메뉴 건너뛰기




Volumn 8, Issue 5, 2008, Pages 609-615

Display scaffolds: protein engineering for novel therapeutics

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; CD23 ANTIGEN; CD8 ANTIGEN; CELL ADHESION MOLECULE; CYTOTOXIC T LYMPHOCYTE ANTIGEN 4; EPIDERMAL GROWTH FACTOR RECEPTOR 2; FIBRONECTIN; IMMUNOGLOBULIN HEAVY CHAIN; IMMUNOGLOBULIN LIGHT CHAIN; INTERLEUKIN 2 RECEPTOR; INTERLEUKIN 6; LIPOSOME; LYMPHOCYTE RECEPTOR; MONOCLONAL ANTIBODY; NANOCAPSULE; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY; T LYMPHOCYTE RECEPTOR; TGN 1412; VASCULOTROPIN; VASCULOTROPIN RECEPTOR;

EID: 54849406976     PISSN: 14714892     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.coph.2008.06.007     Document Type: Review
Times cited : (58)

References (52)
  • 1
    • 33751347582 scopus 로고    scopus 로고
    • Biopharmaceutical drug discovery using novel protein scaffolds
    • Gill D.S., and Damle N.K. Biopharmaceutical drug discovery using novel protein scaffolds. Curr Opin Biotechnol 17 (2006) 653-658
    • (2006) Curr Opin Biotechnol , vol.17 , pp. 653-658
    • Gill, D.S.1    Damle, N.K.2
  • 2
    • 33845921119 scopus 로고    scopus 로고
    • Proteomebinders: planning a European resource of affinity reagents for analysis of the human proteome
    • Co-ordinated attempt by European consortium to establish an extensive resource of well-characterised affinity reagents. This article describes selection strategies and scaffold binders, with an emphasis on high throughput requirements for targets identified by analysis of the human proteome.
    • Taussig M.J., Stoevesandt O., Borrebaeck C.A., Bradbury A.R., Cahill D., Cambillau C., de Daruvar A., Dubel S., Eichler J., Frank R., et al. Proteomebinders: planning a European resource of affinity reagents for analysis of the human proteome. Nat Methods 4 (2007) 13-17. Co-ordinated attempt by European consortium to establish an extensive resource of well-characterised affinity reagents. This article describes selection strategies and scaffold binders, with an emphasis on high throughput requirements for targets identified by analysis of the human proteome.
    • (2007) Nat Methods , vol.4 , pp. 13-17
    • Taussig, M.J.1    Stoevesandt, O.2    Borrebaeck, C.A.3    Bradbury, A.R.4    Cahill, D.5    Cambillau, C.6    de Daruvar, A.7    Dubel, S.8    Eichler, J.9    Frank, R.10
  • 3
    • 34548522063 scopus 로고    scopus 로고
    • Alternative non-antibody scaffolds for molecular recognition
    • Skerra A. Alternative non-antibody scaffolds for molecular recognition. Curr Opin Biotechnol 18 (2007) 295-304
    • (2007) Curr Opin Biotechnol , vol.18 , pp. 295-304
    • Skerra, A.1
  • 4
    • 30344484440 scopus 로고    scopus 로고
    • Antibody engineering for the development of therapeutic antibodies
    • Kim S.J., Park Y., and Hong H.J. Antibody engineering for the development of therapeutic antibodies. Mol Cells 20 (2005) 17-29
    • (2005) Mol Cells , vol.20 , pp. 17-29
    • Kim, S.J.1    Park, Y.2    Hong, H.J.3
  • 5
    • 32344448382 scopus 로고    scopus 로고
    • Screening for peptide drugs from the natural repertoire of biodiverse protein folds
    • Watt P.M. Screening for peptide drugs from the natural repertoire of biodiverse protein folds. Nat Biotechnol 24 (2006) 177-183
    • (2006) Nat Biotechnol , vol.24 , pp. 177-183
    • Watt, P.M.1
  • 6
    • 27144511241 scopus 로고    scopus 로고
    • Engineering novel binding proteins from nonimmunoglobulin domains
    • Comprehensive scaffold review that, while published in 2005, is an ideal introduction to the diversity of alternative scaffolds and the rationale behind their design and study.
