메뉴 건너뛰기




Volumn 5, Issue 1, 2013, Pages 87-95

In situ click chemistry: From small molecule discovery to synthetic antibodies

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; ARTIFICIAL RECEPTOR;

EID: 84871759698     PISSN: 17579694     EISSN: 17579708     Source Type: Journal    
DOI: 10.1039/c2ib20110k     Document Type: Article
Times cited : (39)

References (51)
  • 1
    • 57349094892 scopus 로고    scopus 로고
    • Rapid characterization of binding specificity and cross-reactivity of antibodies using recombinant human protein arrays
    • G. Kijanka S. IpCho S. Baars H. Chen K. Hadley A. Beveridge E. Gould D. Murphy Rapid characterization of binding specificity and cross-reactivity of antibodies using recombinant human protein arrays J. Immunol. Methods 2009 340 2 132 137
    • (2009) J. Immunol. Methods , vol.340 , Issue.2 , pp. 132-137
    • Kijanka, G.1    Ipcho, S.2    Baars, S.3    Chen, H.4    Hadley, K.5    Beveridge, A.6    Gould, E.7    Murphy, D.8
  • 3
    • 0027971497 scopus 로고
    • Three-dimensional structures of the free and the antigen-complexed Fab from monoclonal anti-lysozyme antibody D44.1
    • B. C. Braden H. Souchon J.-L. Eiselé G. A. Bentley T. N. Bhat J. Navaza R. J. Poljak Three-dimensional structures of the free and the antigen-complexed Fab from monoclonal anti-lysozyme antibody D44.1 J. Mol. Biol. 1994 243 4 767 781
    • (1994) J. Mol. Biol. , vol.243 , Issue.4 , pp. 767-781
    • Braden, B.C.1    Souchon, H.2    Eiselé, J.-L.3    Bentley, G.A.4    Bhat, T.N.5    Navaza, J.6    Poljak, R.J.7
  • 5
    • 0034436049 scopus 로고    scopus 로고
    • Mutual Conformational Adaptations in Antigen and Antibody upon Complex Formation between an Fab and HIV-1 Capsid Protein p24
    • S. Monaco-Malbet C. Berthet-Colominas A. Novelli N. Battaï N. Piga V. Cheynet F. Mallet S. Cusack Mutual Conformational Adaptations in Antigen and Antibody upon Complex Formation between an Fab and HIV-1 Capsid Protein p24 Structure 2000 8 10 1069 1077
    • (2000) Structure , vol.8 , Issue.10 , pp. 1069-1077
    • Monaco-Malbet, S.1    Berthet-Colominas, C.2    Novelli, A.3    Battaï, N.4    Piga, N.5    Cheynet, V.6    Mallet, F.7    Cusack, S.8
  • 7
    • 78649876890 scopus 로고    scopus 로고
    • Synthetic receptors with antibody-like binding affinities
    • T. Kodadek Synthetic receptors with antibody-like binding affinities Curr. Opin. Chem. Biol. 2010 14 6 713 720
    • (2010) Curr. Opin. Chem. Biol. , vol.14 , Issue.6 , pp. 713-720
    • Kodadek, T.1
  • 8
    • 0032530717 scopus 로고    scopus 로고
    • VEGF and the Fab fragment of a humanized neutralizing antibody: Crystal structure of the complex at 2.4 Å resolution and mutational analysis of the interface
    • Y. A. Muller Y. Chen H. W. Christinger B. Li B. C. Cunningham H. B. Lowman A. M. de Vos VEGF and the Fab fragment of a humanized neutralizing antibody: crystal structure of the complex at 2.4 Å resolution and mutational analysis of the interface Structure (London) 1998 6 9 1153 1167
    • (1998) Structure (London) , vol.6 , Issue.9 , pp. 1153-1167
