메뉴 건너뛰기




Volumn 5, Issue 7, 1999, Pages 313-322

Assembly of binding loops on aromatic templates as VCAM-1 mimetics

Author keywords

Chemoselective ligation; Constrained cyclic peptides; Drug design; Template assembly; VCAM 1 mimetics

Indexed keywords

BENZYL DERIVATIVE; BETA1 INTEGRIN; BIPHENYL; INTEGRIN; NAPHTHALENE; OXIME; VASCULAR CELL ADHESION MOLECULE 1;

EID: 0032794902     PISSN: 10752617     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1099-1387(199907)5:7<313::AID-PSC200>3.0.CO;2-F     Document Type: Article
Times cited : (7)

References (39)
  • 1
    • 0031434205 scopus 로고    scopus 로고
    • Non-native architectures in protein design and mimicry
    • Mutter M, Tuchscherer G. Non-native architectures in protein design and mimicry. Cell Mol Life Sci 1997; 53: 851-863.
    • (1997) Cell Mol Life Sci , vol.53 , pp. 851-863
    • Mutter, M.1    Tuchscherer, G.2
  • 3
    • 0032144119 scopus 로고    scopus 로고
    • Functionalization of designed folded polypeptides
    • Baltzer L. Functionalization of designed folded polypeptides. Curr Opinion Struct Biol 1998; 8: 466-470.
    • (1998) Curr Opinion Struct Biol , vol.8 , pp. 466-470
    • Baltzer, L.1
  • 4
    • 0032578392 scopus 로고    scopus 로고
    • Modular synthesis of de novo designed metalloproteins for light-induced electron transfer
    • Rau HK, Dejonge N, Haehnel W. Modular synthesis of de novo designed metalloproteins for light-induced electron transfer. Proc Natl Acad Sci USA 1998; 95: 11526-11531.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 11526-11531
    • Rau, H.K.1    Dejonge, N.2    Haehnel, W.3
  • 5
    • 0031902085 scopus 로고    scopus 로고
    • Protein design: On the threshold of functional properties
    • Tuchscherer G, Schleibler L, Dumy P, Mutter M. Protein design: on the threshold of functional properties. Biopolymers 1998; 47: 63-73.
    • (1998) Biopolymers , vol.47 , pp. 63-73
    • Tuchscherer, G.1    Schleibler, L.2    Dumy, P.3    Mutter, M.4
  • 6
    • 0029904435 scopus 로고    scopus 로고
    • Minimizing a binding domain from protein A
    • Braisted AC, Wells JA. Minimizing a binding domain from protein A. Proc Natl Acad Sci USA 1996; 93: 5688-5692.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 5688-5692
    • Braisted, A.C.1    Wells, J.A.2
  • 8
    • 0030567375 scopus 로고    scopus 로고
    • Economy in protein design: Evolution of a metal-independent motif based on the zinc finger domains
    • Struthers MD, Cheng RP, Imperiali B. Economy in protein design: evolution of a metal-independent motif based on the zinc finger domains. J Am Chem Soc 1996; 118: 3073-3081.
    • (1996) J Am Chem Soc , vol.118 , pp. 3073-3081
    • Struthers, M.D.1    Cheng, R.P.2    Imperiali, B.3
  • 10
  • 11
    • 0030822252 scopus 로고    scopus 로고
    • Scaffolds for engineering novel binding sites in proteins
    • Nygren PA, Uhlen M. Scaffolds for engineering novel binding sites in proteins. Curr Opinion Struct Biol 1997; 7: 463-469.
    • (1997) Curr Opinion Struct Biol , vol.7 , pp. 463-469
    • Nygren, P.A.1    Uhlen, M.2
  • 12
    • 0029050766 scopus 로고
    • Scorpion toxins as natural scaffolds for protein engineering
    • Vita C, Roumestand C, Toma F, Menez A. Scorpion toxins as natural scaffolds for protein engineering. Proc Natl Acad Sci USA 1995; 92: 6404-6408.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 6404-6408
    • Vita, C.1    Roumestand, C.2    Toma, F.3    Menez, A.4
  • 13
    • 0030047220 scopus 로고    scopus 로고
    • Functionalized protein-like structures from conformationally defined synthetic combinatorial libraries
    • Perez-Paya E, Houghten RA, Blondelle SE. Functionalized protein-like structures from conformationally defined synthetic combinatorial libraries. J Biol Chem 1996; 271: 4120-4126.
    • (1996) J Biol Chem , vol.271 , pp. 4120-4126
    • Perez-Paya, E.1    Houghten, R.A.2    Blondelle, S.E.3
  • 14
    • 0030595361 scopus 로고    scopus 로고
    • Use of a conformationally restricted secondary structural element to display peptide libraries: A two stranded alpha helical coiled-coil stabilized by lactam bridges
