Camelid single-domain antibody fragments: Uses and prospects to investigate protein misfolding and aggregation, and to treat diseases associated with these phenomena.
Dumoulin, Mireille ; Université de Liège > Département des sciences de la vie > Enzymologie et repliement des protéines
Language :
English
Title :
Camelid single-domain antibody fragments: Uses and prospects to investigate protein misfolding and aggregation, and to treat diseases associated with these phenomena.
C.M. Dobson Protein folding and misfolding Nature 426 2003 884 890
A.V. Sorokin, E.R. Kim, and L.P. Ovchinnikov Proteasome system of protein degradation and processing Biochemistry (Moscow) 74 2009 1411 1442
F. Chiti, and C.M. Dobson Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75 2006 333 366
C.M. Dobson Principles of protein folding, misfolding and aggregation Semin. Cell Dev. Biol. 15 2004 3 16
E.R. Dorsey, R. Constantinescu, and J.P. Thompson Projected number of people with Parkinson disease in the most populous nations, 2005 through 2030 Neurology 68 2007 384 386
W. Thies, and L. Bleiler 2013 Alzheimer's disease facts and figures Alzheimers Dement. 9 2013 208 245
G.H. Suh, S.H. Ryu, and D.W. Lee Cholinesterase inhibitors for Alzheimer disease: do they provide more than symptomatic benefits? Am. J. Geriatr. Psychiatry 19 2011 266 273
M.A. Brodsky, B.S. Park, and J.G. Nutt Effects of a dopamine agonist on the pharmacodynamics of levodopa in Parkinson disease Arch. Neurol. 67 2010 27 32
M. Sunde, L.C. Serpell, and M. Bartlam Common core structure of amyloid fibrils by synchrotron X-ray diffraction J. Mol. Biol. 273 1997 729 739
M. Stefani, and C.M. Dobson Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution J. Mol. Med. 81 2003 678 699
T. Guilliams, F. El-Turk, and A.K. Buell Nanobodies raised against monomeric alpha-synuclein distinguish between fibrils at different maturation stages J. Mol. Biol. 425 2013 2397 2411
M.F. Mossuto, A. Dhulesia, and G. Devlin The non-core regions of human lysozyme amyloid fibrils influence cytotoxicity J. Mol. Biol. 402 2010 783 796
J.T. Jarrett, and P.T. Lansbury Jr. Seeding "one-dimensional crystallization" of amyloid: a pathogenic mechanism in Alzheimer's disease and scrapie? Cell 73 1993 1055 1058
S.I. Cohen, S. Linse, and L.M. Luheshi Proliferation of amyloid-beta42 aggregates occurs through a secondary nucleation mechanism Proc. Natl. Acad. Sci. U. S. A. 110 2013 9758 9763
J.S. Jeong, A. Ansaloni, and R. Mezzenga Novel mechanistic insight into the molecular basis of amyloid polymorphism and secondary nucleation during amyloid formation J. Mol. Biol. 425 2013 1765 1781
G. Ramachandran, and J.B. Udgaonkar Evidence for the existence of a secondary pathway for fibril growth during the aggregation of tau J. Mol. Biol. 421 2012 296 314
M. Costanzo, and C. Zurzolo The cell biology of prion-like spread of protein aggregates: mechanisms and implication in neurodegeneration Biochem. J. 452 2013 1 17
M.A. Speed, T. Morshead, and D.I. Wang Conformation of P22 tailspike folding and aggregation intermediates probed by monoclonal antibodies Protein Sci. 6 1997 99 108
B. O'Nuallain, and R. Wetzel Conformational Abs recognizing a generic amyloid fibril epitope Proc. Natl. Acad. Sci. U. S. A. 99 2002 1485 1490
B. O'Nuallain, I. Klyubin, and J.M. Mc Donald A monoclonal antibody against synthetic Abeta dimer assemblies neutralizes brain-derived synaptic plasticity-disrupting Abeta J. Neurochem. 119 2011 189 201
M. Dumoulin, and C.M. Dobson Probing the origins, diagnosis and treatment of amyloid diseases using antibodies Biochimie 86 2004 589 600
F. Eghiaian, J. Grosclaude, and S. Lesceu Insight into the PrPC - >PrPSc conversion from the structures of antibody-bound ovine prion scrapie-susceptibility variants Proc. Natl. Acad. Sci. U. S. A. 101 2004 10254 10259
R. Kayed, E. Head, and F. Sarsoza Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers Mol. Neurodegener. 2 2007 18
