αII and βII isoforms interact with high affinity at the tetramerization site. Biochem J 374:613-624. (Pubitemid 37163906)
    • (2003) Biochemical Journal , vol.374 , Issue.3 , pp. 613-624
    • Bignone, P.A.1    Baines, A.J.2
  • 15
    • 35648953361 scopus 로고    scopus 로고
    • Conformational change of erythroid α-spectrin at the tetramerization site upon binding β-spectrin
    • DOI 10.1110/ps.073115307
    • Long F, McElheny D, Jiang S, Park S, Caffrey MS, Fung LW-M (2007) Conformational change of erythroid α-spectrin at the tetramerization site upon binding β-spectrin. Protein Sci 16:2519-2530. (Pubitemid 350036757)
    • (2007) Protein Science , vol.16 , Issue.11 , pp. 2519-2530
    • Long, F.1    Mcelheny, D.2    Jiang, S.3    Park, S.4    Caffrey, M.S.5    Fung, L.W.-M.6
  • 16
    • 0346220014 scopus 로고    scopus 로고
    • Structural Analysis of the αN-Terminal Region of Erythroid and Nonerythroid Spectrins by Small-Angle X-ray Scattering
    • DOI 10.1021/bi0353833
    • Mehboob S, Jacob J, May M, Kotula L, Thiyagarajan P, Johnson ME, Fung LW-M (2003) Structural analysis of the alpha N-terminal region of erythroid and nonerythroid spectrins by small-angle X-ray scattering. Biochemistry 42:14702-14710. (Pubitemid 37532018)
    • (2003) Biochemistry , vol.42 , Issue.49 , pp. 14702-14710
    • Mehboob, S.1    Jacob, J.2    May, M.3    Kotula, L.4    Thiyagarajan, P.5    Johnson, M.E.6    Fung, L.W.-M.7
  • 17
    • 77951994713 scopus 로고    scopus 로고
    • Crystal structure of the non-erythroid α-spectrin tetramerization site reveals differences between erythroid and non-erythroid spectrin tetramer formation
    • Mehboob S, Song Y, Witek M, Long F, Santarsiero BD, Johnson ME, Fung LW-M (2010) Crystal structure of the non-erythroid α-spectrin tetramerization site reveals differences between erythroid and non-erythroid spectrin tetramer formation. J Biol Chem 285:14572-14584.
    • (2010) J Biol Chem , vol.285 , pp. 14572-14584
    • Mehboob, S.1    Song, Y.2    Witek, M.3    Long, F.4    Santarsiero, B.D.5    Johnson, M.E.6    Fung, L.W.-M.7
  • 18
    • 58549116132 scopus 로고    scopus 로고
    • Structural and dynamic study of the tetramerization region of non-erythroid alphaspectrin: A frayed helix revealed by site-directed spin labeling electron paramagnetic resonance
    • Li Q, Fung LW-M (2009) Structural and dynamic study of the tetramerization region of non-erythroid alphaspectrin: a frayed helix revealed by site-directed spin labeling electron paramagnetic resonance. Biochemistry 48:206-215.