    • Binz H.K., Amstutz P., and Pluckthun A. Engineering novel binding proteins from nonimmunoglobulin domains. Nat Biotechnol 23 (2005) 1257-1268. Comprehensive scaffold review that, while published in 2005, is an ideal introduction to the diversity of alternative scaffolds and the rationale behind their design and study.
    • (2005) Nat Biotechnol , vol.23 , pp. 1257-1268
    • Binz, H.K.1    Amstutz, P.2    Pluckthun, A.3
  • 7
    • 24944450680 scopus 로고    scopus 로고
    • Artificial, non-antibody binding proteins for pharmaceutical and industrial applications
    • Hey T., Fiedler E., Rudolph R., and Fiedler M. Artificial, non-antibody binding proteins for pharmaceutical and industrial applications. Trends Biotechnol 23 (2005) 514-522
    • (2005) Trends Biotechnol , vol.23 , pp. 514-522
    • Hey, T.1    Fiedler, E.2    Rudolph, R.3    Fiedler, M.4
  • 8
    • 41249087476 scopus 로고    scopus 로고
    • Comprehensive analysis of the factors contributing to the stability and solubility of autonomous human VH domains
    • HH domains, and thus, could not have been identified by analysis of natural sequences and structures..."-a comment possibly with half an eye on the intellectual property landscape.
    • HH domains, and thus, could not have been identified by analysis of natural sequences and structures..."-a comment possibly with half an eye on the intellectual property landscape.
    • (2008) J Biol Chem , vol.283 , pp. 3639-3654
    • Barthelemy, P.A.1    Raab, H.2    Appleton, B.A.3    Bond, C.J.4    Wu, P.5    Wiesmann, C.6    Sidhu, S.S.7
  • 10
    • 34547742068 scopus 로고    scopus 로고
    • Small antibody mimetics comprising two complementarity-determining regions and a framework region for tumor targeting
    • This article reports a novel approach to reduction of the antibody Fv, by linking CDRs from adjacent domains through a single framework region. Importantly, when linked to the toxin colicin Ia to produce 'pheromonicins' these constructs exhibited targeted inhibition of tumour growth. Questions remain, for example immunogenicity of such protein, but an innovative and promising approach.
    • Qiu X.Q., Wang H., Cai B., Wang L.L., and Yue S.T. Small antibody mimetics comprising two complementarity-determining regions and a framework region for tumor targeting. Nat Biotechnol 25 (2007) 921-929. This article reports a novel approach to reduction of the antibody Fv, by linking CDRs from adjacent domains through a single framework region. Importantly, when linked to the toxin colicin Ia to produce 'pheromonicins' these constructs exhibited targeted inhibition of tumour growth. Questions remain, for example immunogenicity of such protein, but an innovative and promising approach.
    • (2007) Nat Biotechnol , vol.25 , pp. 921-929
    • Qiu, X.Q.1    Wang, H.2    Cai, B.3    Wang, L.L.4    Yue, S.T.5
  • 15
    • 38449104431 scopus 로고    scopus 로고
    • High-affinity TCRs generated by phage display provide CD4+ T cells with the ability to recognize and kill tumor cell lines
    • Zhao Y., Bennett A.D., Zheng Z., Wang Q.J., Robbins P.F., Yu L.Y., Li Y., Molloy P.E., Dunn S.M., Jakobsen B.K., et al. High-affinity TCRs generated by phage display provide CD4+ T cells with the ability to recognize and kill tumor cell lines. J Immunol 179 (2007) 5845-5854
    • (2007) J Immunol , vol.179 , pp. 5845-5854
    • Zhao, Y.1    Bennett, A.D.2    Zheng, Z.3    Wang, Q.J.4    Robbins, P.F.5    Yu, L.Y.6    Li, Y.7    Molloy, P.E.8    Dunn, S.M.9    Jakobsen, B.K.10
  • 16
    • 4344565797 scopus 로고    scopus 로고
    • Structural evidence for evolution of shark Ig new antigen receptor variable domain antibodies from a cell-surface receptor
    • Streltsov V.A., Varghese J.N., Carmichael J.A., Irving R.A., Hudson P.J., and Nuttall S.D. Structural evidence for evolution of shark Ig new antigen receptor variable domain antibodies from a cell-surface receptor. Proc Natl Acad Sci U S A 101 (2004) 12444-12449