C. Haupt, M. Bereza, and S.T. Kumar Pattern recognition with a fibril-specific antibody fragment reveals the surface variability of natural amyloid fibrils J. Mol. Biol. 408 2011 529 540
H. Arai, C. Glabe, and H. Luecke Crystal structure of a conformation-dependent rabbit IgG Fab specific for amyloid prefibrillar oligomers Biochim. Biophys. Acta 1820 2012 1908 1914
M. Tayebi, D.R. Jones, and W.A. Taylor PrP(Sc)-specific antibodies with the ability to immunodetect prion oligomers PLoS ONE 6 2011 e19998
E.J. De Genst, T. Guilliams, and J. Wellens Structure and properties of a complex of alpha-synuclein and a single-domain camelid antibody J. Mol. Biol. 402 2010 326 343
G. Goldsteins, H. Persson, and K. Andersson Exposure of cryptic epitopes on transthyretin only in amyloid and in amyloidogenic mutants Proc. Natl. Acad. Sci. U. S. A. 96 1999 3108 3113
K. Manoutcharian, G. Acero, and M.E. Munguia Amyloid-beta peptide-specific single chain Fv antibodies isolated from an immune phage display library J. Neuroimmunol. 145 2003 12 17
Z.F. Zhao, G.Q. Gao, and S. Liu Screening for a human single chain Fv antibody against epitope on amyloid-beta 1-40 from a human phage display library Chin. Med. J. (Engl.) 120 2007 1931 1934
M. Medecigo, K. Manoutcharian, and V. Vasilevko Novel amyloid-beta specific scFv and VH antibody fragments from human and mouse phage display antibody libraries J. Neuroimmunol. 223 2010 104 114
C. Hamers-Casterman, T. Atarhouch, and S. Muyldermans Naturally occurring antibodies devoid of light chains Nature 363 1993 446 448
F. Van Bockstaele, J.B. Holz, and H. Revets The development of nanobodies for therapeutic applications Curr. Opin. Investig. Drugs 10 2009 1212 1224
S. Muyldermans Single domain camel antibodies: current status J. Biotechnol. 74 2001 277 302
R. van der Linden, B. de Geus, and W. Stok Induction of immune responses and molecular cloning of the heavy chain antibody repertoire of Lama glama J. Immunol. Methods 240 2000 185 195
M. Lauwereys, M. Arbabi Ghahroudi, and A. Desmyter Potent enzyme inhibitors derived from dromedary heavy-chain antibodies EMBO J. 17 1998 3512 3520
M. Dumoulin, K. Conrath, and A. Van Meirhaeghe Single-domain antibody fragments with high conformational stability Protein Sci. 11 2002 500 515
M.P. Lefranc, F. Ehrenmann, and C. Ginestoux Use of IMGT((R)) databases and tools for antibody engineering and humanization Methods Mol. Biol. 907 2012 3 37
K.E. Conrath, U. Wernery, and S. Muyldermans Emergence and evolution of functional heavy-chain antibodies in Camelidae Dev. Comp. Immunol. 27 2003 87 103
S. Muyldermans, C. Cambillau, and L. Wyns Recognition of antigens by single-domain antibody fragments: the superfluous luxury of paired domains Trends Biochem. Sci. 26 2001 230 235
S. Muyldermans, T. Atarhouch, and J. Saldanha Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains Protein Eng. 7 1994 1129 1135
K.B. Vu, M.A. Ghahroudi, and L. Wyns Comparison of llama VH sequences from conventional and heavy chain antibodies Mol. Immunol. 34 1997 1121 1131
T.T. Wu, G. Johnson, and E.A. Kabat Length distribution of CDRH3 in antibodies Proteins 16 1993 1 7
P.H. Chan, E. Pardon, and L. Menzer Engineering a camelid antibody fragment that binds to the active site of human lysozyme and inhibits its conversion into amyloid fibrils Biochemistry 47 2008 11041 11054
A. Desmyter, T.R. Transue, and M.A. Ghahroudi Crystal structure of a camel single-domain VH antibody fragment in complex with lysozyme Nat. Struct. Biol. 3 1996 803 811
K. Decanniere, S. Muyldermans, and L. Wyns Canonical antigen-binding loop structures in immunoglobulins: more structures, more canonical classes? J. Mol. Biol. 300 2000 83 91
E. De Genst, K. Silence, and K. Decanniere Molecular basis for the preferential cleft recognition by dromedary heavy-chain antibodies Proc. Natl. Acad. Sci. U. S. A. 103 2006 4586 4591
