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Volumn 48, Issue 36, 2009, Pages 8559-8567

N-terminal aliphatic residues dictate the structure, stability, assembly, and small molecule binding of the coiled-coil region of cartilage oligomeric matrix protein

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE-SCANNING MUTAGENESIS; ALL-TRANS-RETINOL; COILED COIL; COILED-COIL DOMAINS; CURCUMIN; HELICAL STRUCTURES; HYDROPHOBIC POCKETS; MATRIX PROTEINS; N-TERMINALS; POLAR RESIDUES; SMALL MOLECULES; SMALL-MOLECULE BINDINGS;

EID: 70149086075     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900534r     Document Type: Article
Times cited : (69)

References (63)
  • 2
    • 0028090357 scopus 로고
    • Cartilage Oligomeric Matrix Protein (Comp) Is an Abundant Component of Tendon
    • Dicesare, P., Hauser, N., Lehman, D., Pasumarti, S., and Paulsson, M. (1994) Cartilage Oligomeric Matrix Protein (Comp) Is an Abundant Component of Tendon. FEBS Lett. 354, 237-240.
    • (1994) FEBS Lett. , vol.354 , pp. 237-240
    • Dicesare, P.1    Hauser, N.2    Lehman, D.3    Pasumarti, S.4    Paulsson, M.5
  • 3
    • 0032456952 scopus 로고    scopus 로고
    • COMP (cartilage oligomeric matrix protein) is synthesized in ligament tendon, meniscus and articular cartilage
    • Muller, G., Michele, A., and Altenburg, E. (1998) COMP (cartilage oligomeric matrix protein) is synthesized in ligament tendon, meniscus and articular cartilage. Connect. Tissue Res. 39, 233-244.
    • (1998) Connect. Tissue Res. , vol.39 , pp. 233-244
    • Muller, G.1    Michele, A.2    Altenburg, E.3
  • 4
    • 0034264873 scopus 로고    scopus 로고
    • Expression of cartilage oligomeric matrix protein (COMP) by embryonic and adult osteoblasts
    • Di Cesare, P. E., Fang, C., Leslie, M. P., Tulli, H., Perris, R., and Carlson, C. S. (2000) Expression of cartilage oligomeric matrix protein (COMP) by embryonic and adult osteoblasts. J. Orthop. Res. 18, 713-720.
    • (2000) J. Orthop. Res. , vol.18 , pp. 713-720
    • Di Cesare, P.E.1    Fang, C.2    Leslie, M.P.3    Tulli, H.4    Perris, R.5    Carlson, C.S.6
  • 5
    • 0026499722 scopus 로고
    • Comp (Cartilage Oligomeric Matrix Protein) Is Structurally Related to the Thrombospondins
    • Oldberg, A., Antonsson, P., Lindblom, K., and Heinegard, D. (1992) Comp (Cartilage Oligomeric Matrix Protein) Is Structurally Related to the Thrombospondins. J. Biol. Chem. 267, 22346-22350.
    • (1992) J. Biol. Chem. , vol.267 , pp. 22346-22350
    • Oldberg, A.1    Antonsson, P.2    Lindblom, K.3    Heinegard, D.4
  • 6
    • 0028213804 scopus 로고
    • The Thrombospondin-Like Chains of Cartilage Oligomeric Matrix Protein Are Assembled by a 5-Stranded R-Helical Bundle between Residue-20 and Residue-83
    • Efimov, V. P., Lustig, A., and Engel, J. (1994) The Thrombospondin-Like Chains of Cartilage Oligomeric Matrix Protein Are Assembled by a 5-Stranded R-Helical Bundle between Residue-20 and Residue-83. FEBS Lett. 341, 54-58.
    • (1994) FEBS Lett. , vol.341 , pp. 54-58
    • Efimov, V.P.1    Lustig, A.2    Engel, J.3
  • 7
    • 0032493665 scopus 로고    scopus 로고
    • Cartilage oligomeric matrix protein shows high affinity zinc-dependent interaction with triple helical collagen
    • Rosenberg, K., Olsson, H., Morgelin, M., and Heinegard, D. (1998) Cartilage oligomeric matrix protein shows high affinity zinc-dependent interaction with triple helical collagen. J. Biol. Chem. 273, 20397-20403.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20397-20403
    • Rosenberg, K.1    Olsson, H.2    Morgelin, M.3    Heinegard, D.4
  • 8
    • 35748950738 scopus 로고    scopus 로고
    • COMP acts as a catalyst in collagen fibrillogenesis
    • Halasz, K., Kassner, A., Morgelin, M., and Heinegard, D. (2007) COMP acts as a catalyst in collagen fibrillogenesis. J. Biol. Chem. 282, 31166-31173.