    • (2009) Biochemistry , vol.48 , pp. 206-215
    • Li, Q.1    Fung, L.W.-M.2
  • 20
    • 0021818675 scopus 로고
    • Filamentous fusion phage: Novel expression vectors that display cloned antigens on the virion surface
    • Smith GP (1985) Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science 228:1315-1317. (Pubitemid 15000355)
    • (1985) Science , vol.228 , Issue.4705 , pp. 1315-1317
    • Smith, G.P.1
  • 21
    • 28444488346 scopus 로고    scopus 로고
    • Filamentous phage display in the new millennium
    • DOI 10.1021/cr000261r
    • Kehoe JW, Kay BK (2005) Filamentous phage display in the new millennium. Chem Rev 105:4056-4072. (Pubitemid 41724069)
    • (2005) Chemical Reviews , vol.105 , Issue.11 , pp. 4056-4072
    • Kehoe, J.W.1    Kay, B.K.2
  • 22
    • 0025226085 scopus 로고
    • Phage antibodies: Filamentous phage displaying antibody variable domains
    • McCafferty J, Griffiths AD, Winter G, Chiswell DJ (1990) Phage antibodies: filamentous phage displaying antibody variable domains. Nature 348:552-554. (Pubitemid 120015109)
    • (1990) Nature , vol.348 , Issue.6301 , pp. 552-554
    • McCafferty, J.1    Griffiths, A.D.2    Winter, G.3    Chiswell, D.J.4
  • 23
    • 3142743794 scopus 로고    scopus 로고
    • Antibodies from phage antibody libraries
    • DOI 10.1016/j.jim.2004.04.007, PII S0022175904001292
    • Bradbury AR, Marks JD (2004) Antibodies from phage antibody libraries. J Immunol Methods 290:29-49. (Pubitemid 38917129)
    • (2004) Journal of Immunological Methods , vol.290 , Issue.1-2 , pp. 29-49
    • Bradbury, A.R.M.1    Marks, J.D.2
  • 24
    • 27144431943 scopus 로고    scopus 로고
    • Selecting and screening recombinant antibody libraries
    • DOI 10.1038/nbt1126, PII N1126
    • Hoogenboom HR (2005) Selecting and screening recombinant antibody libraries. Nat Biotechnol 23: 1105-1116. (Pubitemid 41486392)
    • (2005) Nature Biotechnology , vol.23 , Issue.9 , pp. 1105-1116
    • Hoogenboom, H.R.1
  • 26
    • 0034846967 scopus 로고    scopus 로고
    • Screening phage-displayed combinatorial peptide libraries
    • DOI 10.1006/meth.2001.1185
    • Kay BK, Kasanov J, Yamabhai M (2001) Screening phage-displayed combinatorial peptide libraries. Methods 24:240-246. (Pubitemid 32846430)
    • (2001) Methods , vol.24 , Issue.3 , pp. 240-246
    • Kay, B.K.1    Kasanov, J.2    Yamabhai, M.3
  • 27
    • 84886012022 scopus 로고    scopus 로고
    • Biotinylation of protein targets for affinity selection experiments with phage
    • Kay BK, Thai S, Volgina V (2009) Biotinylation of protein targets for affinity selection experiments with phage. Methods Mol Biol 498:185-196.
    • (2009) Methods Mol Biol , vol.498 , pp. 185-196
    • Kay, B.K.1    Thai, S.2    Volgina, V.3
  • 28
    • 0035171080 scopus 로고    scopus 로고
    • Kabat Database and its applications: Future directions
    • Johnson G, Wu TT (2001) Kabat database and its applications: future directions. Nucleic Acids Res 29: 205-206. (Pubitemid 32054448)
    • (2001) Nucleic Acids Research , vol.29 , Issue.1 , pp. 205-206
    • Johnson, G.1    Wu, T.T.2
  • 29
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network
    • Andrade MA, Chacon P, Merelo JJ, Moran F (1993) Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network. Protein Eng 6:383-390. (Pubitemid 23197398)
    • (1993) Protein Engineering , vol.6 , Issue.4 , pp. 383-390
    • Andrade, M.A.1    Chacon, P.2    Merelo, J.J.3    Moran, F.4
  • 30
    • 53249140513 scopus 로고    scopus 로고
    • Conformational changes at the tetramerization site of erythroid α-spectrin upon binding β-spectrin: A spin label EPR study
    • Antoniou C, Lam VQ, Fung LW-M (2008) Conformational changes at the tetramerization site of erythroid α-spectrin upon binding β-spectrin: a spin label EPR study. Biochemistry 47:10765-10772.
    • (2008) Biochemistry , pp. 10765-10772
    • Antoniou, C.1    Lam, V.Q.2    Fung, L.W.-M.3
  • 31
    • 70349920964 scopus 로고    scopus 로고
    • Association studies of erythoid alpha-spectrin at the tetramerization site
    • Lam VQ, Antoniou C, Rolius R, Fung LW-M (2009) Association studies of erythoid alpha-spectrin at the tetramerization site. Br J Haematol 147:392-395.