A. Desmyter, S. Spinelli, and F. Payan Three camelid VHH domains in complex with porcine pancreatic alpha-amylase. Inhibition and versatility of binding topology J. Biol. Chem. 277 2002 23645 23650
J. Wesolowski, V. Alzogaray, and J. Reyelt Single domain antibodies: promising experimental and therapeutic tools in infection and immunity Med. Microbiol. Immunol. 198 2009 157 174
T.R. Transue, E. De Genst, and M.A. Ghahroudi Camel single-domain antibody inhibits enzyme by mimicking carbohydrate substrate Proteins 32 1998 515 522
A. Marquardt, S. Muyldermans, and M. Przybylski A synthetic camel anti-lysozyme peptide antibody (peptibody) with flexible loop structure identified by high-resolution affinity mass spectrometry Chemistry 12 2006 1915 1923
J. Govaert, M. Pellis, and N. Deschacht Dual beneficial effect of interloop disulfide bond for single domain antibody fragments J. Biol. Chem. 287 2012 1970 1979
V.K. Nguyen, R. Hamers, and L. Wyns Camel heavy-chain antibodies: diverse germline V(H)H and specific mechanisms enlarge the antigen-binding repertoire EMBO J. 19 2000 921 930
G. Wei, W. Meng, and H. Guo Potent neutralization of influenza A virus by a single-domain antibody blocking M2 ion channel protein PLoS ONE 6 2011 e28309
J. Yan, G. Li, and Y. Hu Construction of a synthetic phage-displayed nanobody library with CDR3 regions randomized by trinucleotide cassettes for diagnostic applications J. Transl. Med. 12 2014 343
F. Fleetwood, N. Devoogdt, and M. Pellis Surface display of a single-domain antibody library on gram-positive bacteria Cell. Mol. Life Sci. 70 2013 1081 1093
J. Dong, A.A. Thompson, and Y. Fan A single-domain llama antibody potently inhibits the enzymatic activity of botulinum neurotoxin by binding to the non-catalytic alpha-exosite binding region J. Mol. Biol. 397 2010 1106 1118
C. Perruchini, F. Pecorari, and J.P. Bourgeois Llama VHH antibody fragments against GFAP: better diffusion in fixed tissues than classical monoclonal antibodies Acta Neuropathol. 118 2009 685 695
F. Rahbarizadeh, M.J. Rasaee, and M. Forouzandeh-Moghadam High expression and purification of the recombinant camelid anti-MUC1 single domain antibodies in Escherichia coli Protein Expr. Purif. 44 2005 32 38
H. Bakherad, S.L. Mousavi Gargari, and I. Rasooli In vivo neutralization of botulinum neurotoxins serotype E with heavy-chain camelid antibodies (VHH) Mol. Biotechnol. 55 2013 159 167
L.G. Frenken, R.H. van der Linden, and P.W. Hermans Isolation of antigen specific llama VHH antibody fragments and their high level secretion by Saccharomyces cerevisiae J. Biotechnol. 78 2000 11 21
A. Gorlani, H. de Haard, and T. Verrips Expression of VHHs in Saccharomyces cerevisiae Methods Mol. Biol. 911 2012 277 286
S. De Buck, V. Virdi, and T. De Meyer Production of camel-like antibodies in plants Methods Mol. Biol. 911 2012 305 324
Y.H. Teh, and T.A. Kavanagh High-level expression of Camelid nanobodies in Nicotiana benthamiana Transgenic Res. 19 2010 575 586
F. Rahbarizadeh, D. Ahmadvand, and Z. Sharifzadeh Nanobody; an old concept and new vehicle for immunotargeting Immunol. Invest. 40 2011 299 338
M. Arbabi Ghahroudi, A. Desmyter, and L. Wyns Selection and identification of single domain antibody fragments from camel heavy-chain antibodies FEBS Lett. 414 1997 521 526
K. Conrath, M. Lauwereys, and L. Wyns Camel single-domain antibodies as modular building units in bispecific and bivalent antibody constructs J. Biol. Chem. 276 2001 7346 7350
M. Dumoulin, A.M. Last, and A. Desmyter A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme Nature 424 2003 783 788
Y. Hagihara, S. Mine, and K. Uegaki Stabilization of an immunoglobulin fold domain by an engineered disulfide bond at the buried hydrophobic region J. Biol. Chem. 282 2007 36489 36495
D. Saerens, K. Conrath, and J. Govaert Disulfide bond introduction for general stabilization of immunoglobulin heavy-chain variable domains J. Mol. Biol. 377 2008 478 488