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 12444-12449
    • Streltsov, V.A.1    Varghese, J.N.2    Carmichael, J.A.3    Irving, R.A.4    Hudson, P.J.5    Nuttall, S.D.6
  • 17
    • 34247098240 scopus 로고    scopus 로고
    • Evolution of an interloop disulfide bond in high-affinity antibody mimics based on fibronectin type III domain and selected by yeast surface display: molecular convergence with single-domain camelid and shark antibodies
    • Lipovsek D., Lippow S.M., Hackel B.J., Gregson M.W., Cheng P., Kapila A., and Wittrup K.D. Evolution of an interloop disulfide bond in high-affinity antibody mimics based on fibronectin type III domain and selected by yeast surface display: molecular convergence with single-domain camelid and shark antibodies. J Mol Biol 368 (2007) 1024-1041
    • (2007) J Mol Biol , vol.368 , pp. 1024-1041
    • Lipovsek, D.1    Lippow, S.M.2    Hackel, B.J.3    Gregson, M.W.4    Cheng, P.5    Kapila, A.6    Wittrup, K.D.7
  • 18
    • 34249852867 scopus 로고    scopus 로고
    • High-affinity single-domain binding proteins with a binary-code interface
    • Tyrosine residues are traditionally over-represented in antibody paratopes. This study asks whether binding-loops comprised only tyrosine and serine residues can generate sufficient conformational and interface diversity to effectively target antigen. The authors answer in the positive, and present a 'monobody'-maltose-binding protein co-crystallographic structure which shows dominant contributions of tyrosine residues and molecular mimicry of β-cyclodextrin, an MBP substrate. Food for thought for the molecular library generation community!
    • Koide A., Gilbreth R.N., Esaki K., Tereshko V., and Koide S. High-affinity single-domain binding proteins with a binary-code interface. Proc Natl Acad Sci U S A 104 (2007) 6632-6637. Tyrosine residues are traditionally over-represented in antibody paratopes. This study asks whether binding-loops comprised only tyrosine and serine residues can generate sufficient conformational and interface diversity to effectively target antigen. The authors answer in the positive, and present a 'monobody'-maltose-binding protein co-crystallographic structure which shows dominant contributions of tyrosine residues and molecular mimicry of β-cyclodextrin, an MBP substrate. Food for thought for the molecular library generation community!
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 6632-6637
    • Koide, A.1    Gilbreth, R.N.2    Esaki, K.3    Tereshko, V.4    Koide, S.5
  • 19
    • 43949138210 scopus 로고    scopus 로고
    • Alanine scanning mutagenesis of the prototypic cyclotide reveals a cluster of residues essential for bioactivity
    • Simonsen S.M., Sando L., Rosengren K.J., Wang C.K., Colgrave M.L., Daly N.L., and Craik D.J. Alanine scanning mutagenesis of the prototypic cyclotide reveals a cluster of residues essential for bioactivity. J Biol Chem 283 (2008) 9805-9813
    • (2008) J Biol Chem , vol.283 , pp. 9805-9813
    • Simonsen, S.M.1    Sando, L.2    Rosengren, K.J.3    Wang, C.K.4    Colgrave, M.L.5    Daly, N.L.6    Craik, D.J.7
  • 20
    • 42449136263 scopus 로고    scopus 로고
    • Designed TPR modules as novel anticancer agents
    • Cortajarena A.L., Yi F., and Regan L. Designed TPR modules as novel anticancer agents. ACS Chem Biol 3 (2008) 161-166
    • (2008) ACS Chem Biol , vol.3 , pp. 161-166
    • Cortajarena, A.L.1    Yi, F.2    Regan, L.3
  • 21
    • 34547958191 scopus 로고    scopus 로고
    • Selection and evolution of enzymes from a partially randomized non-catalytic scaffold
    • Another excellent paper from one of the pioneers in the protein display field. Selection technologies have always been a necessary component of any scaffold design system, and here the authors harness the combinatorial power of ribosome display in combination with a dual zinc finger-based scaffold library, to derive novel proteins that both bound their target and catalysed an RNA ligase enzymatic reaction.