    • (2009) Br J Haematol , vol.147 , pp. 392-395
    • Lam, V.Q.1    Antoniou, C.2    Rolius, R.3    Fung, L.W.-M.4
  • 32
    • 77954699179 scopus 로고    scopus 로고
    • Crystal structure and functional interpretation of the erythrocyte spectrin tetramerization domain complex
    • Ipsaro JJ, Harper SL, Messick TE, Marmorstein R, Mondragón A, Speicher DW (2010) Crystal structure and functional interpretation of the erythrocyte spectrin tetramerization domain complex. Blood 115: 4843-4852.
    • (2010) Blood , vol.115 , pp. 4843-4852
    • Ipsaro, J.J.1    Harper, S.L.2    Messick, T.E.3    Marmorstein, R.4    Mondragón, A.5    Speicher, D.W.6
  • 34
    • 28544443188 scopus 로고    scopus 로고
    • Conformational studies of the tetramerization site of human erythroid spectrin by cysteine-scanning spin-labeling EPR methods
    • DOI 10.1021/bi051009m
    • Mehboob S, Luo BH, Fu W, Johnson ME, Fung LW-M (2005) Conformational studies of the tetramerization site of human erythroid spectrin by cysteine-scanning spin-labeling EPR methods. Biochemistry 44: 15898-15905. (Pubitemid 41746920)
    • (2005) Biochemistry , vol.44 , Issue.48 , pp. 15898-15905
    • Mehboob, S.1    Luo, B.-H.2    Fu, W.3    Johnson, M.E.4    Fung, L.W.-M.5
  • 35
    • 0033588274 scopus 로고    scopus 로고
    • Structures of two repeats of spectrin suggest models of flexibility
    • DOI 10.1016/S0092-8674(00)81980-7
    • Grum VL, Li D, MacDonald RI, Mondragon A (1999) Structures of two repeats of spectrin suggest models of flexibility. Cell 98:523-535. (Pubitemid 29402489)
    • (1999) Cell , vol.98 , Issue.4 , pp. 523-535
    • Grum, V.L.1    Li, D.2    MacDonald, R.I.3    Mondragon, A.4
  • 36
    • 69249157215 scopus 로고    scopus 로고
    • The L49F mutation in alpha erythroid spectrin induces local disorder in the tetramer association region: Fluorescence and molecular dynamics studies of free and bound alpha spectrin
    • Song Y, Pipalia NH, Fung LW-M (2009) The L49F mutation in alpha erythroid spectrin induces local disorder in the tetramer association region: fluorescence and molecular dynamics studies of free and bound alpha spectrin. Protein Sci 18:1916-1925.
    • (2009) Protein Sci , vol.18 , pp. 1916-1925
    • Song, Y.1    Pipalia, N.H.2    Fung, L.W.-M.3
  • 37
    • 4744369286 scopus 로고    scopus 로고
    • Substantial energetic improvement with minimal structural perturbation in a high affinity mutant antibody
    • DOI 10.1016/j.jmb.2004.08.019, PII S0022283604009878
    • Midelfort KS, Hernandez HH, Lippow SM, Tidor B, Drennan CL, Wittrop KD (2004) Substantial energetic improvement with minimal structural perturbation in a high affinity mutant antibody. J Mol Biol 343:685-701. (Pubitemid 39311615)
    • (2004) Journal of Molecular Biology , vol.343 , Issue.3 , pp. 685-701
    • Midelfort, K.S.1    Hernandez, H.H.2    Lippow, S.M.3    Tidor, B.4    Drennan, C.L.5    Wittrup, K.D.6
  • 39
    • 0030920225 scopus 로고    scopus 로고
    • Comparison of the salt-dependent self-association of brain and erythroid spectrin
    • DOI 10.1021/bi970186n