    • (2007) J. Biol. Chem. , vol.282 , pp. 31166-31173
    • Halasz, K.1    Kassner, A.2    Morgelin, M.3    Heinegard, D.4
  • 11
    • 0942290435 scopus 로고    scopus 로고
    • 587 f Arg) in the C-terminal, collagen-binding domain of cartilage oligomeric matrix protein (COMP)
    • DOI 10.1042/BJ20031179
    • Spitznagel, L., Nitsche, D. P., Paulsson, M., Maurer, P., and Zaucke, F. (2004) Characterization of a pseudoachondroplasia-associated mutation (His(587) f Arg) in the C-terminal, collagen-binding domain of cartilage oligomeric matrix protein (COMP). Biochem. J. 377, 479-487. (Pubitemid 38142203)
    • (2004) Biochemical Journal , vol.377 , Issue.2 , pp. 479-487
    • Spitznagel, L.1    Nitsche, D.P.2    Paulsson, M.3    Maurer, P.4    Zaucke, F.5
  • 12
    • 13444269135 scopus 로고    scopus 로고
    • COMP mutations, chondrocyte function and cartilage matrix
    • DOI 10.1016/j.matbio.2004.09.006, PII S0945053X04001234
    • Hecht, J. T., Hayes, E., Haynes, R., and Cole, W. G. (2005) COMP mutations, chondrocyte function and cartilage matrix. Matrix Biol. 23, 525-533. (Pubitemid 40202751)
    • (2005) Matrix Biology , vol.23 , Issue.8 , pp. 525-533
    • Hecht, J.T.1    Hayes, E.2    Haynes, R.3    Cole, W.G.4
  • 13
    • 18844427523 scopus 로고    scopus 로고
    • COMP mutation screening as an aid for the clinical diagnosis and counselling of patients with a suspected diagnosis of pseudoachondroplasia or multiple epiphyseal dysplasia
    • Kennedy, J., Jackson, G., Ramsden, S., Taylor, J., Newman, W., Wright, M. J., Donnai, D., Elles, R., and Briggs, M. D. (2005) COMP mutation screening as an aid for the clinical diagnosis and counselling of patients with a suspected diagnosis of pseudoachondroplasia or multiple epiphyseal dysplasia. Eur. J. Hum. Genet. 13, 547-555.
    • (2005) Eur. J. Hum. Genet. , vol.13 , pp. 547-555
    • Kennedy, J.1    Jackson, G.2    Ramsden, S.3    Taylor, J.4    Newman, W.5    Wright, M.J.6    Donnai, D.7    Elles, R.8    Briggs, M.D.9
  • 14
    • 39049089695 scopus 로고    scopus 로고
    • COMP mutations: Domain-dependent relationship between abnormal chondrocyte trafficking and clinical PSACH and MED phenotypes
    • Chen, T. L. L., Posey, K. L., Hecht, J. T., and Vertel, B. M. (2008) COMP mutations: Domain-dependent relationship between abnormal chondrocyte trafficking and clinical PSACH and MED phenotypes. J. Cell. Biochem. 103, 778-787.
    • (2008) J. Cell. Biochem. , vol.103 , pp. 778-787
    • Chen, T.L.L.1    Posey, K.L.2    Hecht, J.T.3    Vertel, B.M.4
  • 15
    • 0029868783 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic study of the pentamerizing domain from cartilage oligomeric matrix protein: A five- Stranded α-helical bundle
    • DOI 10.1002/(SICI)1097-0134(199602)24:2<259::AID-PROT13>3.0.CO;2-M
    • Efimov, V. P., Engel, J., and Malashkevich, V. N. (1996) Crystallization and preliminary crystallographic study of the pentamerizing domain from cartilage oligomeric matrix protein: A five-stranded α-helical bundle. Proteins: Struct., Funct., Genet. 24, 259-262. (Pubitemid 26076374)
    • (1996) Proteins: Structure, Function and Genetics , vol.24 , Issue.2 , pp. 259-262
    • Efimov, V.P.1    Engel, J.2    Malashkevich, V.N.3
  • 16
    • 0029911261 scopus 로고    scopus 로고
    • The crystal structure of a five-stranded coiled coil in COMP: A prototype ion channel?
