메뉴 건너뛰기




Volumn 408, Issue 2, 2011, Pages 304-320

Design of peptide inhibitors that bind the bZIP domain of Epstein-Barr virus protein BZLF1

Author keywords

bZIP transcription factors; BZLF1; interaction specificity; protein design; protein protein interaction inhibitor

Indexed keywords

BASIC REGION LEUCINE ZIPPER; HETERODIMER; LEUCINE; PROTEIN INHIBITOR; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR BZLF1; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 79953709095     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.02.046     Document Type: Article
Times cited : (14)

References (54)
  • 1
    • 0026331267 scopus 로고
    • X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil
    • O'Shea E.K., Klemm J.D., Kim P.S., and Alber T. X-ray structure of the GCN4 leucine zipper, a two-stranded, parallel coiled coil Science 254 1991 539 544 (Pubitemid 21917367)
    • (1991) Science , vol.254 , Issue.5031 , pp. 539-544
    • O'Shea, E.K.1    Klemm, J.D.2    Kim, P.S.3    Alber, T.4
  • 2
    • 32444448106 scopus 로고    scopus 로고
    • Structural basis of lytic cycle activation by the Epstein-Barr virus ZEBRA protein
    • DOI 10.1016/j.molcel.2006.01.006, PII S1097276506000074
    • Petosa C., Morand P., Baudin F., Moulin M., Artero J.B., and Muller C.W. Structural basis of lytic cycle activation by the Epstein-Barr virus ZEBRA protein Mol. Cell 21 2006 565 572 (Pubitemid 43228011)
    • (2006) Molecular Cell , vol.21 , Issue.4 , pp. 565-572
    • Petosa, C.1    Morand, P.2    Baudin, F.3    Moulin, M.4    Artero, J.-B.5    Muller, C.W.6
  • 3
    • 0028894384 scopus 로고
    • Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA
    • Glover J.N., and Harrison S.C. Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA Nature 373 1995 257 261
    • (1995) Nature , vol.373 , pp. 257-261
    • Glover, J.N.1    Harrison, S.C.2
  • 7
    • 34247500390 scopus 로고    scopus 로고
    • Positive aspects of negative design: Simultaneous selection of specificity and interaction stability
    • DOI 10.1021/bi602506p
    • Mason J.M., Muller K.M., and Arndt K.M. Positive aspects of negative design: simultaneous selection of specificity and interaction stability Biochemistry 46 2007 4804 4814 (Pubitemid 46651203)
    • (2007) Biochemistry , vol.46 , Issue.16 , pp. 4804-4814
    • Mason, J.M.1    Muller, K.M.2    Arndt, K.M.3
  • 8
    • 70350489266 scopus 로고    scopus 로고
    • Role of hydrophobic and electrostatic interactions in coiled coil stability and specificity
    • Mason J.M., Hagemann U.B., and Arndt K.M. Role of hydrophobic and electrostatic interactions in coiled coil stability and specificity Biochemistry 48 2009 10380 10388
    • (2009) Biochemistry , vol.48 , pp. 10380-10388
    • Mason, J.M.1    Hagemann, U.B.2    Arndt, K.M.3
  • 9
    • 33747786692 scopus 로고    scopus 로고
    • Experimental identification of homodimerizing B-ZIP families in Homo sapiens
    • DOI 10.1016/j.jsb.2006.02.018, PII S1047847706001067, Fibrous Protein Structure
    • Acharya A., Rishi V., Moll J., and Vinson C. Experimental identification of homodimerizing B-ZIP families in Homo sapiens J. Struct. Biol. 155 2006 130 139 (Pubitemid 44278647)
    • (2006) Journal of Structural Biology , vol.155 , Issue.2 , pp. 130-139
    • Acharya, A.1    Rishi, V.2    Moll, J.3    Vinson, C.4
  • 10
    • 0028786167 scopus 로고
    • Extending dimerization interfaces: The bZIP basic region can form a coiled coil