    • Muller, Y.A.1    Chen, Y.2    Christinger, H.W.3    Li, B.4    Cunningham, B.C.5    Lowman, H.B.6    De Vos, A.M.7
  • 9
    • 0025074907 scopus 로고
    • In vitro selection of RNA molecules that bind specific ligands
    • A. D. Ellington J. W. Szostak In vitro selection of RNA molecules that bind specific ligands Nature 1990 346 6287 818 822
    • (1990) Nature , vol.346 , Issue.6287 , pp. 818-822
    • Ellington, A.D.1    Szostak, J.W.2
  • 10
    • 0025112794 scopus 로고
    • Searching for peptide ligands with an epitope library
    • J. K. Scott G. P. Smith Searching for peptide ligands with an epitope library Science 1990 249 4967 386 390
    • (1990) Science , vol.249 , Issue.4967 , pp. 386-390
    • Scott, J.K.1    Smith, G.P.2
  • 11
    • 0030974119 scopus 로고    scopus 로고
    • In vitro selection and evolution of functional proteins by using ribosome display
    • J. Hanes A. Plückthun In vitro selection and evolution of functional proteins by using ribosome display Proc. Natl. Acad. Sci. U. S. A. 1997 94 10 4937 4942
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , Issue.10 , pp. 4937-4942
    • Hanes, J.1    Plückthun, A.2
  • 12
    • 0030817279 scopus 로고    scopus 로고
    • RNA-peptide fusions for the in vitro selection of peptides and proteins
    • R. W. Roberts J. W. Szostak RNA-peptide fusions for the in vitro selection of peptides and proteins Proc. Natl. Acad. Sci. U. S. A. 1997 94 23 12297 12302
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , Issue.23 , pp. 12297-12302
    • Roberts, R.W.1    Szostak, J.W.2
  • 13
    • 0030994634 scopus 로고    scopus 로고
    • Yeast surface display for screening combinatorial polypeptide libraries
    • E. T. Boder K. D. Wittrup Yeast surface display for screening combinatorial polypeptide libraries Nat. Biotechnol. 1997 15 6 553 557
    • (1997) Nat. Biotechnol. , vol.15 , Issue.6 , pp. 553-557
    • Boder, E.T.1    Wittrup, K.D.2
  • 14
    • 0026419328 scopus 로고
    • A new type of synthetic peptide library for identifying ligand-binding activity
    • K. S. Lam S. E. Salmon E. M. Hersh V. J. Hruby W. M. Kazmierski R. J. Knapp A new type of synthetic peptide library for identifying ligand-binding activity Nature 1991 354 6348 82 84
    • (1991) Nature , vol.354 , Issue.6348 , pp. 82-84
    • Lam, K.S.1    Salmon, S.E.2    Hersh, E.M.3    Hruby, V.J.4    Kazmierski, W.M.5    Knapp, R.J.6
  • 15
    • 0037087516 scopus 로고    scopus 로고
    • Click chemistry in situ: Acetylcholinesterase as a reaction vessel for the selective assembly of a femtomolar inhibitor from an array of building blocks
    • W. G. Lewis L. G. Green F. Grynszpan Z. Radic P. R. Carlier P. Taylor M. G. Finn K. B. Sharpless Click chemistry in situ: acetylcholinesterase as a reaction vessel for the selective assembly of a femtomolar inhibitor from an array of building blocks Angew. Chem., Int. Ed. 2002 41 6 1053 1057
    • (2002) Angew. Chem., Int. Ed. , vol.41 , Issue.6 , pp. 1053-1057