D. Saerens, M. Pellis, and R. Loris Identification of a universal VHH framework to graft non-canonical antigen-binding loops of camel single-domain antibodies J. Mol. Biol. 352 2005 597 607
P. Vanlandschoot, C. Stortelers, and E. Beirnaert Nanobodies(R): new ammunition to battle viruses Antivir. Res. 92 2011 389 407
M. Dumoulin, J.R. Kumita, and C.M. Dobson Normal and aberrant biological self-assembly: insights from studies of human lysozyme and its amyloidogenic variants Acc. Chem. Res. 39 2006 603 610
S. Girnius, M. Skinner, and B. Spencer A new lysozyme tyr54asn mutation causing amyloidosis in a family of Swedish ancestry with gastrointestinal symptoms Amyloid 19 2012 182 185
M. Dumoulin, R.J.K. Johnson, V. Bellotti, and C. Dobson Human lysozyme amyloidosis V. Uversky, A.L. Fink, Protein Misfolding, Aggregation and Conformational Diseases. II. Molecular Basis of Conformational Diseases Vol. II 2007 K. A. P. Dordrecht (The Netherlands) 285 308
M. Dumoulin Familial amyloidosis caused by lysozyme mutations J.W.K. Marina Ramirez-Alvarado, C.M. Dobson, Protein Misfolding Diseases: Basis of Protein Misfolding, Pathophysiology, Current, and Emerging Therapies 2010 John Wileys and Sons, Inc. Hoboken, New Jersy, USA 867 884
S. Reitamo, M. Klockars, and M. Adinolfi Human lysozyme (origin and distribution in health and disease) Ric. Clin. Lab. 8 1978 211 231
D.R. Booth, M. Sunde, and V. Bellotti Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis Nature 385 1997 787 793
R.J. Johnson, J. Christodoulou, and M. Dumoulin Rationalising lysozyme amyloidosis: insights from the structure and solution dynamics of T70N lysozyme J. Mol. Biol. 352 2005 823 836
D. Canet, A.M. Last, and P. Tito Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme Nat. Struct. Biol. 9 2002 308 315
M. Dumoulin, D. Canet, and A.M. Last Reduced global cooperativity is a common feature underlying the amyloidogenicity of pathogenic lysozyme mutations J. Mol. Biol. 346 2005 773 788
E.J. De Genst, P.H. Chan, and E. Pardon A nanobody binding to non-amyloidogenic regions of the protein human lysozyme enhances partial unfolding but inhibits amyloid fibril formation J. Phys. Chem. B 117 2013 13245 13258
S. Valleix, J.D. Gillmore, and F. Bridoux Hereditary systemic amyloidosis due to Asp76Asn variant beta2-microglobulin N. Engl. J. Med. 366 2012 2276 2283
R.P. Linke, H. Hampl, and H. Lobeck Lysine-specific cleavage of beta 2-microglobulin in amyloid deposits associated with hemodialysis Kidney Int. 36 1989 675 681
V. Bellotti, M. Stoppini, and P. Mangione Beta2-microglobulin can be refolded into a native state from ex vivo amyloid fibrils Eur. J. Biochem. 258 1998 61 67
H.L. Ploegh, H.T. Orr, and J.L. Stominger Biosynthesis and cell surface localization of nonglycosylated human histocompatibility antigens J. Immunol. 126 1981 270 275
P.J. Bjorkman, M.A. Saper, and B. Samraoui Structure of the human class I histocompatibility antigen, HLA-A2 Nature 329 1987 506 512
C.H. Trinh, D.P. Smith, and A.P. Kalverda Crystal structure of monomeric human beta-2-microglobulin reveals clues to its amyloidogenic properties Proc. Natl. Acad. Sci. U. S. A. 99 2002 9771 9776
T. Eichner, and S.E. Radford Understanding the complex mechanisms of beta2-microglobulin amyloid assembly FEBS J. 278 2011 3868 3883
G. Esposito, A. Corazza, and V. Bellotti Pathological self-aggregation of beta(2)-microglobulin: a challenge for protein biophysics Subcell. Biochem. 65 2012 165 183
T. Eichner, and S.E. Radford A generic mechanism of beta2-microglobulin amyloid assembly at neutral pH involving a specific proline switch J. Mol. Biol. 386 2009 1312 1326
C. Santambrogio, S. Ricagno, and M. Colombo DE-loop mutations affect beta2 microglobulin stability, oligomerization, and the low-pH unfolded form Protein Sci. 19 2010 1386 1394