    • Krylov D., Olive M., and Vinson C. Extending dimerization interfaces: the bZIP basic region can form a coiled coil EMBO J. 14 1995 5329 5337
    • (1995) EMBO J. , vol.14 , pp. 5329-5337
    • Krylov, D.1    Olive, M.2    Vinson, C.3
  • 11
    • 0030802419 scopus 로고    scopus 로고
    • A dominant negative to activation protein-1 (AP1) that abolishes DNA binding and inhibits oncogenesis
    • DOI 10.1074/jbc.272.30.18586
    • Olive M., Krylov D., Echlin D.R., Gardner K., Taparowsky E., and Vinson C. A dominant negative to activation protein-1 (AP1) that abolishes DNA binding and inhibits oncogenesis J. Biol. Chem. 272 1997 18586 18594 (Pubitemid 27318198)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.30 , pp. 18586-18594
    • Olive, M.1    Krylov, D.2    Echlin, D.R.3    Gardner, K.4    Taparowsky, E.5    Vinson, C.6
  • 12
    • 0031883280 scopus 로고    scopus 로고
    • A dominant-negative inhibitor of CREB reveals that it is a general mediator of stimulus-dependent transcription of c-fos
    • Ahn S., Olive M., Aggarwal S., Krylov D., Ginty D.D., and Vinson C. A dominant-negative inhibitor of CREB reveals that it is a general mediator of stimulus-dependent transcription of c-fos Mol. Cell. Biol. 18 1998 967 977 (Pubitemid 28063431)
    • (1998) Molecular and Cellular Biology , vol.18 , Issue.2 , pp. 967-977
    • Ahn, S.1    Olive, M.2    Aggarwal, S.3    Krylov, D.4    Ginty, D.D.5    Vinson, C.6
  • 14
    • 33847719801 scopus 로고    scopus 로고
    • Inhibition of CCAAT/enhancer binding protein family DNA binding in mouse epidermis prevents and regresses papillomas
    • DOI 10.1158/0008-5472.CAN-06-2746
    • Oh W.J., Rishi V., Orosz A., Gerdes M.J., and Vinson C. Inhibition of CCAAT/enhancer binding protein family DNA binding in mouse epidermis prevents and regresses papillomas Cancer Res. 67 2007 1867 1876 (Pubitemid 46383414)
    • (2007) Cancer Research , vol.67 , Issue.4 , pp. 1867-1876
    • Won, J.O.1    Rishi, V.2    Orosz, A.3    Gerdes, M.J.4    Vinson, C.5
  • 15
    • 29444447288 scopus 로고    scopus 로고
    • Structure-based prediction of bZIP partnering specificity
    • DOI 10.1016/j.jmb.2005.11.036, PII S0022283605014233
    • Grigoryan G., and Keating A.E. Structure-based prediction of bZIP partnering specificity J. Mol. Biol. 355 2006 1125 1142 (Pubitemid 43012152)
    • (2006) Journal of Molecular Biology , vol.355 , Issue.5 , pp. 1125-1142
    • Grigoryan, G.1    Keating, A.E.2
  • 16
    • 4143058720 scopus 로고    scopus 로고
    • Predicting specificity in bZIP coiled-coil protein interactions
    • Fong J.H., Keating A.E., and Singh M. Predicting specificity in bZIP coiled-coil protein interactions Genome Biol. 5 2004 R11
    • (2004) Genome Biol. , vol.5 , pp. 11
    • Fong, J.H.1    Keating, A.E.2    Singh, M.3
  • 17
    • 0028303384 scopus 로고
    • A thermodynamic scale for leucine zipper stability and dimerization specificity: e and g interhelical interactions
    • Krylov D., Mikhailenko I., and Vinson C. A thermodynamic scale for leucine zipper stability and dimerization specificity: e and g interhelical interactions EMBO J. 13 1994 2849 2861 (Pubitemid 24191695)
    • (1994) EMBO Journal , vol.13 , Issue.12 , pp. 2849-2861
    • Krylov, D.1    Mikhailenko, I.2    Vinson, C.3
  • 18
    • 33749025290 scopus 로고    scopus 로고
    • Stability of 100 homo and heterotypic coiled-coil a-a′ pairs for ten amino acids (A, L, I, V, N, K, S, T, E, and R)
    • DOI 10.1021/bi060822u
    • Acharya A., Rishi V., and Vinson C. Stability of 100 homo and heterotypic coiled-coil a-a′ pairs for ten amino acids (A, L, I, V, N, K, S, T, E, and R) Biochemistry 45 2006 11324 11332 (Pubitemid 44453980)