    • Seelig B., and Szostak J.W. Selection and evolution of enzymes from a partially randomized non-catalytic scaffold. Nature 448 (2007) 828-831. Another excellent paper from one of the pioneers in the protein display field. Selection technologies have always been a necessary component of any scaffold design system, and here the authors harness the combinatorial power of ribosome display in combination with a dual zinc finger-based scaffold library, to derive novel proteins that both bound their target and catalysed an RNA ligase enzymatic reaction.
    • (2007) Nature , vol.448 , pp. 828-831
    • Seelig, B.1    Szostak, J.W.2
  • 22
    • 39149098445 scopus 로고    scopus 로고
    • Designed armadillo repeat proteins as general peptide-binding scaffolds: consensus design and computational optimization of the hydrophobic core
    • This laboratory has been at the forefront of scaffold design and selection system development for the past two decades. Libraries of this scaffold will be focussed squarely on isolation of peptide-specific binders.
    • Parmeggiani F., Pellarin R., Larsen A.P., Varadamsetty G., Stumpp M.T., Zerbe O., Caflisch A., and Pluckthun A. Designed armadillo repeat proteins as general peptide-binding scaffolds: consensus design and computational optimization of the hydrophobic core. J Mol Biol 376 (2008) 1282-1304. This laboratory has been at the forefront of scaffold design and selection system development for the past two decades. Libraries of this scaffold will be focussed squarely on isolation of peptide-specific binders.
    • (2008) J Mol Biol , vol.376 , pp. 1282-1304
    • Parmeggiani, F.1    Pellarin, R.2    Larsen, A.P.3    Varadamsetty, G.4    Stumpp, M.T.5    Zerbe, O.6    Caflisch, A.7    Pluckthun, A.8
  • 24
    • 41149134858 scopus 로고    scopus 로고
    • Structure and specificity of lamprey monoclonal antibodies
    • •]. It will be interesting to compare in vitro selection on the basis of large engineered VLR libraries, with in vivo selection from lamprey immunisation. Such comparative experiments have only been possible to date in immunoglobulin-based antibody systems (murine, camel and shark). It will be a true test of the ability of protein engineering to mimic in vivo selection in the alternative scaffold space, especially as VLRs are modular and amenable to affinity maturation through module shuffling as well as point mutation.
    • •]. It will be interesting to compare in vitro selection on the basis of large engineered VLR libraries, with in vivo selection from lamprey immunisation. Such comparative experiments have only been possible to date in immunoglobulin-based antibody systems (murine, camel and shark). It will be a true test of the ability of protein engineering to mimic in vivo selection in the alternative scaffold space, especially as VLRs are modular and amenable to affinity maturation through module shuffling as well as point mutation.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 2040-2045
    • Herrin, B.R.1    Alder, M.N.2    Roux, K.H.3    Sina, C.4    Ehrhardt, G.R.5    Boydston, J.A.6    Turnbough Jr., C.L.7    Cooper, M.D.8
  • 25
    • 39449124952 scopus 로고    scopus 로고
    • Antibody responses of variable lymphocyte receptors in the lamprey
    • After decades of searching for immunoglobulin-based antibodies in lampreys, it now appears that the adaptive arm of the immune response in these animals is mediated by modular leucine-rich repeat units.
    • Alder M.N., Herrin B.R., Sadlonova A., Stockard C.R., Grizzle W.E., Gartland L.A., Gartland G.L., Boydston J.A., Turnbough Jr. C.L., and Cooper M.D. Antibody responses of variable lymphocyte receptors in the lamprey. Nat Immunol 9 (2008) 319-327. After decades of searching for immunoglobulin-based antibodies in lampreys, it now appears that the adaptive arm of the immune response in these animals is mediated by modular leucine-rich repeat units.