    • Begg GE, Morris MB, Ralston GB (1997) Comparison of the salt-dependent self-association of brain and erythroid spectrin. Biochemistry 36:6977-6985. (Pubitemid 27258110)
    • (1997) Biochemistry , vol.36 , Issue.23 , pp. 6977-6985
    • Begg, G.E.1    Morris, M.B.2    Ralston, G.B.3
  • 40
    • 0035900013 scopus 로고    scopus 로고
    • αβ spectrin coiled coil association at the tetramerization site
    • DOI 10.1021/bi010984k
    • Mehboob S, Luo BH, Patel BM, Fung LW-M (2001) alpha beta Spectrin coiled coil association at the tetramerization site. Biochemistry 16:12457-12464. (Pubitemid 32962586)
    • (2001) Biochemistry , vol.40 , Issue.41 , pp. 12457-12464
    • Mehboob, S.1    Luo, B.-H.2    Patel, B.M.3    Fung, L.W.-M.4
  • 41
    • 0032524188 scopus 로고    scopus 로고
    • Spectrin self-association site: Characterization and study of β-spectrin mutations associated with hereditary elliptocytosis
    • Nicolas G, Pedroni S, Fournier C, Gautero H, Craescu C, Dhermy D, Lecomte MC (1998) Spectrin self-association site: characterization and study of beta-spectrin mutations associated with hereditary elliptocytosis. Biochemistry J 332:81-89. (Pubitemid 28239321)
    • (1998) Biochemical Journal , vol.332 , Issue.1 , pp. 81-89
    • Nicolas, G.1    Pedroni, S.2    Fournier, C.3    Gautero, H.4    Craescu, C.5    Dhermy, D.6    Lecomte, M.C.7
  • 42
    • 0038159470 scopus 로고    scopus 로고
    • Solution structural studies on human erythrocyte α-spectrin tetramerization site
    • DOI 10.1074/jbc.M300617200
    • Park S, Caffrey MS, Johnson ME, Fung LW-M (2003) Solution structural studies on human erythrocyte αa-spectrin tetramerization site. J Biol Chem 278: 21837-21844. (Pubitemid 36792589)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.24 , pp. 21837-21844
    • Park, S.1    Caffrey, M.S.2    Johnson, M.E.3    Fung, L.W.-M.4
  • 43
    • 0031592935 scopus 로고    scopus 로고
    • Solution structure of the spectrin repeat: A left-handed antiparallel triple-helical coiled-coil
    • DOI 10.1006/jmbi.1997.1344
    • Pascual J, Pfuhl M, Walther D, Saraste M, Nilges M (1997) Solution structure of the spectrin repeat: a lefthanded antiparallel triple-helical coiled-coil. J Mol Biol 273:740-751. (Pubitemid 27488814)
    • (1997) Journal of Molecular Biology , vol.273 , Issue.3 , pp. 740-751
    • Pascual, J.1    Pfuhl, M.2    Walther, D.3    Saraste, M.4    Nilges, M.5
  • 44
    • 0027749280 scopus 로고
    • Crystal structure of the repetitive segments of spectrin
    • Yan Y, Winograd E, Viel A, Cronin T, Harrison SC, Branton D (1993) Crystal structure of the repetitive segments of spectrin. Science 262:2027-2030. (Pubitemid 24041880)
    • (1993) Science , vol.262 , Issue.5142 , pp. 2027-2030
    • Yan, Y.1    Winograd, E.2    Viel, A.3    Cronin, T.4    Harrison, S.C.5    Branton, D.6
  • 48
    • 23844547333 scopus 로고    scopus 로고
    • Detection of dynamic water molecules in a microcrystalline sample of the SH3 domain of α-spectrin by MAS solid-state NMR
    • DOI 10.1007/s10858-005-1718-z