    • (2006) Biochemistry , vol.45 , Issue.38 , pp. 11324-11332
    • Acharya, A.1    Rishi, V.2    Vinson, C.3
  • 19
    • 77953102600 scopus 로고    scopus 로고
    • Side-chain pairing preferences in the parallel coiled-coil dimer motif: Insight on ion pairing between core and flanking sites
    • Steinkruger J.D., Woolfson D.N., and Gellman S.H. Side-chain pairing preferences in the parallel coiled-coil dimer motif: insight on ion pairing between core and flanking sites J. Am. Chem. Soc. 132 2010 7586 7588
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 7586-7588
    • Steinkruger, J.D.1    Woolfson, D.N.2    Gellman, S.H.3
  • 20
    • 65249171530 scopus 로고    scopus 로고
    • Design of protein-interaction specificity gives selective bZIP-binding peptides
    • Grigoryan G., Reinke A.W., and Keating A.E. Design of protein-interaction specificity gives selective bZIP-binding peptides Nature 458 2009 859 864
    • (2009) Nature , vol.458 , pp. 859-864
    • Grigoryan, G.1    Reinke, A.W.2    Keating, A.E.3
  • 21
    • 0037595546 scopus 로고    scopus 로고
    • Comprehensive identification of human bZIP interactions with coiled-coil arrays
    • DOI 10.1126/science.1084648
    • Newman J.R., and Keating A.E. Comprehensive identification of human bZIP interactions with coiled-coil arrays Science 300 2003 2097 2101 (Pubitemid 36760137)
    • (2003) Science , vol.300 , Issue.5628 , pp. 2097-2101
    • Newman, J.R.S.1    Keating, A.E.2
  • 22
    • 33646157076 scopus 로고    scopus 로고
    • Deciphering B-ZIP transcription factor interactions in vitro and in vivo
    • Vinson C., Acharya A., and Taparowsky E.J. Deciphering B-ZIP transcription factor interactions in vitro and in vivo Biochim. Biophys. Acta 1759 2006 4 12
    • (2006) Biochim. Biophys. Acta , vol.1759 , pp. 4-12
    • Vinson, C.1    Acharya, A.2    Taparowsky, E.J.3
  • 23
    • 0023503201 scopus 로고
    • Polymorphic proteins encoded within BZLF1 of defective and standard Epstein-Barr viruses disrupt latency
    • Countryman J., Jenson H., Seibl R., Wolf H., and Miller G. Polymorphic proteins encoded within BZLF1 of defective and standard Epstein-Barr viruses disrupt latency J. Virol. 61 1987 3672 3679 (Pubitemid 18011461)
    • (1987) Journal of Virology , vol.61 , Issue.12 , pp. 3672-3679
    • Countryman, J.1    Jenson, H.2    Seibl, R.3    Wolf, H.4    Miller, G.5
  • 24
    • 0027282974 scopus 로고
    • A transcription factor with homology to the AP-1 family links RNA transcription and DNA replication in the lytic cycle of Epstein-Barr virus
    • Schepers A., Pich D., and Hammerschmidt W. A transcription factor with homology to the AP-1 family links RNA transcription and DNA replication in the lytic cycle of Epstein-Barr virus EMBO J. 12 1993 3921 3929 (Pubitemid 23282768)
    • (1993) EMBO Journal , vol.12 , Issue.10 , pp. 3921-3929
    • Schepers, A.1    Pich, D.2    Hammerschmidt, W.3
  • 25
    • 0034660443 scopus 로고    scopus 로고
    • The Epstein-Barr virus lytic program is controlled by the co-operative functions of two transactivators
    • Feederle R., Kost M., Baumann M., Janz A., Drouet E., Hammerschmidt W., and Delecluse H.J. The Epstein-Barr virus lytic program is controlled by the co-operative functions of two transactivators EMBO J. 19 2000 3080 3089 (Pubitemid 30386778)
    • (2000) EMBO Journal , vol.19 , Issue.12 , pp. 3080-3089
    • Feederle, R.1    Kost, M.2    Baumann, M.3    Janz, A.4    Drouet, E.5    Hammerschmidt, W.6    Delecluse, H.-J.7