    • (2008) Nat Immunol , vol.9 , pp. 319-327
    • Alder, M.N.1    Herrin, B.R.2    Sadlonova, A.3    Stockard, C.R.4    Grizzle, W.E.5    Gartland, L.A.6    Gartland, G.L.7    Boydston, J.A.8    Turnbough Jr., C.L.9    Cooper, M.D.10
  • 26
    • 34147174947 scopus 로고    scopus 로고
    • Pharma consolidates its grip on post-antibody landscape
    • Read this for an introduction to commercial interests operating in the scaffold space. See also reference [3].
    • Sheridan C. Pharma consolidates its grip on post-antibody landscape. Nat Biotechnol 25 (2007) 365-366. Read this for an introduction to commercial interests operating in the scaffold space. See also reference [3].
    • (2007) Nat Biotechnol , vol.25 , pp. 365-366
    • Sheridan, C.1
  • 27
    • 33646740974 scopus 로고    scopus 로고
    • Antagonists to human and mouse vascular endothelial growth factor receptor 2 generated by directed protein evolution in vitro
    • Getmanova E.V., Chen Y., Bloom L., Gokemeijer J., Shamah S., Warikoo V., Wang J., Ling V., and Sun L. Antagonists to human and mouse vascular endothelial growth factor receptor 2 generated by directed protein evolution in vitro. Chem Biol 13 (2006) 549-556
    • (2006) Chem Biol , vol.13 , pp. 549-556
    • Getmanova, E.V.1    Chen, Y.2    Bloom, L.3    Gokemeijer, J.4    Shamah, S.5    Warikoo, V.6    Wang, J.7    Ling, V.8    Sun, L.9
  • 30
    • 42449111198 scopus 로고    scopus 로고
    • Stabilization of a β-hairpin in monomeric Alzheimer's amyloid- β peptide inhibits amyloid formation
    • Hoyer W., Gronwall C., Jonsson A., Stahl S., and Hard T. Stabilization of a β-hairpin in monomeric Alzheimer's amyloid- β peptide inhibits amyloid formation. Proc Natl Acad Sci U S A (2008)
    • (2008) Proc Natl Acad Sci U S A
    • Hoyer, W.1    Gronwall, C.2    Jonsson, A.3    Stahl, S.4    Hard, T.5
  • 32
    • 42149121917 scopus 로고    scopus 로고
    • [(18)F]FBEM-Z(HER2:342) - Affibody molecule - a new molecular tracer for in vivo monitoring of HER2 expression by positron emission tomography
    • Kramer-Marek G., Kiesewetter D.O., Martiniova L., Jagoda E., Lee S.B., and Capala J. [(18)F]FBEM-Z(HER2:342) - Affibody molecule - a new molecular tracer for in vivo monitoring of HER2 expression by positron emission tomography. Eur J Nucl Med Mol Imaging 35 (2008) 1008-1018
    • (2008) Eur J Nucl Med Mol Imaging , vol.35 , pp. 1008-1018
    • Kramer-Marek, G.1    Kiesewetter, D.O.2    Martiniova, L.3    Jagoda, E.4    Lee, S.B.5    Capala, J.6
  • 34
    • 33847794292 scopus 로고    scopus 로고
    • Labelling chemistry and characterization of [90Y/177Lu]-DOTA-ZHER2:342-3 Affibody molecule, a candidate agent for locoregional treatment of urinary bladder carcinoma
    • Fortin M.A., Orlova A., Malmstrom P.U., and Tolmachev V. Labelling chemistry and characterization of [90Y/177Lu]-DOTA-ZHER2:342-3 Affibody molecule, a candidate agent for locoregional treatment of urinary bladder carcinoma. Int J Mol Med 19 (2007) 285-291
    • (2007) Int J Mol Med , vol.19 , pp. 285-291
    • Fortin, M.A.1    Orlova, A.2    Malmstrom, P.U.3    Tolmachev, V.4
  • 35
    • 33947516890 scopus 로고    scopus 로고
    • Comparison of benzoate- and dodecaborate-based linkers for attachment of radioiodine to HER2-targeting affibody ligand
    • Tran T., Orlova A., Sivaev I., Sandstrom M., and Tolmachev V. Comparison of benzoate- and dodecaborate-based linkers for attachment of radioiodine to HER2-targeting affibody ligand. Int J Mol Med 19 (2007) 485-493
    • (2007) Int J Mol Med , vol.19 , pp. 485-493
    • Tran, T.1    Orlova, A.2    Sivaev, I.3    Sandstrom, M.4    Tolmachev, V.5
