-
1
-
-
33751347582
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
9
-
-
36849005918
-
Validation of a stable recombinant antibodies repertoire for the direct selection of functional intracellular reagents
-
Villani M.E., Di Carli M., Donini M., Traversini G., Lico C., Franconi R., Benvenuto E., and Desiderio A. Validation of a stable recombinant antibodies repertoire for the direct selection of functional intracellular reagents. J Immunol Methods 329 (2008) 11-20
-
(2008)
J Immunol Methods
, vol.329
, pp. 11-20
-
-
Villani, M.E.1
Di Carli, M.2
Donini, M.3
Traversini, G.4
Lico, C.5
Franconi, R.6
Benvenuto, E.7
Desiderio, A.8
-
10
-
-
34547742068
-
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
-
12
-
-
35748949254
-
Structure of an IgNAR-AMA1 complex: targeting a conserved hydrophobic cleft broadens malarial strain recognition
-
Henderson K.A., Streltsov V.A., Coley A.M., Dolezal O., Hudson P.J., Batchelor A.H., Gupta A., Bai T., Murphy V.J., Anders R.F., et al. Structure of an IgNAR-AMA1 complex: targeting a conserved hydrophobic cleft broadens malarial strain recognition. Structure 15 (2007) 1452-1466
-
(2007)
Structure
, vol.15
, pp. 1452-1466
-
-
Henderson, K.A.1
Streltsov, V.A.2
Coley, A.M.3
Dolezal, O.4
Hudson, P.J.5
Batchelor, A.H.6
Gupta, A.7
Bai, T.8
Murphy, V.J.9
Anders, R.F.10
-
13
-
-
33646545070
-
Experimental therapy of African trypanosomiasis with a nanobody-conjugated human trypanolytic factor
-
Baral T.N., Magez S., Stijlemans B., Conrath K., Vanhollebeke B., Pays E., Muyldermans S., and De Baetselier P. Experimental therapy of African trypanosomiasis with a nanobody-conjugated human trypanolytic factor. Nat Med 12 (2006) 580-584
-
(2006)
Nat Med
, vol.12
, pp. 580-584
-
-
Baral, T.N.1
Magez, S.2
Stijlemans, B.3
Conrath, K.4
Vanhollebeke, B.5
Pays, E.6
Muyldermans, S.7
De Baetselier, P.8
-
14
-
-
21444445173
-
Directed evolution of human T-cell receptors with picomolar affinities by phage display
-
Li Y., Moysey R., Molloy P.E., Vuidepot A.L., Mahon T., Baston E., Dunn S., Liddy N., Jacob J., Jakobsen B.K., et al. Directed evolution of human T-cell receptors with picomolar affinities by phage display. Nat Biotechnol 23 (2005) 349-354
-
(2005)
Nat Biotechnol
, vol.23
, pp. 349-354
-
-
Li, Y.1
Moysey, R.2
Molloy, P.E.3
Vuidepot, A.L.4
Mahon, T.5
Baston, E.6
Dunn, S.7
Liddy, N.8
Jacob, J.9
Jakobsen, B.K.10
-
15
-
-
38449104431
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
23
-
-
38049034890
-
Stabilizing ionic interactions in a full-consensus ankyrin repeat protein
-
Merz T., Wetzel S.K., Firbank S., Pluckthun A., Grutter M.G., and Mittl P.R. Stabilizing ionic interactions in a full-consensus ankyrin repeat protein. J Mol Biol 376 (2008) 232-240
-
(2008)
J Mol Biol
, vol.376
, pp. 232-240
-
-
Merz, T.1
Wetzel, S.K.2
Firbank, S.3
Pluckthun, A.4
Grutter, M.G.5
Mittl, P.R.6
-
24
-
-
41149134858
-
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
-
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
-
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
-
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
-
28
-
-
28644436100
-
Multivalent avimer proteins evolved by exon shuffling of a family of human receptor domains
-
Silverman J., Liu Q., Bakker A., To W., Duguay A., Alba B.M., Smith R., Rivas A., Li P., Le H., et al. Multivalent avimer proteins evolved by exon shuffling of a family of human receptor domains. Nat Biotechnol 23 (2005) 1556-1561
-
(2005)
Nat Biotechnol
, vol.23
, pp. 1556-1561
-
-
Silverman, J.1
Liu, Q.2
Bakker, A.3
To, W.4
Duguay, A.5
Alba, B.M.6
Smith, R.7
Rivas, A.8
Li, P.9
Le, H.10
-
29
-
-
34347380371
-