  • 26
    • 0038678667 scopus 로고    scopus 로고
    • Synergistic autoactivation of the Epstein-Barr virus immediate-early BRLF1 promoter by Rta and Zta
    • DOI 10.1016/S0042-6822(03)00145-4
    • Liu P., and Speck S.H. Synergistic autoactivation of the Epstein-Barr virus immediate-early BRLF1 promoter by Rta and Zta Virology 310 2003 199 206 (Pubitemid 37487621)
    • (2003) Virology , vol.310 , Issue.2 , pp. 199-206
    • Liu, P.1    Speck, S.H.2
  • 27
    • 4944266319 scopus 로고    scopus 로고
    • Epstein-Barr virus: 40 Years on
    • DOI 10.1038/nrc1452
    • Young L.S., and Rickinson A.B. Epstein-Barr virus: 40 years on Nat. Rev. Cancer 4 2004 757 768 (Pubitemid 39331148)
    • (2004) Nature Reviews Cancer , vol.4 , Issue.10 , pp. 757-768
    • Young, L.S.1    Rickinson, A.B.2
  • 29
    • 77749289862 scopus 로고    scopus 로고
    • Identification of bZIP interaction partners of viral proteins HBZ, MEQ, BZLF1, and K-bZIP using coiled-coil arrays
    • Reinke A.W., Grigoryan G., and Keating A.E. Identification of bZIP interaction partners of viral proteins HBZ, MEQ, BZLF1, and K-bZIP using coiled-coil arrays Biochemistry 49 2010 1985 1997
    • (2010) Biochemistry , vol.49 , pp. 1985-1997
    • Reinke, A.W.1    Grigoryan, G.2    Keating, A.E.3
  • 30
    • 0038420735 scopus 로고    scopus 로고
    • The zipper region of Epstein-Barr virus bZIP transcription factor Zta is necessary but not sufficient to direct DNA binding
    • DOI 10.1128/JVI.77.14.8173-8177.2003
    • Hicks M.R., Al-Mehairi S.S., and Sinclair A.J. The zipper region of Epstein-Barr virus bZIP transcription factor Zta is necessary but not sufficient to direct DNA binding J. Virol. 77 2003 8173 8177 (Pubitemid 36792814)
    • (2003) Journal of Virology , vol.77 , Issue.14 , pp. 8173-8177
    • Hicks, M.R.1    Al-Mehairi, S.S.2    Sinclair, A.J.3
  • 31
    • 0000236570 scopus 로고
    • Peptide 'Velcro': Design of a heterodimeric coiled coil
    • O'Shea E.K., Lumb K.J., and Kim P.S. Peptide 'Velcro': design of a heterodimeric coiled coil Curr. Biol. 3 1993 658 667
    • (1993) Curr. Biol. , vol.3 , pp. 658-667
    • O'Shea, E.K.1    Lumb, K.J.2    Kim, P.S.3
  • 33
    • 17444433002 scopus 로고    scopus 로고
    • The design of coiled-coil structures and assemblies
    • DOI 10.1016/S0065-3233(05)70004-8, Fibrous Proteins Coiled-Coils, Collagen and Elastomers
    • Woolfson D.N. The design of coiled-coil structures and assemblies Adv. Protein Chem. 70 2005 79 112 (Pubitemid 40544781)
    • (2005) Advances in Protein Chemistry , vol.70 , pp. 79-112
    • Woolfson, D.N.1
  • 34
    • 49549094267 scopus 로고    scopus 로고
    • Structural specificity in coiled-coil interactions
    • Grigoryan G., and Keating A. Structural specificity in coiled-coil interactions Curr. Opin. Struct. Biol. 18 2008 477 483
    • (2008) Curr. Opin. Struct. Biol. , vol.18 , pp. 477-483
    • Grigoryan, G.1    Keating, A.2
  • 35
    • 0027756896 scopus 로고
    • A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants
    • Harbury P.B., Zhang T., Kim P.S., and Alber T. A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants Science 262 1993 1401 1407
    • (1993) Science , vol.262 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 36
    • 28944446279 scopus 로고    scopus 로고
    • Orientation and oligomerization specificity of the Bcr coiled-coil oligomerization domain
    • DOI 10.1021/bi051493t
