2197:
20:
142:
tags can be conjugated to
Affimers. Specific cysteine residues can be introduced to the protein to allow thiol chemistry to uniformly orient Affimers on a solid support eg ELISA plates. This flexible functionalisation of the Affimer molecule allows functionality across multiple applications and assay
622:
Stadler LK, Hoffmann T, Tomlinson DC, Song Q, Lee T, Busby M, Nyathi Y, Gendra E, Tiede C, Flanagan K, Cockell SJ, Wipat A, Harwood C, Wagner SD, Knowles MA, Davis JJ, Keegan N, Ferrigno PK (September 2011). "Structure-function studies of an engineered scaffold protein derived from Stefin A. II:
151:
Affimers are recombinant proteins. As they are manufactured using recombinant bacterial production processes, the batch-to-batch consistency for
Affimers is improved compared to polyclonal antibodies, overcoming some of the issues of reproducibility and security of supply.
92:. Stabilization of the two peptides by the protein scaffold constrains the possible conformations that the peptides can take. This increases the binding affinity and specificity compared to libraries of free peptides, though can limit the target repertoire of Affimers.
126:
Multimeric forms
Affimers have been generated and shown to yield titres in the range of 200–400 mg/L under small-scale culture using bacterial host systems. Multimeric forms of Affimers with the same target specificity provide
2042:
King R, Tiede C, Simmons K, Fishwick C, Tomlinson D, Ajjan R (February 2015). "Inhibition of complement C3 and fibrinogen interaction: a potential novel therapeutic target to reduce cardiovascular disease in diabetes".
1993:
1792:
Pechlivani, Nikoletta; Kearney, Katherine J.; Tiede, Christian; Cheah, Ramsah; Phoenix, Fladia; Ponnambalam, Sreenivasan; Ault, James R.; McPherson, Michael J.; Tomlinson, Darren C.; Ajjan, Ramzi A. (2022-05-01).
42:
in different applications. These affinity reagents have been optimized to increase their stability, make them tolerant to a range of temperatures and pH, reduce their size, and to increase their expression in
1630:
Robinson JI, Baxter EW, Owen RL, Thomsen M, Tomlinson DC, Waterhouse MP, Win SJ, Nettleship JE, Tiede C, Foster RJ, Owens RJ, Fishwick CW, Harris SA, Goldman A, McPherson MJ, Morgan AW (January 2018).
1407:
1500:
Davis JJ, Tkac J, Humphreys R, Buxton AT, Lee TA, Ko
Ferrigno P (May 2009). "Peptide aptamers in label-free protein detection: 2. Chemical optimization and detection of distinct protein isoforms".
1436:
1564:
252:
associated with the
Affimer scaffold, at levels comparable to a marketed antibody therapeutic. Furthermore, initial preclinical studies showed good efficacy and tolerability of the anti-
1325:
Weckman NE, McRae C, Ko
Ferrigno P, Seshia AA (October 2016). "Comparison of the specificity and affinity of surface immobilised Affimer binders using the quartz crystal microbalance".
1535:
755:"Gene organization of oryzacystatin-II, a new cystatin superfamily member of plant origin, is closely related to that of oryzacystatin-I but different from those of animal cystatins"
1997:
1268:
Fisher MJ, Williamson DJ, Burslem GM, Plante JP, Manfield IW, Tiede C, Ault JR, Stockley PG, Plein S, Maqbool A, Tomlinson DC, Foster R, Warriner SL, Bon RS (December 2015).
1598:
352:"Affimers as an Alternative to Antibodies in an Affinity LC-MS Assay for Quantification of the Soluble Receptor of Advanced Glycation End-Products (sRAGE) in Human Serum"
215:
where Avacta are developing PD-L1 inhibitors as alternatives to Opdivo and Yervoy, though requires half life modification to prevent rapid excretion through the kidney.
103:
libraries of 10 randomized sequences are used to screen for
Affimer proteins that exhibit high-specificity binding to the target protein with binding affinities in the
163:. Two separate loop sequences, incorporating a total of 12 to 36 amino acids, form the target interaction surface so interaction surfaces can range form 650–1000
2086:
2149:
1465:
Davis JJ, Tkac J, Laurenson S, Ko
Ferrigno P (February 2007). "Peptide aptamers in label-free protein detection: 1. Characterization of the immobilized scaffold".
1768:
1733:
Johnson A, Song Q, Ko
Ferrigno P, Bueno PR, Davis JJ (August 2012). "Sensitive affimer and antibody based impedimetric label-free assays for C-reactive protein".
175:
Affimer technology has been commercialised and developed by Avacta, which is developing these affinity reagents as tools for diagnostics and as biotherapeutics.
535:
Woodman R, Yeh JT, Laurenson S, Ko
Ferrigno P (October 2005). "Design and validation of a neutral protein scaffold for the presentation of peptide aptamers".