K. Domanska, S. Vanderhaegen, and V. Srinivasan Atomic structure of a nanobody-trapped domain-swapped dimer of an amyloidogenic beta2-microglobulin variant Proc. Natl. Acad. Sci. U. S. A. 108 2011 1314 1319
G. Esposito, R. Michelutti, and G. Verdone Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibril formation Protein Sci. 9 2000 831 845
M.I. Ivanova, M.J. Thompson, and D. Eisenberg A systematic screen of beta(2)-microglobulin and insulin for amyloid-like segments Proc. Natl. Acad. Sci. U. S. A. 103 2006 4079 4082
S. Vanderhaegen, M. Fislage, and K. Domanska Structure of an early native-like intermediate of beta2-microglobulin amyloidogenesis Protein Sci. 22 2013 1349 1357
T. Pringsheim, N. Jette, and A. Frolkis The prevalence of Parkinson's disease: a systematic review and meta-analysis Mov. Disord. 29 2014 1583 1590
N. Malek, D. Swallow, and K.A. Grosset Alpha-synuclein in peripheral tissues and body fluids as a biomarker for Parkinson's disease - a systematic review Acta Neurol. Scand. 130 2014 59 72
V.N. Uversky, J. Li, and P. Souillac Biophysical properties of the synucleins and their propensities to fibrillate: inhibition of alpha-synuclein assembly by beta- and gamma-synucleins J. Biol. Chem. 277 2002 11970 11978
J.M. George The synucleins Genome Biol. 3 2002 REVIEWS3002
H.A. Lashuel, C.R. Overk, and A. Oueslati The many faces of alpha-synuclein: from structure and toxicity to therapeutic target Nat. Rev. Neurosci. 14 2013 38 48
N.M. Bonini, and B.I. Giasson Snaring the function of alpha-synuclein Cell 123 2005 359 361
J. Burre, M. Sharma, and T. Tsetsenis Alpha-synuclein promotes SNARE-complex assembly in vivo and in vitro Science 329 2010 1663 1667
M. Kasten, and C. Klein The many faces of alpha-synuclein mutations Mov. Disord. 28 2013 697 701
K. Beyer Alpha-synuclein structure, posttranslational modification and alternative splicing as aggregation enhancers Acta Neuropathol. 112 2006 237 251
W. Wang, I. Perovic, and J. Chittuluru A soluble alpha-synuclein construct forms a dynamic tetramer Proc. Natl. Acad. Sci. U. S. A. 108 2011 17797 17802
B.A. Silva, L. Breydo, and V.N. Uversky Targeting the chameleon: a focused look at alpha-synuclein and its roles in neurodegeneration Mol. Neurobiol. 47 2013 446 459
H.J. Koo, M.Y. Choi, and H. Im Aggregation-defective alpha-synuclein mutants inhibit the fibrillation of Parkinson's disease-linked alpha-synuclein variants Biochem. Biophys. Res. Commun. 386 2009 165 169
J. Meuvis, M. Gerard, and L. Desender The conformation and the aggregation kinetics of alpha-synuclein depend on the proline residues in its C-terminal region Biochemistry 49 2010 9345 9352
C.R. Bodner, A.S. Maltsev, and C.M. Dobson Differential phospholipid binding of alpha-synuclein variants implicated in Parkinson's disease revealed by solution NMR spectroscopy Biochemistry 49 2010 862 871
H.Y. Kim, M.K. Cho, and A. Kumar Structural properties of pore-forming oligomers of alpha-synuclein J. Am. Chem. Soc. 131 2009 17482 17489
Z. Qin, D. Hu, and S. Han Role of different regions of alpha-synuclein in the assembly of fibrils Biochemistry 46 2007 13322 13330
L. Solforosi, M. Milani, and N. Mancini A closer look at prion strains: characterization and important implications Prion 7 2013 99 108
S.K. Kaufman, and M.I. Diamond Prion-like propagation of protein aggregation and related therapeutic strategies Neurotherapeutics 10 2013 371 382
A. Thompson, A. MacKay, and P. Rudge Behavioral and psychiatric symptoms in prion disease Am. J. Psychiatry 171 2014 265 274
A. Ladogana, M. Puopolo, and E.A. Croes Mortality from Creutzfeldt-Jakob disease and related disorders in Europe, Australia, and Canada Neurology 64 2005 1586 1591
A. Kraus, B.R. Groveman, and B. Caughey Prions and the potential transmissibility of protein misfolding diseases Annu. Rev. Microbiol. 67 2013 543 564
K.M. Pan, M. Baldwin, and J. Nguyen Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins Proc. Natl. Acad. Sci. U. S. A. 90 1993 10962 10966