    • Taylor C.M., and Keating A.E. Orientation and oligomerization specificity of the Bcr coiled-coil oligomerization domain Biochemistry 44 2005 16246 16256 (Pubitemid 41785823)
    • (2005) Biochemistry , vol.44 , Issue.49 , pp. 16246-16256
    • Taylor, C.M.1    Keating, A.E.2
  • 37
    • 4344575287 scopus 로고    scopus 로고
    • Coiled coil domains: Stability, specificity, and biological implications
    • DOI 10.1002/cbic.200300781
    • Mason J.M., and Arndt K.M. Coiled coil domains: stability, specificity, and biological implications ChemBioChem 5 2004 170 176 (Pubitemid 39256232)
    • (2004) ChemBioChem , vol.5 , Issue.2 , pp. 170-176
    • Mason, J.M.1    Arndt, K.M.2
  • 38
    • 0030804094 scopus 로고    scopus 로고
    • Leucine is the most stabilizing aliphatic amino acid in the d position of a dimeric leucine zipper coiled coil
    • DOI 10.1021/bi971424h
    • Moitra J., Szila'k L., Krylov D., and Vinson C. Leucine is the most stabilizing aliphatic amino acid in the d position of a dimeric leucine zipper coiled coil Biochemistry 36 1997 12567 12573 (Pubitemid 27446681)
    • (1997) Biochemistry , vol.36 , Issue.41 , pp. 12567-12573
    • Moitra, J.1    Szilak, L.2    Krylov, D.3    Vinson, C.4
  • 39
    • 1342268069 scopus 로고    scopus 로고
    • Defining the minimum size of a hydrophobic cluster in two-stranded α-helical coiled-coils: Effects on protein stability
    • DOI 10.1110/ps.03443204
    • Lu S.M., and Hodges R.S. Defining the minimum size of a hydrophobic cluster in two-stranded alpha-helical coiled-coils: effects on protein stability Protein Sci. 13 2004 714 726 (Pubitemid 38252569)
    • (2004) Protein Science , vol.13 , Issue.3 , pp. 714-726
    • Lu, S.M.1    Hodges, R.S.2
  • 40
    • 2242475745 scopus 로고    scopus 로고
    • A heterodimerizing leucine zipper coiled coil system for examining the specificity of a position interactions: Amino acids I, V, L, N, A, and K
    • DOI 10.1021/bi020486r
    • Acharya A., Ruvinov S.B., Gal J., Moll J.R., and Vinson C. A heterodimerizing leucine zipper coiled coil system for examining the specificity of a position interactions: amino acids I, V, L, N, A, and K Biochemistry 41 2002 14122 14131 (Pubitemid 35403330)
    • (2002) Biochemistry , vol.41 , Issue.48 , pp. 14122-14131
    • Acharya, A.1    Ruvinov, S.B.2    Gal, J.3    Moll, J.R.4    Vinson, C.5
  • 41
    • 0034616959 scopus 로고    scopus 로고
    • Effects of side-chain characteristics on stability and oligomerization state of a de novo-designed model coiled-coil: 20 amino acid substitutions in position "d"
    • Tripet B., Wagschal K., Lavigne P., Mant C.T., and Hodges R.S. Effects of side-chain characteristics on stability and oligomerization state of a de novo-designed model coiled-coil: 20 amino acid substitutions in position "d" J. Mol. Biol. 300 2000 377 402
    • (2000) J. Mol. Biol. , vol.300 , pp. 377-402
    • Tripet, B.1    Wagschal, K.2    Lavigne, P.3    Mant, C.T.4    Hodges, R.S.5
  • 42
    • 0037217406 scopus 로고    scopus 로고
    • Automated design of specificity in molecular recognition
    • DOI 10.1038/nsb877
    • Havranek J.J., and Harbury P.B. Automated design of specificity in molecular recognition Nat. Struct. Biol. 10 2003 45 52 (Pubitemid 36034176)
    • (2003) Nature Structural Biology , vol.10 , Issue.1 , pp. 45-52
    • Havranek, J.J.1    Harbury, P.B.2
  • 43
    • 77951685234 scopus 로고    scopus 로고
    • A synthetic coiled-coil interactome provides heterospecific modules for molecular engineering