    • Lewis, W.G.1    Green, L.G.2    Grynszpan, F.3    Radic, Z.4    Carlier, P.R.5    Taylor, P.6    Finn, M.G.7    Sharpless, K.B.8
  • 16
    • 0019407381 scopus 로고
    • On the attribution and additivity of binding energies
    • W. P. Jencks On the attribution and additivity of binding energies Proc. Natl. Acad. Sci. U. S. A. 1981 78 7 4046 4050
    • (1981) Proc. Natl. Acad. Sci. U. S. A. , vol.78 , Issue.7 , pp. 4046-4050
    • Jencks, W.P.1
  • 21
    • 77949786732 scopus 로고    scopus 로고
    • In situ click chemistry: Probing the binding landscapes of biological molecules
    • S. K. Mamidyala M. G. Finn In situ click chemistry: probing the binding landscapes of biological molecules Chem. Soc. Rev. 2010 39 4 1252 1261
    • (2010) Chem. Soc. Rev. , vol.39 , Issue.4 , pp. 1252-1261
    • Mamidyala, S.K.1    Finn, M.G.2
  • 22
    • 0035918145 scopus 로고    scopus 로고
    • Generation of sequence-specific, high affinity anti-DNA antibodies
    • M. L. Cerutti J. M. Centeno F. A. Goldbaum G. de Prat-Gay Generation of sequence-specific, high affinity anti-DNA antibodies J. Biol. Chem. 2001 276 16 12769 12773
    • (2001) J. Biol. Chem. , vol.276 , Issue.16 , pp. 12769-12773
    • Cerutti, M.L.1    Centeno, J.M.2    Goldbaum, F.A.3    De Prat-Gay, G.4
  • 23
    • 0025321903 scopus 로고
    • Crystal structures of an antibody to a peptide and its complex with peptide antigen at 2.8 Å
    • R. L. Stanfield T. M. Fieser R. A. Lerner I. A. Wilson Crystal structures of an antibody to a peptide and its complex with peptide antigen at 2.8 Å Science 1990 248 4956 712 719
    • (1990) Science , vol.248 , Issue.4956 , pp. 712-719
    • Stanfield, R.L.1    Fieser, T.M.2    Lerner, R.A.3    Wilson, I.A.4
  • 24
    • 33646352962 scopus 로고    scopus 로고
    • Potent antibody therapeutics by design
    • P. J. Carter Potent antibody therapeutics by design Nat. Rev. Immunol. 2006 6 5 343 357
    • (2006) Nat. Rev. Immunol. , vol.6 , Issue.5 , pp. 343-357
    • Carter, P.J.1
  • 27
    • 0018346902 scopus 로고
    • Production of antibodies against phosphocholine, phosphatidylcholine, sphingomyelin, and lipid A by injection of liposomes containing lipid A
    • B. G. Schuster M. Neidig B. M. Alving C. R. Alving Production of antibodies against phosphocholine, phosphatidylcholine, sphingomyelin, and lipid A by injection of liposomes containing lipid A. J. Immunol. 1979 122 3 900 905
    • (1979) J. Immunol. , vol.122 , Issue.3 , pp. 900-905
    • Schuster, B.G.1    Neidig, M.2    Alving, B.M.3    Alving, C.R.4
  • 28
    • 77951235960 scopus 로고    scopus 로고
    • High affinity anti-inorganic material antibody generation by integrating graft and evolution technologies: Potential of antibodies as biointerface molecules
    • T. Hattori M. Umetsu T. Nakanishi T. Togashi N. Yokoo H. Abe S. Ohara T. Adschiri I. Kumagai High affinity anti-inorganic material antibody generation by integrating graft and evolution technologies: potential of antibodies as biointerface molecules J. Biol. Chem. 2010 285 10 7784 7793
    • (2010) J. Biol. Chem. , vol.285 , Issue.10 , pp. 7784-7793