M.W. Brazier, A.I. Mot, and A.R. White Immunotherapeutic approaches in prion disease: progress, challenges and potential directions Ther. Deliv. 4 2013 615 628
R. Zahn, A. Liu, and T. Luhrs NMR solution structure of the human prion protein Proc. Natl. Acad. Sci. U. S. A. 97 2000 145 150
A. Andreeva, D. Howorth, and J.M. Chandonia Data growth and its impact on the SCOP database: new developments Nucleic Acids Res. 36 2008 D419 D425
G. Forloni, N. Angeretti, and R. Chiesa Neurotoxicity of a prion protein fragment Nature 362 1993 543 546
R.N. Abskharon, G. Giachin, and A. Wohlkonig Probing the N-terminal beta-sheet conversion in the crystal structure of the human prion protein bound to a nanobody J. Am. Chem. Soc. 136 2014 937 944
D.R. Jones, W.A. Taylor, and C. Bate A camelid anti-PrP antibody abrogates PrP replication in prion-permissive neuroblastoma cell lines PLoS ONE 5 2010 e9804
M.A. David, D.R. Jones, and M. Tayebi Potential candidate camelid antibodies for the treatment of protein-misfolding diseases J. Neuroimmunol. 272 2014 76 85
A. Abu-Baker, and G.A. Rouleau Oculopharyngeal muscular dystrophy: recent advances in the understanding of the molecular pathogenic mechanisms and treatment strategies Biochim. Biophys. Acta 1772 2007 173 185
A. Banerjee, L.H. Apponi, and G.K. Pavlath PABPN1: molecular function and muscle disease FEBS J. 280 2013 4230 4250
A. Chartier, B. Benoit, and M. Simonelig A Drosophila model of oculopharyngeal muscular dystrophy reveals intrinsic toxicity of PABPN1 EMBO J. 25 2006 2253 2262
X. Fan, P. Dion, and J. Laganiere Oligomerization of polyalanine expanded PABPN1 facilitates nuclear protein aggregation that is associated with cell death Hum. Mol. Genet. 10 2001 2341 2351
N. Scarafone, C. Pain, and A. Fratamico Amyloid-like fibril formation by polyQ proteins: a critical balance between the polyQ length and the constraints imposed by the host protein PLoS ONE 7 2012 e31253
V. Raz, T. Abraham, and E.W. van Zwet Reversible aggregation of PABPN1 pre-inclusion structures Nucleus 2 2011 208 218
P. Verheesen, A. de Kluijver, and S. van Koningsbruggen Prevention of oculopharyngeal muscular dystrophy-associated aggregation of nuclear polyA-binding protein with a single-domain intracellular antibody Hum. Mol. Genet. 15 2006 105 111
A. Impagliazzo, A.W. Tepper, and T.C. Verrips Structural basis for a PABPN1 aggregation-preventing antibody fragment in OPMD FEBS Lett. 584 2010 1558 1564
A. Chartier, V. Raz, and E. Sterrenburg Prevention of oculopharyngeal muscular dystrophy by muscular expression of Llama single-chain intrabodies in vivo Hum. Mol. Genet. 18 2009 1849 1859
D.M. Walsh, I. Klyubin, and J.V. Fadeeva Amyloid-beta oligomers: their production, toxicity and therapeutic inhibition Biochem. Soc. Trans. 30 2002 552 557
J. Hardy, and D.J. Selkoe The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics Science 297 2002 353 356
D.S. Wang, D.W. Dickson, and J.S. Malter Tissue transglutaminase, protein cross-linking and Alzheimer's disease: review and views Int. J. Clin. Exp. Pathol. 1 2008 5 18
D.M. Walsh, A.M. Minogue, and C. Sala Frigerio The APP family of proteins: similarities and differences Biochem. Soc. Trans. 35 2007 416 420
D.W. Banner, B. Gsell, and J. Benz Mapping the conformational space accessible to BACE2 using surface mutants and cocrystals with Fab fragments, Fynomers and Xaperones Acta Crystallogr. D Biol. Crystallogr. 69 2013 1124 1137
T. Sato, N. Dohmae, and Y. Qi Potential link between amyloid beta-protein 42 and C-terminal fragment gamma 49-99 of beta-amyloid precursor protein J. Biol. Chem. 278 2003 24294 24301
B. De Strooper, and W. Annaert Novel research horizons for presenilins and gamma-secretases in cell biology and disease Annu. Rev. Cell Dev. Biol. 26 2010 235 260
T. Iwatsubo, A. Odaka, and N. Suzuki Visualization of A beta 42(43) and A beta 40 in senile plaques with end-specific A beta monoclonals: evidence that an initially deposited species is A beta 42(43) Neuron 13 1994 45 53