    • Malashkevich, V. N., Kammerer, R. A., Efimov, V. P., Schulthess, T., and Engel, J. (1996) The crystal structure of a five-stranded coiled coil in COMP: A prototype ion channel? Science 274, 761-765.
    • (1996) Science , vol.274 , pp. 761-765
    • Malashkevich, V.N.1    Kammerer, R.A.2    Efimov, V.P.3    Schulthess, T.4    Engel, J.5
  • 17
    • 0032530389 scopus 로고    scopus 로고
    • All-trans retinol, vitamin D and other hydrophobic compounds bind in the axial pore of the five-stranded coiled-coil domain of cartilage oligomeric matrix protein
    • DOI 10.1093/emboj/17.18.5265
    • Guo, Y., Bozic, D., Malashkevich, V. N., Kammerer, R. A., Schulthess, T., and Enger, J. (1998) All-trans retinol, vitamin D and other hydrophobic compounds bind in the axial pore of the five-stranded coiled-coil domain of cartilage oligomeric matrix protein. EMBO J. 17, 5265-5272. (Pubitemid 28427042)
    • (1998) EMBO Journal , vol.17 , Issue.18 , pp. 5265-5272
    • Guo, Y.1    Bozic, D.2    Malashkevich, V.N.3    Kammerer, R.A.4    Schulthess, T.5    Engel, J.6
  • 18
    • 0033935599 scopus 로고    scopus 로고
    • The unusually stable coiled-coil domain of COMP exhibits cold and heat denaturation in 4-6 M guanidinium chloride
    • Guo, Y., Kammerer, R. A., and Engel, J. (2000) The unusually stable coiled-coil domain of COMP exhibits cold and heat denaturation in 4-6 M guanidinium chloride. Biophys. Chem. 85, 179-186.
    • (2000) Biophys. Chem. , vol.85 , pp. 179-186
    • Guo, Y.1    Kammerer, R.A.2    Engel, J.3
  • 19
    • 0037112753 scopus 로고    scopus 로고
    • 3
    • DOI 10.1093/emboj/cdf628
    • Ozbek, S., Engel, J., and Stetefeld, J. (2002) Storage function of cartilage oligomeric matrix protein: The crystal structure of the coiled-coil domain in complex with vitamin D-3. EMBO J. 21, 5960-5968. (Pubitemid 35415314)
    • (2002) EMBO Journal , vol.21 , Issue.22 , pp. 5960-5968
    • Ozbek, S.1    Engel, J.2    Stetefeld, J.3
  • 20
    • 53249133258 scopus 로고    scopus 로고
    • Mutation Gln(54)Leu of the conserved polar residue in the interfacial coiled coil position (d) results in significant stabilization of the original structure of the COMP pentamerization domain
    • Terskikh, A. V., Potekhin, S. A., Melnik, T. N., and Kajava, A. V. (1997) Mutation Gln(54)Leu of the conserved polar residue in the interfacial coiled coil position (d) results in significant stabilization of the original structure of the COMP pentamerization domain. Lett. Pept. Sci. 4, 297-304.
    • (1997) Lett. Pept. Sci. , vol.4 , pp. 297-304
    • Terskikh, A.V.1    Potekhin, S.A.2    Melnik, T.N.3    Kajava, A.V.4
  • 21
    • 0037305504 scopus 로고    scopus 로고
    • Computational design of a water-soluble analog of phospholamban
    • Slovic, A. M., Summa, C. M., Lear, J. D., and DeGrado, W. F. (2003) Computational design of a water-soluble analog of phospholamban. Protein Sci. 12, 337-348.
    • (2003) Protein Sci. , vol.12 , pp. 337-348
    • Slovic, A.M.1    Summa, C.M.2    Lear, J.D.3    DeGrado, W.F.4
  • 22
    • 16444362685 scopus 로고    scopus 로고
    • De novo design of a pentameric coiled-coil: Decoding the motif for tetramer versus pentamer formation in water-soluble phospholamban
    • Slovic, A. M., Lear, J. D., and DeGrado, W. F. (2005) De novo design of a pentameric coiled-coil: Decoding the motif for tetramer versus pentamer formation in water-soluble phospholamban. J. Pept. Res. 65, 312-321.