    • Houston ME, Wallace A, Bianchi E, Pessi A, Hodges RS. Use of a conformationally restricted secondary structural element to display peptide libraries: a two stranded alpha helical coiled-coil stabilized by lactam bridges. J Mol Biol 1996; 262: 270-282.
    • (1996) J Mol Biol , vol.262 , pp. 270-282
    • Houston, M.E.1    Wallace, A.2    Bianchi, E.3    Pessi, A.4    Hodges, R.S.5
  • 15
    • 0024665396 scopus 로고
    • A chemical approach to protein design: Template Assembled Synthetic Proteins (TASP)
    • Mutter M, Vuilleumier S. A chemical approach to protein design: Template Assembled Synthetic Proteins (TASP). Angew Chem Int Ed Engl 1989; 28: 535-554.
    • (1989) Angew Chem Int Ed Engl , vol.28 , pp. 535-554
    • Mutter, M.1    Vuilleumier, S.2
  • 18
    • 85044015679 scopus 로고
    • Topological templates as tool in molecular recognition and peptide mimicry: Synthesis of a TASK library
    • Sila U, Mutter M. Topological templates as tool in molecular recognition and peptide mimicry: Synthesis of a TASK library. J Mol Recognition 1995; 8: 2934.
    • (1995) J Mol Recognition , vol.8 , pp. 2934
    • Sila, U.1    Mutter, M.2
  • 19
    • 0029907747 scopus 로고    scopus 로고
    • Protein-loop mimetics: A diketopiperazine-based template to stabilize loop conformations in cyclic peptides containing the NPNa and RGD motifs
    • Bisang C, Weber C, Robinson JA. Protein-loop mimetics: a diketopiperazine-based template to stabilize loop conformations in cyclic peptides containing the NPNA and RGD motifs. Helv Chim Acta 1996; 79: 1825-1842.
    • (1996) Helv Chim Acta , vol.79 , pp. 1825-1842
    • Bisang, C.1    Weber, C.2    Robinson, J.A.3
  • 20
    • 0029856490 scopus 로고    scopus 로고
    • A tricyclic template derived from (2S,4R)-4-hydroxyproline for the synthesis of protein loop mimetics
    • Beeli R, Steger M, Linden A, Robinson JA. A tricyclic template derived from (2S,4R)-4-hydroxyproline for the synthesis of protein loop mimetics. Helv Chim Acta 1996; 79: 2235-2248.
    • (1996) Helv Chim Acta , vol.79 , pp. 2235-2248
    • Beeli, R.1    Steger, M.2    Linden, A.3    Robinson, J.A.4
  • 21
    • 0002426257 scopus 로고    scopus 로고
    • A template for the solid-phase synthesis of conformationally restricted protein loop mimetics
    • Emery F, Bisang C, Favre M, Jiang L, Robinson JA. A template for the solid-phase synthesis of conformationally restricted protein loop mimetics. Chem Commun 1996; 2155-2156.
    • (1996) Chem Commun , pp. 2155-2156
    • Emery, F.1    Bisang, C.2    Favre, M.3    Jiang, L.4    Robinson, J.A.5
  • 22
    • 0025232814 scopus 로고
    • Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids
    • Fields GB, Noble RL. Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids. Int J Pept Protein Res 1990; 35: 161-214.
    • (1990) Int J Pept Protein Res , vol.35 , pp. 161-214
    • Fields, G.B.1    Noble, R.L.2
  • 23
    • 0038590584 scopus 로고
    • Continuous flow methods in organic synthesis
    • Sheppard RC. Continuous flow methods in organic synthesis. Chem Brit 1983; 402.
    • (1983) Chem Brit , pp. 402
    • Sheppard, R.C.1
  • 24
    • 0018085515 scopus 로고
    • Solid-phase peptide synthesis using mild base cleavage of Ncursive Greek chi-fluorenylmethyloxy-carbonylamino acids, exemplified by a synthesis of dihydrosomatostatin
    • Chang CD, Meienhofer J. Solid-phase peptide synthesis using mild base cleavage of Ncursive Greek chi-fluorenylmethyloxy-carbonylamino acids, exemplified by a synthesis of dihydrosomatostatin. Int J Pept Protein Res 1978; 11: 246-249.
    • (1978) Int J Pept Protein Res , vol.11 , pp. 246-249
    • Chang, C.D.1    Meienhofer, J.2
  • 25
    • 0030657857 scopus 로고    scopus 로고
    • Use of Alloc-amino acids in solid-phase peptide synthesis-tandem deprotection-coupling reactions using neutral conditions
    • Thieret N, Alsina J, Giralt E, Guibé F, Albericio F. Use of Alloc-amino acids in solid-phase peptide synthesis-tandem deprotection-coupling reactions using neutral conditions. Tetrahedron Lett 1997; 41: 7275-7278.
    • (1997) Tetrahedron Lett , vol.41 , pp. 7275-7278
    • Thieret, N.1    Alsina, J.2    Giralt, E.3    Guibé, F.4    Albericio, F.5
  • 26
    • 0026641501 scopus 로고
    • Regio-chemical control in the oxidative coupling of metal phenolates: Highly selective synthesis of symmetric, hydroxylated biaryls