Phage display selection of Affibody molecules with specific binding to the extracellular domain of the epidermal growth factor receptor
-
Friedman M., Nordberg E., Hoiden-Guthenberg I., Brismar H., Adams G.P., Nilsson F.Y., Carlsson J., and Stahl S. Phage display selection of Affibody molecules with specific binding to the extracellular domain of the epidermal growth factor receptor. Protein Eng Des Sel 20 (2007) 189-199
-
(2007)
Protein Eng Des Sel
, vol.20
, pp. 189-199
-
-
Friedman, M.1
Nordberg, E.2
Hoiden-Guthenberg, I.3
Brismar, H.4
Adams, G.P.5
Nilsson, F.Y.6
Carlsson, J.7
Stahl, S.8
-
30
-
-
42449111198
-
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
-
31
-
-
44849128916
-
Generation of Affibody ligands binding the IL-2 receptor alpha
-
Gronwall C., Snelders E., Jarelov Palm A., Eriksson F., Herne N., and Stahl S. Generation of Affibody ligands binding the IL-2 receptor alpha. Biotechnol Appl Biochem 50 (2008) 97-112
-
(2008)
Biotechnol Appl Biochem
, vol.50
, pp. 97-112
-
-
Gronwall, C.1
Snelders, E.2
Jarelov Palm, A.3
Eriksson, F.4
Herne, N.5
Stahl, S.6
-
32
-
-
42149121917
-
[(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
-
33
-
-
33947672248
-
Radionuclide therapy of HER2-positive microxenografts using a 177Lu-labeled HER2-specific Affibody molecule
-
Tolmachev V., Orlova A., Pehrson R., Galli J., Baastrup B., Andersson K., Sandstrom M., Rosik D., Carlsson J., Lundqvist H., et al. Radionuclide therapy of HER2-positive microxenografts using a 177Lu-labeled HER2-specific Affibody molecule. Cancer Res 67 (2007) 2773-2782
-
(2007)
Cancer Res
, vol.67
, pp. 2773-2782
-
-
Tolmachev, V.1
Orlova, A.2
Pehrson, R.3
Galli, J.4
Baastrup, B.5
Andersson, K.6
Sandstrom, M.7
Rosik, D.8
Carlsson, J.9
Lundqvist, H.10
-
34
-
-
33847794292
-
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
-
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
-
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
-
37
-
-
34248549239
-
A designed ankyrin repeat protein evolved to picomolar affinity to Her2
-
Zahnd C., Wyler E., Schwenk J.M., Steiner D., Lawrence M.C., McKern N.M., Pecorari F., Ward C.W., Joos T.O., and Pluckthun A. A designed ankyrin repeat protein evolved to picomolar affinity to Her2. J Mol Biol 369 (2007) 1015-1028
-
(2007)
J Mol Biol
, vol.369
, pp. 1015-1028
-
-
Zahnd, C.1
Wyler, E.2
Schwenk, J.M.3
Steiner, D.4
Lawrence, M.C.5
McKern, N.M.6
Pecorari, F.7
Ward, C.W.8
Joos, T.O.9
Pluckthun, A.10
-
38
-
-
34247853389
-
Inhibition of caspase-2 by a designed ankyrin repeat protein: specificity, structure, and inhibition mechanism
-
Schweizer A., Roschitzki-Voser H., Amstutz P., Briand C., Gulotti-Georgieva M., Prenosil E., Binz H.K., Capitani G., Baici A., Pluckthun A., et al. Inhibition of caspase-2 by a designed ankyrin repeat protein: specificity, structure, and inhibition mechanism. Structure 15 (2007) 625-636
-
(2007)
Structure
, vol.15
, pp. 625-636
-
-
Schweizer, A.1
Roschitzki-Voser, H.2
Amstutz, P.3
Briand, C.4
Gulotti-Georgieva, M.5
Prenosil, E.6
Binz, H.K.7
Capitani, G.8
Baici, A.9
Pluckthun, A.10
-
39
-
-
34547911739
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
51
-
-
12244251436
-
Isolation of llama antibody fragments for prevention of dandruff by phage display in shampoo
-
Dolk E., van der Vaart M., Lutje Hulsik D., Vriend G., de Haard H., Spinelli S., Cambillau C., Frenken L., and Verrips T. Isolation of llama antibody fragments for prevention of dandruff by phage display in shampoo. Appl Environ Microbiol 71 (2005) 442-450
-
(2005)
Appl Environ Microbiol
, vol.71
, pp. 442-450
-
-
Dolk, E.1
van der Vaart, M.2
Lutje Hulsik, D.3
Vriend, G.4
de Haard, H.5
Spinelli, S.6
Cambillau, C.7
Frenken, L.8
Verrips, T.9
|