    • (2005) J. Pept. Res. , vol.65 , pp. 312-321
    • Slovic, A.M.1    Lear, J.D.2    DeGrado, W.F.3
  • 24
    • 0038265111 scopus 로고    scopus 로고
    • A novel method to measure self-association of small amphipathic molecules: Temperature profiling in reversed-phase chromatography
    • Lee, D. L., Mant, C. T., and Hodges, R. S. (2003) A novel method to measure self-association of small amphipathic molecules: temperature profiling in reversed-phase chromatography. J. Biol. Chem. 278, 22918-22927.
    • (2003) J. Biol. Chem. , vol.278 , pp. 22918-22927
    • Lee, D.L.1    Mant, C.T.2    Hodges, R.S.3
  • 25
    • 33750078696 scopus 로고    scopus 로고
    • Glutamine deamidation destabilizes human γD-crystallin and lowers the kinetic barrier to unfolding
    • Flaugh, S. L., Mills, I. A., and King, J. (2006) Glutamine deamidation destabilizes human γD-crystallin and lowers the kinetic barrier to unfolding. J. Biol. Chem. 281, 30782-30793.
    • (2006) J. Biol. Chem. , vol.281 , pp. 30782-30793
    • Flaugh, S.L.1    Mills, I.A.2    King, J.3
  • 26
    • 0027404071 scopus 로고
    • Stabilization of α-helical structures in short peptides via end capping
    • Forood, B., Feliciano, E. J., and Nambiar, K. P. (1993) Stabilization of α-helical structures in short peptides via end capping. Proc. Natl. Acad. Sci. U.S.A. 90, 838-842.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 838-842
    • Forood, B.1    Feliciano, E.J.2    Nambiar, K.P.3
  • 27
    • 0025420076 scopus 로고
    • Measuring and Increasing Protein Stability
    • Pace, C. N. (1990) Measuring and Increasing Protein Stability. Trends Biotechnol. 8, 93-98.
    • (1990) Trends Biotechnol. , vol.8 , pp. 93-98
    • Pace, C.N.1
  • 28
    • 0023406843 scopus 로고
    • Calculating thermodynamic data for transitions of any molecularity from equilibrium melting curves
    • Marky, L. A., and Breslauer, K. J. (1987) Calculating thermodynamic data for transitions of any molecularity from equilibrium melting curves. Biopolymers 26, 1601-1620.
    • (1987) Biopolymers , vol.26 , pp. 1601-1620
    • Marky, L.A.1    Breslauer, K.J.2
  • 29
    • 0029969360 scopus 로고    scopus 로고
    • The C-terminal domain of cartilage matrix protein assembles into a triple-stranded α-helical coiled-coil structure
    • Beck, K., Gambee, J. E., Bohan, C. A., and Bachinger, H. P. (1996) The C-terminal domain of cartilage matrix protein assembles into a triple-stranded α-helical coiled-coil structure. J. Mol. Biol. 256, 909-923.
    • (1996) J. Mol. Biol. , vol.256 , pp. 909-923
    • Beck, K.1    Gambee, J.E.2    Bohan, C.A.3    Bachinger, H.P.4
  • 30
    • 0030983330 scopus 로고    scopus 로고
    • A single amino acid can switch the oligomerization state of the α-helical coiled-coil domain of cartilage matrix protein
    • DOI 10.1093/emboj/16.13.3767
    • Beck, K., Gambee, J. E., Kamawal, A., and Bachinger, H. P. (1997) A single amino acid can switch the oligomerization state of the α-helical coiled-coil domain of cartilage matrix protein. EMBO J. 16, 3767-3777. (Pubitemid 27280992)
    • (1997) EMBO Journal , vol.16 , Issue.13 , pp. 3767-3777
    • Beck, K.1    Gambee, J.E.2    Kamawal, A.3    Bachinger, H.P.4
  • 31
    • 0019756004 scopus 로고
    • Analysis of Data from the Analytical Ultra-Centrifuge by Non-Linear Least-Squares Techniques
    • Johnson, M. L., Correia, J. J., Yphantis, D. A., and Halvorson, H. R. (1981) Analysis of Data from the Analytical Ultra-Centrifuge by Non-Linear Least-Squares Techniques. Biophys. J. 36, 575-588.