    • Sartori G, Maggi R, Bigi F, Arienti A, Casnati G. Regio-chemical control in the oxidative coupling of metal phenolates: highly selective synthesis of symmetric, hydroxylated biaryls. Tetrahedron 1992; 48: 9483.
    • (1992) Tetrahedron , vol.48 , pp. 9483
    • Sartori, G.1    Maggi, R.2    Bigi, F.3    Arienti, A.4    Casnati, G.5
  • 29
    • 0028208244 scopus 로고
    • Residues within a conserved amino acid motif of domains 1 and 4 of VCAM-1 are required for binding to VLA-4
    • Vonderheide RH, Tedder TF, Springer TA, Staunton DE. Residues within a conserved amino acid motif of domains 1 and 4 of VCAM-1 are required for binding to VLA-4. J Cell Biol 1994; 125: 215-222.
    • (1994) J Cell Biol , vol.125 , pp. 215-222
    • Vonderheide, R.H.1    Tedder, T.F.2    Springer, T.A.3    Staunton, D.E.4
  • 31
    • 0029379848 scopus 로고
    • Ideas crystallized on immunoglobulin superfamily-integrin interactions
    • De Fougerolles A, Springer TA. Ideas crystallized on immunoglobulin superfamily-integrin interactions. Curr Biol 1995; 2: 639-643.
    • (1995) Curr Biol , vol.2 , pp. 639-643
    • De Fougerolles, A.1    Springer, T.A.2
  • 33
    • 0029046132 scopus 로고
    • The crystal structure of an N-terminal two-domain fragment of VCAM-1: A cyclic peptide based on the domain 1 CD-loop can inhibit VCAM-1/cursive Greek chi4 integrin interaction
    • Wang JH, Pepinsky RB, Stehle T, Liu JH, Karpusas M, Browning B, Osborn N. The crystal structure of an N-terminal two-domain fragment of VCAM-1: a cyclic peptide based on the domain 1 CD-loop can inhibit VCAM-1/cursive Greek chi4 integrin interaction. Proc Natl Acad Sci USA 1995; 92: 5714-5718.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5714-5718
    • Wang, J.H.1    Pepinsky, R.B.2    Stehle, T.3    Liu, J.H.4    Karpusas, M.5    Browning, B.6    Osborn, N.7
  • 34
    • 0028231302 scopus 로고
    • Facile synthesis of homogeneous artificial proteins
    • Rose K. Facile synthesis of homogeneous artificial proteins. J Am Chem Soc 1994; 116: 30.
    • (1994) J Am Chem Soc , vol.116 , pp. 30
    • Rose, K.1
  • 35
    • 0029847275 scopus 로고    scopus 로고
    • Comparative total syntheses of turkey ovomucold third domain by both stepwise solid phase synthesis and native chemical ligation
    • Lu W, Qasim MA, Kent SBH. Comparative total syntheses of turkey ovomucold third domain by both stepwise solid phase synthesis and native chemical ligation. J Am Chem Soc 1996; 118: 8518-8523.
    • (1996) J Am Chem Soc , vol.118 , pp. 8518-8523
    • Lu, W.1    Qasim, M.A.2    Kent, S.B.H.3
  • 36
    • 0027756777 scopus 로고
    • Template assembled synthetic proteins: Condensation of a multifunctional peptide to a topological template via chemoselective ligation
    • Tuchscherer G. Template assembled synthetic proteins: condensation of a multifunctional peptide to a topological template via chemoselective ligation. Tetrahedron Lett 1993; 34: 8419.
    • (1993) Tetrahedron Lett , vol.34 , pp. 8419
    • Tuchscherer, G.1
  • 37
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation and signaling in cell adhesion
    • Hynes RO. Integrins: versatility, modulation and signaling in cell adhesion. Cell 1992; 69: 11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 38
    • 0027982876 scopus 로고
    • Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm
    • Springer TA. Traffic signals for lymphocyte recirculation and leukocyte emigration: the multistep paradigm. Cell 1994; 76: 301-314.
    • (1994) Cell , vol.76 , pp. 301-314
    • Springer, T.A.1
  • 39
    • 0026574125 scopus 로고
    • Role of integrin alpha 4 beta 7/alpha 4 beta P inlymphocyte adherence to fibronectin and VCAM-1 and in homotypic cell clustering
    • Ruegg C, Postigo AA, Sikorski EE, Butcher EC, Pytela R, Erle DJ. Role of integrin alpha 4 beta 7/alpha 4 beta P inlymphocyte adherence to fibronectin and VCAM-1 and in homotypic cell clustering. J Cell Biol 1992; 117: 179-189.
    • (1992) J Cell Biol , vol.117 , pp. 179-189
    • Ruegg, C.1    Postigo, A.A.2    Sikorski, E.E.3    Butcher, E.C.4    Pytela, R.5    Erle, D.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.