    • Chevelkov V, Faelber K, Diehl A, Heinemann U, Oschkinat H, Reif B (2005) Detection of dynamic water molecules in a microcrystalline sample of the SH3 domain of alpha-spectrin by MAS solid-state NMR. J Biomol NMR 31:295-310. (Pubitemid 41348906)
    • (2005) Journal of Biomolecular NMR , vol.31 , Issue.4 , pp. 295-310
    • Chevelkov, V.1    Faelber, K.2    Diehl, A.3    Heinemann, U.4    Oschkinat, H.5    Reif, B.6
  • 49
    • 33847710333 scopus 로고    scopus 로고
    • Phosphorylation of a threonine unique to the short C-terminal isoform of βII-spectrin links regulation of α-βspectrin interaction to neuritogenesis
    • DOI 10.1074/jbc.M605920200
    • Bignone PA, King MD, Pinder JC, Baines AJ (2007) Phosphorylation of a threonine unique to the short Cterminal isoform of betaII-spectrin links regulation of alpha-beta spectrin interaction to neuritogenesis. J Biol Chem 282:888-896. (Pubitemid 47076581)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.2 , pp. 888-896
    • Bignone, P.A.1    King, M.D.A.2    Pinder, J.C.3    Baines, A.J.4
  • 50
    • 34547959977 scopus 로고    scopus 로고
    • The ring-infected erythrocyte surface antigen (RESA) of Plasmodium falciparum stabilizes spectrin tetramers and suppresses further invasion
    • DOI 10.1182/blood-2007-02-076919
    • Pei X, Guo X, Coppel R, Bhattacharjee S, Haldar K, Gratzer W, Mohandas N, An X (2007) The ring-infected erythrocyte surface antigen of Plasmodium falciparum stabilizes spectrin tetramers and suppresses further invasion. Blood 110:1036-1042. (Pubitemid 47267445)
    • (2007) Blood , vol.110 , Issue.3 , pp. 1036-1042
    • Pei, X.1    Guo, X.2    Coppel, R.3    Bhattacharjee, S.4    Haldar, K.5    Gratzer, W.6    Mohandas, N.7    An, X.8
  • 51
    • 0033880909 scopus 로고    scopus 로고
    • Spectrin tethers and mesh in the biosynthetic pathway
    • de Matteis MA, Morrow JS (2000) Spectrin tethers and mesh in the biosynthetic pathway. J Cell Sci 113: 2331-2343. (Pubitemid 30599339)
    • (2000) Journal of Cell Science , vol.113 , Issue.13 , pp. 2331-2343
    • De Matteis, M.A.1    Morrow, J.S.2
  • 52
    • 0000589008 scopus 로고    scopus 로고
    • Of membrane stability and mosaics: The spectrin cytoskeleton
    • Handbook of physiology. London: Oxford University Press
    • Morrow JS, Rimm DL, Kennedy SP, Cianci CD, Sinard JH, Weed SA, Of membrane stability and mosaics: the spectrin cytoskeleton, In: Hoffman J, Jamieson J, Eds. (1997) Handbook of physiology. London: Oxford University Press, pp 485-540.
    • (1997) Hoffman J Jamieson J Eds , pp. 485-540
    • Morrow, J.S.1    Rimm, D.L.2    Kennedy, S.P.3    Cianci, C.D.4    Sinard, J.H.5    Weed, S.A.6
  • 53
    • 56349088479 scopus 로고    scopus 로고
    • Alpha II-beta V spectrin bridges the plasma membrane and cortical lattice in the lateral wall of the auditory outer hair cells
    • Legendre K, Safieddine S, Küssel-Andermann P, Petit C, El-Amraoui A (2008) alphaII-betaV spectrin bridges the plasma membrane and cortical lattice in the lateral wall of the auditory outer hair cells. J Cell Sci 121: 3347-3356.