    • (1981) Biophys. J. , vol.36 , pp. 575-588
    • Johnson, M.L.1    Correia, J.J.2    Yphantis, D.A.3    Halvorson, H.R.4
  • 32
    • 0002498995 scopus 로고
    • Computer-aided interpretation of analytical sedimentation data for proteins
    • (Harding, S. E., Rowe, A. J., and Horton, J. C., Eds.) Royal Society of Chemistry, Cambridge, U.K.
    • Laue, T. M., Shah, B. D., Ridgeway, T. M., and Pelletier, S. L. (1992) Computer-aided interpretation of analytical sedimentation data for proteins. In Analytical Ultracentrifugation in Biochemistry and Polymer Science (Harding, S. E., Rowe, A. J., and Horton, J. C., Eds.) pp 90-125, Royal Society of Chemistry, Cambridge, U.K.
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 90-125
    • Laue, T.M.1    Shah, B.D.2    Ridgeway, T.M.3    Pelletier, S.L.4
  • 33
    • 0345328130 scopus 로고    scopus 로고
    • Photophysical studies on binding curcumin to bovine serum albumin
    • Barik, A., Priyadarsini, K. I., and Mohan, H. (2003) Photophysical studies on binding curcumin to bovine serum albumin. Photochem. Photobiol. 77, 597-603.
    • (2003) Photochem. Photobiol. , vol.77 , pp. 597-603
    • Barik, A.1    Priyadarsini, K.I.2    Mohan, H.3
  • 34
    • 0034335286 scopus 로고    scopus 로고
    • Effect of solvent on the excited-state photophysical properties of curcumin
    • Khopde, S. M., Priyadarsini, K. I., Palit, D. K., and Mukherjee, T. (2000) Effect of solvent on the excited-state photophysical properties of curcumin. Photochem. Photobiol. 72, 626-631.
    • (2000) Photochem. Photobiol. , vol.72 , pp. 626-631
    • Khopde, S.M.1    Priyadarsini, K.I.2    Palit, D.K.3    Mukherjee, T.4
  • 35
    • 34548847733 scopus 로고    scopus 로고
    • Using circular dichroism spectra to estimate protein secondary structure
    • Greenfield, N. J. (2006) Using circular dichroism spectra to estimate protein secondary structure. Nat. Protoc. 1, 2876-2890.
    • (2006) Nat. Protoc. , vol.1 , pp. 2876-2890
    • Greenfield, N.J.1
  • 36
    • 34548819311 scopus 로고    scopus 로고
    • Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions
    • Greenfield, N. J. (2006) Using circular dichroism collected as a function of temperature to determine the thermodynamics of protein unfolding and binding interactions. Nat. Protoc. 1, 2527-2535.
    • (2006) Nat. Protoc. , vol.1 , pp. 2527-2535
    • Greenfield, N.J.1
  • 37
    • 0025271463 scopus 로고
    • PH Dependence of the Urea and Guanidine-Hydrochloride Denaturation of Ribonuclease-a and Ribonuclease-T1
    • Pace, C. N., Laurents, D. V., and Thomson, J. A. (1990) pH Dependence of the Urea and Guanidine-Hydrochloride Denaturation of Ribonuclease-a and Ribonuclease-T1. Biochemistry 29, 2564-2572.
    • (1990) Biochemistry , vol.29 , pp. 2564-2572
    • Pace, C.N.1    Laurents, D.V.2    Thomson, J.A.3
  • 38
    • 0032546758 scopus 로고    scopus 로고
    • Inter-helical interactions in the leucine zipper coiled coil dimer: PH and salt dependence of coupling energy between charged amino acids
    • Krylov, D., Barchi, J., and Vinson, C. (1998) Inter-helical interactions in the leucine zipper coiled coil dimer: pH and salt dependence of coupling energy between charged amino acids. J. Mol. Biol. 279, 959-972.
    • (1998) J. Mol. Biol. , vol.279 , pp. 959-972
    • Krylov, D.1    Barchi, J.2    Vinson, C.3
  • 39
    • 0027050850 scopus 로고
    • Newly ientified actions of the vitamin D endocrine system
    • Walters, M. R. (1992) Newly ientified actions of the vitamin D endocrine system. Endocrinol. Rev. 13, 719-764.
    • (1992) Endocrinol. Rev. , vol.13 , pp. 719-764
    • Walters, M.R.1
  • 40
    • 0028988403 scopus 로고
    • Structure-function relationships in the vitamin D endocrine system
    • Bouillon, R., Okamura, W. H., and Norman, A. W. (1995) Structure-function relationships in the vitamin D endocrine system. Endocrinol. Rev. 16, 200-257.