    • Reinke A.W., Grant R.A., and Keating A.E. A synthetic coiled-coil interactome provides heterospecific modules for molecular engineering J. Am. Chem. Soc. 132 2010 6025 6031
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 6025-6031
    • Reinke, A.W.1    Grant, R.A.2    Keating, A.E.3
  • 44
    • 51749124224 scopus 로고    scopus 로고
    • Targeting metastable coiled-coil domains by computational design
    • Barth P., Schoeffler A., and Alber T. Targeting metastable coiled-coil domains by computational design J. Am. Chem. Soc. 130 2008 12038 12044
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 12038-12044
    • Barth, P.1    Schoeffler, A.2    Alber, T.3
  • 45
    • 70349775833 scopus 로고    scopus 로고
    • Backbone flexibility in computational protein design
    • Mandell D.J., and Kortemme T. Backbone flexibility in computational protein design Curr. Opin. Biotechnol. 20 2009 420 428
    • (2009) Curr. Opin. Biotechnol. , vol.20 , pp. 420-428
    • Mandell, D.J.1    Kortemme, T.2
  • 47
    • 13844297691 scopus 로고    scopus 로고
    • Design of a heterospecific, tetrameric, 21-residue miniprotein with mixed α/β structure
    • DOI 10.1016/j.str.2004.12.009
    • Ali M.H., Taylor C.M., Grigoryan G., Allen K.N., Imperiali B., and Keating A.E. Design of a heterospecific, tetrameric, 21-residue miniprotein with mixed alpha/beta structure Structure 13 2005 225 234 (Pubitemid 40247698)
    • (2005) Structure , vol.13 , Issue.2 , pp. 225-234
    • Ali, M.H.1    Taylor, C.M.2    Grigoryan, G.3    Allen, K.N.4    Imperiali, B.5    Keating, A.E.6
  • 49
    • 77949327063 scopus 로고    scopus 로고
    • Computational design of second-site suppressor mutations at protein-protein interfaces
    • Sammond D.W., Eletr Z.M., Purbeck C., and Kuhlman B. Computational design of second-site suppressor mutations at protein-protein interfaces Proteins 78 2010 1055 1065
    • (2010) Proteins , vol.78 , pp. 1055-1065
    • Sammond, D.W.1    Eletr, Z.M.2    Purbeck, C.3    Kuhlman, B.4
  • 50
    • 69249158062 scopus 로고    scopus 로고
    • Computational design of affinity and specificity at protein-protein interfaces
    • Karanicolas J., and Kuhlman B. Computational design of affinity and specificity at protein-protein interfaces Curr. Opin. Struct. Biol. 19 2009 458 463
    • (2009) Curr. Opin. Struct. Biol. , vol.19 , pp. 458-463
    • Karanicolas, J.1    Kuhlman, B.2
  • 51
    • 34547121250 scopus 로고    scopus 로고
    • L
    • DOI 10.1016/j.jmb.2007.04.069, PII S0022283607005827
    • Fu X., Apgar J.R., and Keating A.E. Modeling backbone flexibility to achieve sequence diversity: the design of novel alpha-helical ligands for Bcl-xL J. Mol. Biol. 371 2007 1099 1117 (Pubitemid 47101807)
    • (2007) Journal of Molecular Biology , vol.371 , Issue.4 , pp. 1099-1117
    • Fu, X.1    Apgar, J.R.2    Keating, A.E.3
  • 52
    • 0037095730 scopus 로고    scopus 로고
    • DNAWorks: An automated method for designing oligonucleotides for PCR-based gene synthesis
    • Hoover D.M., and Lubkowski J. DNAWorks: an automated method for designing oligonucleotides for PCR-based gene synthesis Nucleic Acids Res. 30 2002 e43
    • (2002) Nucleic Acids Res. , vol.30 , pp. 43
    • Hoover, D.M.1    Lubkowski, J.2
  • 53
    • 79958099694 scopus 로고    scopus 로고
    • Analytical Ultracentrifugation Facility, University of Connecticut Storrs, CT
    • Cole J.L., and Lary J.W. HeteroAnalysis 2006 Analytical Ultracentrifugation Facility, University of Connecticut Storrs, CT
    • (2006) HeteroAnalysis
    • Cole, J.L.1    Lary, J.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.