    • Hattori, T.1    Umetsu, M.2    Nakanishi, T.3    Togashi, T.4    Yokoo, N.5    Abe, H.6    Ohara, S.7    Adschiri, T.8    Kumagai, I.9
  • 30
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • L. Lo Conte C. Chothia J. Janin The atomic structure of protein-protein recognition sites J. Mol. Biol. 1999 285 5 2177 2198
    • (1999) J. Mol. Biol. , vol.285 , Issue.5 , pp. 2177-2198
    • Lo Conte, L.1    Chothia, C.2    Janin, J.3
  • 31
    • 0032536197 scopus 로고    scopus 로고
    • Conformations of the third hypervariable region in the VH domain of immunoglobulins
    • V. Morea A. Tramontano M. Rustici C. Chothia A. M. Lesk Conformations of the third hypervariable region in the VH domain of immunoglobulins J. Mol. Biol. 1998 275 2 269 294
    • (1998) J. Mol. Biol. , vol.275 , Issue.2 , pp. 269-294
    • Morea, V.1    Tramontano, A.2    Rustici, M.3    Chothia, C.4    Lesk, A.M.5
  • 32
    • 0033711628 scopus 로고    scopus 로고
    • Diversity in the CDR3 region of V(H) is sufficient for most antibody specificities
    • J. L. Xu M. M. Davis Diversity in the CDR3 region of V(H) is sufficient for most antibody specificities Immunity 2000 13 1 37 45
    • (2000) Immunity , vol.13 , Issue.1 , pp. 37-45
    • Xu, J.L.1    Davis, M.M.2
  • 33
    • 0242551578 scopus 로고    scopus 로고
    • Expressed murine and human CDR-H3 intervals of equal length exhibit distinct repertoires that differ in their amino acid composition and predicted range of structures
    • M. Zemlin M. Klinger J. Link C. Zemlin K. Bauer J. A. Engler H. W. Schroeder, Jr. P. M. Kirkham Expressed murine and human CDR-H3 intervals of equal length exhibit distinct repertoires that differ in their amino acid composition and predicted range of structures J. Mol. Biol. 2003 334 4 733 749
    • (2003) J. Mol. Biol. , vol.334 , Issue.4 , pp. 733-749
    • Zemlin, M.1    Klinger, M.2    Link, J.3    Zemlin, C.4    Bauer, K.5    Engler, J.A.6    Schroeder, Jr.H.W.7    Kirkham, P.M.8
  • 35
    • 0035854724 scopus 로고    scopus 로고
    • Antigen Specificity and High Affinity Binding Provided by One Single Loop of a Camel Single-domain Antibody
    • A. Desmyter K. Decanniere S. Muyldermans L. Wyns Antigen Specificity and High Affinity Binding Provided by One Single Loop of a Camel Single-domain Antibody J. Biol. Chem. 2001 276 28 26285 26290
    • (2001) J. Biol. Chem. , vol.276 , Issue.28 , pp. 26285-26290
    • Desmyter, A.1    Decanniere, K.2    Muyldermans, S.3    Wyns, L.4
  • 37
    • 0033776083 scopus 로고    scopus 로고
    • Identification of novel prostate-specific antigen-binding peptides modulating its enzyme activity
    • P. Wu J. Leinonen E. Koivunen H. Lankinen U. H. Stenman Identification of novel prostate-specific antigen-binding peptides modulating its enzyme activity Eur. J. Biochem. 2000 267 20 6212 6220
    • (2000) Eur. J. Biochem. , vol.267 , Issue.20 , pp. 6212-6220
    • Wu, P.1    Leinonen, J.2    Koivunen, E.3    Lankinen, H.4    Stenman, U.H.5
  • 39
    • 33845364148 scopus 로고    scopus 로고
    • Fragment-based drug design: How big is too big?