    • (1995) Endocrinol. Rev. , vol.16 , pp. 200-257
    • Bouillon, R.1    Okamura, W.H.2    Norman, A.W.3
  • 41
    • 0029007929 scopus 로고
    • The roles of retinoids un vertebrate development
    • Means, A. L., and Gudas, L. J. (1995) The roles of retinoids un vertebrate development. Annu. Rev. Biochem. 64, 201-233.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 201-233
    • Means, A.L.1    Gudas, L.J.2
  • 43
    • 0142039525 scopus 로고    scopus 로고
    • Antiproliferative effect of curcumin against human breast tumor cell lines
    • Mehta, K., Pantazis, P., McQueen, T., and Agarwal, B. (1997) Antiproliferative effect of curcumin against human breast tumor cell lines. Anticancer Drugs 8, 471-480.
    • (1997) Anticancer Drugs , vol.8 , pp. 471-480
    • Mehta, K.1    Pantazis, P.2    McQueen, T.3    Agarwal, B.4
  • 45
    • 0034618287 scopus 로고    scopus 로고
    • On the antioxidant mechanism of curucmin: Classical methods are needed to determine antioxidant mechanism and activity
    • Barclay, L. R. C., Vinqvist, M. R., Mukai, K., Goto, H., Hasimoto, Y., Tokunaga, A., and Uno, H. (2000) On the antioxidant mechanism of curucmin: Classical methods are needed to determine antioxidant mechanism and activity. Org. Lett. 2, 2841-2843.
    • (2000) Org. Lett. , vol.2 , pp. 2841-2843
    • Barclay, L.R.C.1    Vinqvist, M.R.2    Mukai, K.3    Goto, H.4    Hasimoto, Y.5    Tokunaga, A.6    Uno, H.7
  • 46
    • 10944243759 scopus 로고    scopus 로고
    • Curcumin, a novel p300/CREB-binding protein-specific inhibitor of acetyltransferase, represses the acetylation of histone/nonhistone proteins and histone acetyltransferase-dependent chromatin transcription
    • Balasubramanyam, K., Varier, R. A., Altaf, M., Swaminathan, V., Siddappa, N. B., Ranga, U., and Kundu, T. K. (2004) Curcumin, a novel p300/CREB-binding protein-specific inhibitor of acetyltransferase, represses the acetylation of histone/nonhistone proteins and histone acetyltransferase-dependent chromatin transcription. J. Biol. Chem. 279, 51163-51171.
    • (2004) J. Biol. Chem. , vol.279 , pp. 51163-51171
    • Balasubramanyam, K.1    Varier, R.A.2    Altaf, M.3    Swaminathan, V.4    Siddappa, N.B.5    Ranga, U.6    Kundu, T.K.7
  • 48
    • 4344575287 scopus 로고    scopus 로고
    • Coiled coil domains: Stability, specificity, and biological implications
    • Mason, J. M., and Arndt, K. M. (2004) Coiled coil domains: Stability, specificity, and biological implications. ChemBioChem 5, 170-176.
    • (2004) ChemBioChem , vol.5 , pp. 170-176
    • Mason, J.M.1    Arndt, K.M.2
  • 49
    • 0024295767 scopus 로고
    • The Leucine Zipper: A Hypothetical Structure Common to a New Class of DNA-Binding Proteins
    • Landschulz, W. H., Johnson, P. F., and McKnight, S. L. (1988) The Leucine Zipper: A Hypothetical Structure Common to a New Class of DNA-Binding Proteins. Science 240, 1759-1764.