F. Kamenetz, T. Tomita, and H. Hsieh APP processing and synaptic function Neuron 37 2003 925 937
D.M. Walsh, and D.J. Selkoe A beta oligomers - a decade of discovery J. Neurochem. 101 2007 1172 1184
I. Kuperstein, K. Broersen, and I. Benilova Neurotoxicity of Alzheimer's disease Abeta peptides is induced by small changes in the Abeta42 to Abeta40 ratio EMBO J. 29 2010 3408 3420
L. Wu, P. Rosa-Neto, and G.Y. Hsiung Early-onset familial Alzheimer's disease (EOFAD) Can. J. Neurol. Sci. 39 2012 436 445
S.S. Sisodia, and P.H. St George-Hyslop gamma-Secretase, Notch, Abeta and Alzheimer's disease: where do the presenilins fit in? Nat. Rev. Neurosci. 3 2002 281 290
D. Lambracht-Washington, and R.N. Rosenberg Active DNA Abeta42 vaccination as immunotherapy for Alzheimer disease Transl. Neurosci. 3 2012 307 313
C.E. Munte, M. Beck Erlach, and W. Kremer Distinct conformational states of the Alzheimer beta-amyloid peptide can be detected by high-pressure NMR spectroscopy Angew. Chem. Int. Ed. Engl. 52 2013 8943 8947
P. Lafaye, I. Achour, and P. England Single-domain antibodies recognize selectively small oligomeric forms of amyloid beta, prevent Abeta-induced neurotoxicity and inhibit fibril formation Mol. Immunol. 46 2009 695 704
C. Wu, M.T. Bowers, and J.E. Shea Molecular structures of quiescently grown and brain-derived polymorphic fibrils of the Alzheimer amyloid abeta9-40 peptide: a comparison to agitated fibrils PLoS Comput. Biol. 6 2010 e1000693
G. Habicht, C. Haupt, and R.P. Friedrich Directed selection of a conformational antibody domain that prevents mature amyloid fibril formation by stabilizing Abeta protofibrils Proc. Natl. Acad. Sci. U. S. A. 104 2007 19232 19237
I. Morgado, K. Wieligmann, and M. Bereza Molecular basis of beta-amyloid oligomer recognition with a conformational antibody fragment Proc. Natl. Acad. Sci. U. S. A. 109 2012 12503 12508
K.S. Rutgers, A. van Remoortere, and M.A. van Buchem Differential recognition of vascular and parenchymal beta amyloid deposition Neurobiol. Aging 32 2011 1774 1783
K.S. Rutgers, R.J. Nabuurs, and S.A. van den Berg Transmigration of beta amyloid specific heavy chain antibody fragments across the in vitro blood-brain barrier Neuroscience 190 2011 37 42
C. Haupt, I. Morgado, and S.T. Kumar Amyloid fibril recognition with the conformational B10 antibody fragment depends on electrostatic interactions J. Mol. Biol. 405 2011 341 348
J. Wacker, R. Ronicke, and M. Westermann Oligomer-targeting with a conformational antibody fragment promotes toxicity in Abeta-expressing flies Acta Neuropathol. Commun. 2 2014 43
P.N. Lacor, M.C. Buniel, and L. Chang Synaptic targeting by Alzheimer's-related amyloid beta oligomers J. Neurosci. 24 2004 10191 10200
M.P. Lambert, P.T. Velasco, and L. Chang Monoclonal antibodies that target pathological assemblies of Abeta J. Neurochem. 100 2007 23 35
E.B. Lee, L.Z. Leng, and B. Zhang Targeting amyloid-beta peptide (Abeta) oligomers by passive immunization with a conformation-selective monoclonal antibody improves learning and memory in Abeta precursor protein (APP) transgenic mice J. Biol. Chem. 281 2006 4292 4299
F. Bard, R. Barbour, and C. Cannon Epitope and isotype specificities of antibodies to beta-amyloid peptide for protection against Alzheimer's disease-like neuropathology Proc. Natl. Acad. Sci. U. S. A. 100 2003 2023 2028
Y. Yan, and C. Wang Abeta42 is more rigid than Abeta40 at the C terminus: implications for Abeta aggregation and toxicity J. Mol. Biol. 364 2006 853 862
B. Kieninger, Z. Gioeva, and S. Kruger PTAA and B10: new approaches to amyloid detection in tissue-evaluation of amyloid detection in tissue with a conjugated polyelectrolyte and a fibril-specific antibody fragment Amyloid 18 2011 47 52
H. Chertkow, and S. Black Imaging biomarkers and their role in dementia clinical trials Can. J. Neurol. Sci. 34 Suppl. 1 2007 S77 S83