  • 36
    • 37849014587 scopus 로고    scopus 로고
    • Modification of adenovirus capsid with a designed protein ligand yields a gene vector targeted to a major molecular marker of cancer
    • Belousova N., Mikheeva G., Gelovani J., and Krasnykh V. Modification of adenovirus capsid with a designed protein ligand yields a gene vector targeted to a major molecular marker of cancer. J Virol 82 (2008) 630-637
    • (2008) J Virol , vol.82 , pp. 630-637
    • Belousova, N.1    Mikheeva, G.2    Gelovani, J.3    Krasnykh, V.4
  • 39
    • 34547911739 scopus 로고    scopus 로고
    • Anticalins as alternative binding proteins for therapeutic use
    • Skerra A. Anticalins as alternative binding proteins for therapeutic use. Curr Opin Mol Ther 9 (2007) 336-344
    • (2007) Curr Opin Mol Ther , vol.9 , pp. 336-344
    • Skerra, A.1
  • 40
    • 0037449785 scopus 로고    scopus 로고
    • Inhibition of Tat-mediated transactivation and HIV-1 replication by human anti-hCyclinT1 intrabodies
    • Bai J., Sui J., Zhu R.Y., Tallarico A.S., Gennari F., Zhang D., and Marasco W.A. Inhibition of Tat-mediated transactivation and HIV-1 replication by human anti-hCyclinT1 intrabodies. J Biol Chem 278 (2003) 1433-1442
    • (2003) J Biol Chem , vol.278 , pp. 1433-1442
    • Bai, J.1    Sui, J.2    Zhu, R.Y.3    Tallarico, A.S.4    Gennari, F.5    Zhang, D.6    Marasco, W.A.7
  • 41
    • 39649109675 scopus 로고    scopus 로고
    • An scFv intrabody against the nonamyloid component of alpha-synuclein reduces intracellular aggregation and toxicity
    • Lynch S.M., Zhou C., and Messer A. An scFv intrabody against the nonamyloid component of alpha-synuclein reduces intracellular aggregation and toxicity. J Mol Biol 377 (2008) 136-147
    • (2008) J Mol Biol , vol.377 , pp. 136-147
    • Lynch, S.M.1    Zhou, C.2    Messer, A.3
  • 42
    • 12844260131 scopus 로고    scopus 로고
    • Trapping prion protein in the endoplasmic reticulum impairs PrPC maturation and prevents PrPSc accumulation
    • Cardinale A., Filesi I., Vetrugno V., Pocchiari M., Sy M.S., and Biocca S. Trapping prion protein in the endoplasmic reticulum impairs PrPC maturation and prevents PrPSc accumulation. J Biol Chem 280 (2005) 685-694
    • (2005) J Biol Chem , vol.280 , pp. 685-694
    • Cardinale, A.1    Filesi, I.2    Vetrugno, V.3    Pocchiari, M.4    Sy, M.S.5    Biocca, S.6
  • 43
    • 35548937288 scopus 로고    scopus 로고
    • A protein silencing switch by ligand-induced proteasome-targeting intrabodies
    • Melchionna T., and Cattaneo A. A protein silencing switch by ligand-induced proteasome-targeting intrabodies. J Mol Biol 374 (2007) 641-654
    • (2007) J Mol Biol , vol.374 , pp. 641-654
    • Melchionna, T.1    Cattaneo, A.2
  • 44
    • 34249804141 scopus 로고    scopus 로고
    • Protein i: interference at protein level by intrabodies
    • The authors explore the function of intrabodies and the concept of protein interference (protein i), presenting a comprehensive overview of intrabody development and selection technologies. They review current intrabodies, their therapeutic applications and the limitations and challenges affecting intrabody delivery.
    • Manikandan J., Pushparaj P.N., and Melendez A.J. Protein i: interference at protein level by intrabodies. Front Biosci 12 (2007) 1344-1352. The authors explore the function of intrabodies and the concept of protein interference (protein i), presenting a comprehensive overview of intrabody development and selection technologies. They review current intrabodies, their therapeutic applications and the limitations and challenges affecting intrabody delivery.