    • (1988) Science , vol.240 , pp. 1759-1764
    • Landschulz, W.H.1    Johnson, P.F.2    McKnight, S.L.3
  • 51
    • 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. (1993) A Switch between 2-Stranded, 3-Stranded and 4-Stranded Coiled Coils in Gcn4 Leucine-Zipper Mutants. Science 262, 1401-1407. (Pubitemid 23983059)
    • (1993) Science , vol.262 , Issue.5138 , pp. 1401-1407
    • Harbury, P.B.1    Zhang, T.2    Kim, P.S.3    Alber, T.4
  • 52
    • 0035881152 scopus 로고    scopus 로고
    • Electrostatic control of half-site spacing preferences by the cyclic AMP response element-binding protein CREB
    • Montclare, J. K., Sloan, L. S., and Schepartz, A. (2001) Electrostatic control of half-site spacing preferences by the cyclic AMP response element-binding protein CREB. Nucleic Acids Res. 29, 3311-3319.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3311-3319
    • Montclare, J.K.1    Sloan, L.S.2    Schepartz, A.3
  • 53
    • 38649119754 scopus 로고    scopus 로고
    • Orthogonal recognition in dimeric coiled coils via buried polar-group modulation
    • Diss, M. L., and Kennan, A. J. (2008) Orthogonal recognition in dimeric coiled coils via buried polar-group modulation. J. Am. Chem. Soc. 130, 1321-1327.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 1321-1327
    • Diss, M.L.1    Kennan, A.J.2
  • 55
    • 33645300372 scopus 로고    scopus 로고
    • The effects of the side chains of hydrophobic aliphatic amino acid residues in an amphipathic polypeptide on the formation of a helix and its association
    • Takei, T., Okonogi, A., Tateno, K., Kimura, A., Kojima, S., Yazaki, K., and Miura, K. (2006) The effects of the side chains of hydrophobic aliphatic amino acid residues in an amphipathic polypeptide on the formation of a helix and its association. J. Biochem. 139, 271-278.
    • (2006) J. Biochem. , vol.139 , pp. 271-278
    • Takei, T.1    Okonogi, A.2    Tateno, K.3    Kimura, A.4    Kojima, S.5    Yazaki, K.6    Miura, K.7
  • 56
    • 0029862745 scopus 로고    scopus 로고
    • A leucine zipper stabilizes the pentameric membrane domain of phospholamban and forms a coiled-coil pore structure
    • Simmerman, H. K. B., Kobayashi, Y. M., Autry, J. M., and Jones, L. R. (1996) A leucine zipper stabilizes the pentameric membrane domain of phospholamban and forms a coiled-coil pore structure. J. Biol. Chem. 271, 5941-5946.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5941-5946
    • Simmerman, H.K.B.1    Kobayashi, Y.M.2    Autry, J.M.3    Jones, L.R.4
  • 57
    • 17144362921 scopus 로고    scopus 로고
    • X-ray structure of a water-soluble analog of the membrane protein phospholamban: Sequence determinants defining the topology of tetrameric and pentameric coiled coils
    • Slovic, A. M., Stayrook, S. E., North, B., and DeGrado, W. F. (2005) X-ray structure of a water-soluble analog of the membrane protein phospholamban: Sequence determinants defining the topology of tetrameric and pentameric coiled coils. J. Mol. Biol. 348, 777-787.
    • (2005) J. Mol. Biol. , vol.348 , pp. 777-787
    • Slovic, A.M.1    Stayrook, S.E.2    North, B.3    Degrado, W.F.4
  • 59
    • 31744435118 scopus 로고    scopus 로고
    • Tuning the erosion rate of artificial protein hydrogels through control of network topology
    • Shen, W., Zhang, K. C., Kornfield, J. A., and Tirrell, D. A. (2006) Tuning the erosion rate of artificial protein hydrogels through control of network topology. Nat. Mater. 5, 153-158.
    • (2006) Nat. Mater. , vol.5 , pp. 153-158
    • Shen, W.1    Zhang, K.C.2    Kornfield, J.A.3    Tirrell, D.A.4
  • 61
    • 33751421457 scopus 로고    scopus 로고
    • Peptide-based fibrous biomaterials: Some things old, new and borrowed
    • Woolfson, D. N., and Ryadnov, M. G. (2006) Peptide-based fibrous biomaterials: Some things old, new and borrowed. Curr. Opin. Chem. Biol. 10, 559-567.
    • (2006) Curr. Opin. Chem. Biol. , vol.10 , pp. 559-567
    • Woolfson, D.N.1    Ryadnov, M.G.2
  • 62
    • 70149103008 scopus 로고    scopus 로고
    • Designing nano-to-micron scale peptide-based self-assembling systems from the bottom up
    • Woolfson, D., Pandya, M., Ryadnov, M., and Smith, A. (2005) Designing nano-to-micron scale peptide-based self-assembling systems from the bottom up. Biopolymers 80, 493-493
    • (2005) Biopolymers , vol.80 , pp. 493-493
    • Woolfson, D.1    Pandya, M.2    Ryadnov, M.3    Smith, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.