R.J. Bateman, C. Xiong, and T.L. Benzinger Clinical and biomarker changes in dominantly inherited Alzheimer's disease N. Engl. J. Med. 367 2012 795 804
D. Schenk, R. Barbour, and W. Dunn Immunization with amyloid-beta attenuates Alzheimer-disease-like pathology in the PDAPP mouse Nature 400 1999 173 177
J.C. Dodart, K.R. Bales, and K.S. Gannon Immunization reverses memory deficits without reducing brain Abeta burden in Alzheimer's disease model Nat. Neurosci. 5 2002 452 457
B. Spencer, and E. Masliah Immunotherapy for Alzheimer's disease: past, present and future Front. Aging Neurosci. 6 2014 114
A. Cardinale, D. Merlo, and P. Giunchedi Therapeutic application of intrabodies against age-related neurodegenerative disorders Curr. Pharm. Des. 20 2014 6028 6036
T. Li, J.P. Bourgeois, and S. Celli Cell-penetrating anti-GFAP VHH and corresponding fluorescent fusion protein VHH-GFP spontaneously cross the blood-brain barrier and specifically recognize astrocytes: application to brain imaging FASEB J. 26 2012 3969 3979
U. Rothbauer, K. Zolghadr, and S. Tillib Targeting and tracing antigens in live cells with fluorescent nanobodies Nat. Methods 3 2006 887 889
I. Van Audenhove, K. Van Impe, and D. Ruano-Gallego Mapping cytoskeletal protein function in cells by means of nanobodies Cytoskeleton (Hoboken) 70 2013 604 622
W.J. Bowers, X.O. Breakefield, and M. Sena-Esteves Genetic therapy for the nervous system Hum. Mol. Genet. 20 2011 R28 R41
J.F. Poduslo, G.L. Curran, and C.T. Berg Macromolecular permeability across the blood-nerve and blood-brain barriers Proc. Natl. Acad. Sci. U. S. A. 91 1994 5705 5709
A. Muruganandam, J. Tanha, and S. Narang Selection of phage-displayed llama single-domain antibodies that transmigrate across human blood-brain barrier endothelium FASEB J. 16 2002 240 242
A. Abulrob, H. Sprong, and P. Van Bergen en Henegouwen The blood-brain barrier transmigrating single domain antibody: mechanisms of transport and antigenic epitopes in human brain endothelial cells J. Neurochem. 95 2005 1201 1214
G. Caljon, V. Caveliers, and T. Lahoutte Using microdialysis to analyse the passage of monovalent nanobodies through the blood-brain barrier Br. J. Pharmacol. 165 2012 2341 2353
R.J. Nabuurs, K.S. Rutgers, and M.M. Welling In vivo detection of amyloid-beta deposits using heavy chain antibody fragments in a transgenic mouse model for Alzheimer's disease PLoS ONE 7 2012 e38284
A.S. Haqqani, N. Caram-Salas, and W. Ding Multiplexed evaluation of serum and CSF pharmacokinetics of brain-targeting single-domain antibodies using a NanoLC-SRM-ILIS method Mol. Pharm. 10 2013 1542 1556
J. De Vos, N. Devoogdt, and T. Lahoutte Camelid single-domain antibody-fragment engineering for (pre)clinical in vivo molecular imaging applications: adjusting the bullet to its target Expert Opin. Biol. Ther. 13 2013 1149 1160
M. D'Huyvetter, C. Xavier, and V. Caveliers Radiolabeled nanobodies as theranostic tools in targeted radionuclide therapy of cancer Expert Opin. Drug Deliv. 2014 1 16
S. Oliveira, G.A. van Dongen, and M. Stigter-van Walsum Rapid visualization of human tumor xenografts through optical imaging with a near-infrared fluorescent anti-epidermal growth factor receptor nanobody Mol. Imaging 11 2011 33 46
V. Cortez-Retamozo, M. Lauwereys, and G. Hassanzadeh Gh Efficient tumor targeting by single-domain antibody fragments of camels Int. J. Cancer 98 2002 456 462
R. Chakravarty, S. Goel, and W. Cai Nanobody: the "magic bullet" for molecular imaging? Theranostics 4 2014 386 398
I. Vaneycken, N. Devoogdt, and N. Van Gassen Preclinical screening of anti-HER2 nanobodies for molecular imaging of breast cancer FASEB J. 25 2011 2433 2446
C. Vincke, R. Loris, and D. Saerens General strategy to humanize a camelid single-domain antibody and identification of a universal humanized nanobody scaffold J. Biol. Chem. 284 2009 3273 3284