    • (2007) Front Biosci , vol.12 , pp. 1344-1352
    • Manikandan, J.1    Pushparaj, P.N.2    Melendez, A.J.3
  • 45
    • 33947315300 scopus 로고    scopus 로고
    • Blocking translocation of cell surface molecules from the ER to the cell surface by intracellular antibodies targeted to the ER
    • This article explores the function of intracellular antibodies that inhibit target protein function through retention in the endoplasmic reticulum and explains the ER processing and degradation cycle. The author has collated a comprehensive list of therapeutic intrabodies utilising ER retention function and discusses the development of intrabodies in terms of delivery mechanisms and functionality in vivo.
    • Boldicke T. Blocking translocation of cell surface molecules from the ER to the cell surface by intracellular antibodies targeted to the ER. J Cell Mol Med 11 (2007) 54-70. This article explores the function of intracellular antibodies that inhibit target protein function through retention in the endoplasmic reticulum and explains the ER processing and degradation cycle. The author has collated a comprehensive list of therapeutic intrabodies utilising ER retention function and discusses the development of intrabodies in terms of delivery mechanisms and functionality in vivo.
    • (2007) J Cell Mol Med , vol.11 , pp. 54-70
    • Boldicke, T.1
  • 46
    • 17044398110 scopus 로고    scopus 로고
    • Making cell-permeable antibodies (transbody) through fusion of protein transduction domains (PTD) with single chain variable fragment (scFv) antibodies: potential advantages over antibodies expressed within the intracellular environment (intrabody)
    • Heng B.C., and Cao T. Making cell-permeable antibodies (transbody) through fusion of protein transduction domains (PTD) with single chain variable fragment (scFv) antibodies: potential advantages over antibodies expressed within the intracellular environment (intrabody). Med Hypotheses 64 (2005) 1105-1108
    • (2005) Med Hypotheses , vol.64 , pp. 1105-1108
    • Heng, B.C.1    Cao, T.2
  • 47
    • 41849116016 scopus 로고    scopus 로고
    • The calm after the cytokine storm: lessons from the TGN1412 trial
    • St Clair E.W. The calm after the cytokine storm: lessons from the TGN1412 trial. J Clin Invest (2008)
    • (2008) J Clin Invest
    • St Clair, E.W.1
  • 48
    • 34247853300 scopus 로고    scopus 로고
    • The Northwick Park tragedy-protecting healthy volunteers in future first-in-man trials
    • An excellent description of what went wrong during the TGN1412 clinical trials, and safeguards being developed to prevent a recurrence. Sobering analysis that will leave researchers asking whether their protein scaffold or immunotherapeutic has a novel mode of action and capacity to modify the body's immune system.
    • Dowsing T., and Kendall M.J. The Northwick Park tragedy-protecting healthy volunteers in future first-in-man trials. J Clin Pharm Ther 32 (2007) 203-207. An excellent description of what went wrong during the TGN1412 clinical trials, and safeguards being developed to prevent a recurrence. Sobering analysis that will leave researchers asking whether their protein scaffold or immunotherapeutic has a novel mode of action and capacity to modify the body's immune system.
    • (2007) J Clin Pharm Ther , vol.32 , pp. 203-207
    • Dowsing, T.1    Kendall, M.J.2
  • 49
    • 34249042875 scopus 로고    scopus 로고
    • Prediction of immunogenicity for therapeutic proteins: state of the art
    • De Groot A.S., and Moise L. Prediction of immunogenicity for therapeutic proteins: state of the art. Curr Opin Drug Discov Devel 10 (2007) 332-340
    • (2007) Curr Opin Drug Discov Devel , vol.10 , pp. 332-340
    • De Groot, A.S.1    Moise, L.2
  • 50
    • 0036687614 scopus 로고    scopus 로고
    • Passive antibody administration (immediate immunity) as a specific defense against biological weapons
    • Casadevall A. Passive antibody administration (immediate immunity) as a specific defense against biological weapons. Emerg Infect Dis 8 (2002) 833-841
    • (2002) Emerg Infect Dis , vol.8 , pp. 833-841
    • Casadevall, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.