    • (2008) J Cell Sci , vol.121 , pp. 3347-3356
    • Legendre, K.1    Safieddine, S.2    Küssel-Andermann, P.3    Petit, C.4    El-Amraoui, A.5
  • 54
    • 0020591175 scopus 로고
    • Synthesis and assembly of spectrin during avian erythropoiesis: Stoichiometric assembly but unequal synthesis of α and β spectrin
    • Blikstad I, Nelson WJ, Moon RT, Lazarides E (1983) Synthesis and assembly of spectrin during avian erythropoiesis: stoichiometric assembly but unequal synthesis of α and β spectrin. Cell 32: 1081-1091. (Pubitemid 13033047)
    • (1983) Cell , vol.32 , Issue.4 , pp. 1081-1091
    • Blikstad, I.1    Nelson, W.J.2    Moon, R.T.3    Lazarides, E.4
  • 55
    • 0020551681 scopus 로고
    • β-Spectrin limits α-spectrin assembly on membranes following synthesis in a chicken erythroid cell lysate
    • Moon RT, Lazarides E (1983) β-spectrin limits α-spectrin assembly on membranes following synthesis in a chicken erythroid cell lysate. Nature 305:62-65. (Pubitemid 13041979)
    • (1983) Nature , vol.305 , Issue.5929 , pp. 62-65
    • Moon, R.T.1    Lazarides, E.2
  • 57
    • 0037335808 scopus 로고    scopus 로고
    • Differentiation of Candida albicans and Candida dubliniensis by using recombinant human antibody single-chain variable fragments specific for hyphae
    • DOI 10.1128/JCM.41.3.1152-1160.2003
    • Bliss JM, Sullivan MA, Malone J, Haidaris CG (2003) Differentiation of Candida albicans and Candida dubliniensis by using recombinant human antibody singlechain variable fragments specific for hyphae. J Clin Microbiol 41:1152-1160. (Pubitemid 36307122)
    • (2003) Journal of Clinical Microbiology , vol.41 , Issue.3 , pp. 1152-1160
    • Bliss, J.M.1    Sullivan, M.A.2    Malone, J.3    Haidaris, C.G.4
  • 58
    • 24144500637 scopus 로고    scopus 로고
    • Efficient construction of a large collection of phage-displayed combinatorial peptide libraries
    • DOI 10.2174/1386207054867337
    • Scholle MD, Kehoe JW, Kay BK (2005) Efficient construction of a large collection of phage-displayed combinatorial peptide libraries. Comb Chem High Throughput Screen 8:545-551. (Pubitemid 41242959)
    • (2005) Combinatorial Chemistry and High Throughput Screening , vol.8 , Issue.6 , pp. 545-551
    • Scholle, M.D.1    Kehoe, J.W.2    Kay, B.K.3
  • 60
    • 28044462393 scopus 로고    scopus 로고
    • Enzyme immunoassay (EIA)/enzyme-linked immunosorbent assay (ELISA)
    • DOI 10.1373/clinchem.2005.051532
    • Lequin RM (2005) Enzyme immunoassay (EIS)/enzyme-linked immunosorbent assay (ELISA). Clin Chem 51:2415-2418. (Pubitemid 41692603)
    • (2005) Clinical Chemistry , vol.51 , Issue.12 , pp. 2415-2418
    • Lequin, R.M.1
  • 61
    • 3042633729 scopus 로고    scopus 로고
    • Molecular recognition properties of FN3 monobodies that bind the Src SH3 domain
    • DOI 10.1016/j.chembiol.2004.04.009, PII S1074552104001334
    • Karatan E, Merguerian M, Han Z, Scholle MD, Koide S, Kay BK (2004) Molecular recognition properties of FN3 monobodies that bind the Src SH3 domain. Chem Biol 11:835-844. (Pubitemid 38836899)
    • (2004) Chemistry and Biology , vol.11 , Issue.6 , pp. 835-844
    • Karatan, E.1    Merguerian, M.2    Han, Z.3    Scholle, M.D.4    Koide, S.5    Kay, B.K.6
  • 65
    • 0035747672 scopus 로고    scopus 로고
    • Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM
    • DOI 10.1002/prot.1168
    • Bates PA, Kelley LA, MacCallum RM, Sternberg MJ (2001) Enhancement of protein modeling by human intervention in applying the automatic programs 3D-JIGSAW and 3D-PSSM. Proteins 5 (Suppl):39-46. (Pubitemid 34113166)
    • (2001) Proteins: Structure, Function and Genetics , vol.45 , Issue.SUPPL. 5 , pp. 39-46
    • Bates, P.A.1    Kelley, L.A.2    MacCallum, R.M.3    Sternberg, M.J.E.4
  • 66
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for highly efficient, load-balanced, and scalable molecular simulation
    • Hess B, Kutzner C, van der Spoel D, Lindahl E (2008) GROMACS 4: algorithms for highly efficient, load-balanced, and scalable molecular simulation. J Chem Theory Comput 4:435-447.
    • (2008) J Chem Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.