    • P. J. Hajduk Fragment-based drug design: how big is too big? J. Med. Chem. 2006 49 24 6972 6976
    • (2006) J. Med. Chem. , vol.49 , Issue.24 , pp. 6972-6976
    • Hajduk, P.J.1
  • 40
    • 0037217406 scopus 로고    scopus 로고
    • Automated design of specificity in molecular recognition
    • J. J. Havranek P. B. Harbury Automated design of specificity in molecular recognition Nat. Struct. Biol. 2003 10 1 45 52
    • (2003) Nat. Struct. Biol. , vol.10 , Issue.1 , pp. 45-52
    • Havranek, J.J.1    Harbury, P.B.2
  • 41
    • 34247500390 scopus 로고    scopus 로고
    • Positive aspects of negative design: Simultaneous selection of specificity and interaction stability
    • J. M. Mason K. M. Muller K. M. Arndt Positive aspects of negative design: simultaneous selection of specificity and interaction stability Biochemistry 2007 46 16 4804 4814
    • (2007) Biochemistry , vol.46 , Issue.16 , pp. 4804-4814
    • Mason, J.M.1    Muller, K.M.2    Arndt, K.M.3
  • 42
    • 79957604998 scopus 로고    scopus 로고
    • A Conserved residue in the yeast Bem1p SH3 domain maintains the high level of binding specificity required for function
    • M. Gorelik K. Stanger A. R. Davidson A Conserved residue in the yeast Bem1p SH3 domain maintains the high level of binding specificity required for function J. Biol. Chem. 2011 286 22 19470 19477
    • (2011) J. Biol. Chem. , vol.286 , Issue.22 , pp. 19470-19477
    • Gorelik, M.1    Stanger, K.2    Davidson, A.R.3
  • 46
    • 7444243906 scopus 로고    scopus 로고
    • Destabilizing Universal Linkers for Signal Amplification in Self-Ligating Probes for RNA
    • H. Abe E. T. Kool Destabilizing Universal Linkers for Signal Amplification in Self-Ligating Probes for RNA J. Am. Chem. Soc. 2004 126 43 13980 13986
    • (2004) J. Am. Chem. Soc. , vol.126 , Issue.43 , pp. 13980-13986
    • Abe, H.1    Kool, E.T.2
  • 47
    • 33747878566 scopus 로고    scopus 로고
    • Reducing Product Inhibition in DNA-Template-Controlled Ligation Reactions
    • C. Dose S. Ficht O. Seitz Reducing Product Inhibition in DNA-Template-Controlled Ligation Reactions Angew. Chem., Int. Ed. 2006 45 32 5369 5373
    • (2006) Angew. Chem., Int. Ed. , vol.45 , Issue.32 , pp. 5369-5373
    • Dose, C.1    Ficht, S.2    Seitz, O.3
  • 48
    • 54349094314 scopus 로고    scopus 로고
    • Achieving Turnover in DNA-Templated Reactions
    • T. N. Grossmann A. Strohbach O. Seitz Achieving Turnover in DNA-Templated Reactions ChemBioChem 2008 9 14 2185 2192
    • (2008) ChemBioChem , vol.9 , Issue.14 , pp. 2185-2192
    • Grossmann, T.N.1    Strohbach, A.2    Seitz, O.3
  • 49
    • 80051581780 scopus 로고    scopus 로고
    • Small-molecule-dependent split aptamer ligation
    • A. K. Sharma J. M. Heemstra Small-molecule-dependent split aptamer ligation J. Am. Chem. Soc. 2011 133 32 12426 12429
    • (2011) J. Am. Chem. Soc. , vol.133 , Issue.32 , pp. 12426-12429
    • Sharma, A.K.1    Heemstra, J.M.2
  • 51
    • 18644384979 scopus 로고    scopus 로고
    • In situ selection of lead compounds by click chemistry: Target-guided optimization of acetylcholinesterase inhibitors
    • A. Krasinski Z. Radic R. Manetsch J. Raushel P. Taylor K. B. Sharpless H. C. Kolb In situ selection of lead compounds by click chemistry: target-guided optimization of acetylcholinesterase inhibitors J. Am. Chem. Soc. 2005 127 18 6686 6692
    • (2005) J. Am. Chem. Soc. , vol.127 , Issue.18 , pp. 6686-6692
    • Krasinski, A.1    Radic, Z.2    Manetsch, R.3    Raushel, J.4    Taylor, P.5    Sharpless, K.B.6    Kolb, H.C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.