1415:
1945:
1444:
1572:
218:
Affimers can be conjugated to form multimers for the design of therapeutics. Examples include the production of multi-specific Affimer molecules to
207:
The small size and stability profile of Affimers combined with their human origin confer drug-like properties. This may represent advantages over
1064:
949:"Abstract 3776: Generation and formatting of an Affimer® biotherapeutic for the inhibition of the PD-L1/PD-1 pathway: Proof of concept in mouse"
894:"Sensitive and selective Affimer-functionalised interdigitated electrode-based capacitive biosensor for Her4 protein tumour biomarker detection"
119:. Affimers are generated using recombinant systems, so their generation is more rapid and reproducible compared to the production of polyclonal
1543:
1963:
1850:
Kyle HF, Wickson KF, Stott J, Burslem GM, Breeze AL, Tiede C, Tomlinson DC, Warriner SL, Nelson A, Wilson AJ, Edwards TA (October 2015).
2142:
663:
Tiede C, Tang AA, Deacon SE, Mandal U, Nettleship JE, Owen RL, George SE, Harrison DJ, Owens RJ, Tomlinson DC, McPherson MJ (May 2014).
2259:
1632:"Affimer proteins inhibit immune complex binding to FcγRIIIa with high specificity through competitive and allosteric modes of action"
1221:"Ultraefficient Cap-Exchange Protocol To Compact Biofunctional Quantum Dots for Sensitive Ratiometric Biosensing and Cell Imaging"
34:
that bind to target proteins with affinity in the nanomolar range. These engineered non-antibody binding proteins are designed to
1606:
1063:
Schlichthaerle T, Eklund AS, Schueder F, Strauss MT, Tiede C, Curd A, Ries J, Peckham M, Tomlinson DC, Jungmann R (August 2018).
199:
can be produced with the potential to express these inhibitors in mammalian cells modify signalling pathways as cell therapies.
88:
Affimer proteins display two peptide loops that can all be randomized to bind to desired target proteins, in a similar manner to
893:
481:
Rawlings AE, Bramble JP, Tang AA, Somner LA, Monnington AE, Cooke DJ, McPherson MJ, Tomlinson DC, Staniland SS (October 2015).
23:
The Affimer protein scaffold – showing the two loops where random peptides can be inserted to create a protein binding surface
2265:
2249:
2223:
2178:
2135:
846:
432:
Sharma R, Deacon SE, Nowak D, George SE, Szymonik MP, Tang AA, Tomlinson DC, Davies AG, McPherson MJ, Wälti C (June 2016).
2094:
256:
immuno-oncology Affimers in mice. It is anticipated that IND filing for the first Affimer therapeutic will occur in 2023.
196:
575:"Structure-function studies of an engineered scaffold protein derived from stefin A. I: Development of the SQM variant"
1219:
Wang W, Guo Y, Tiede C, Chen S, Kopytynski M, Kong Y, Kulak A, Tomlinson D, Chen R, McPherson M, Zhou D (May 2017).
2394:
2271:
229:
and for use as the targeting moiety in chimeric receptors or modified to carry a toxin in Affimer-drug conjugates.
434:"Label-free electrochemical impedance biosensor to detect human interleukin-8 in serum with sub-pg/ml sensitivity"
253:
237:
188:
159:
were engineered to be stable, non-toxic, biologically neutral and contain no post-translational modifications or
1408:"Anti-idiotypic binders for Trastuzumab validated in regulatory bioanalysis assay in collaboration with Covance"
2213:
2205:
2254:
2184:
2127:
1437:"Development and validation of anti-idiotypic Affmers to trastuzumab in a pharmacokinetic assay | Avacta"
2229:
192:
1794:
1162:
Lopata A, Hughes R, Tiede C, Heissler SM, Sellers JR, Knight PJ, Tomlinson D, Peckham M (April 2018).
1334:
1281:
1175:
1016:
847:"Interfacing native and non-native peptides: using Affimers to recognise α-helix mimicking foldamers"
399:
241:
58:
2196:
1370:"Antibody Mimetics for the Detection of Small Organic Compounds Using a Quartz Crystal Microbalance"
115:
screening and development also mean that the target space for Affimers is not limited by the animal
2305:
2159:
573:
Hoffmann T, Stadler LK, Busby M, Song Q, Buxton AT, Wagner SD, Davis JJ, Ko Ferrigno P (May 2010).
483:"Phage display selected magnetite interacting Adhirons for shape controlled nanoparticle synthesis"
104:
89:
62:
39:
1565:"Development and characterisation of Affimer binders to 4 leading therapeutic antibodies | Avacta"
1164:"Affimer proteins for F-actin: novel affinity reagents that label F-actin in live and fixed cells"
948:
2068:
1832:
1095:
976:
924:
827:
784:
665:"Adhiron: a stable and versatile peptide display scaffold for molecular recognition applications"
156:
1971:
1893:"Proteomic profiling of VCP substrates links VCP to K6-linked ubiquitylation and c-Myc function"
1852:"Exploration of the HIF-1α/p300 interface using peptide and Adhiron phage display technologies"
2323:
2060:
1922:
1873:
1824:
1816:
1750:
1715:
1663:
1517:
1482:
1389:
1350:
1307:
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1201:
1144:
1087:
1042:
968:
916:
869:
819:
776:
735:
694:
640:
604:
552:
512:
463:
381:
329:
66:
1003:
Xie C, Tiede C, Zhang X, Wang C, Li Z, Xu X, McPherson MJ, Tomlinson DC, Xu W (August 2017).
2315:
2163:
2052:
1912:
1904:
1863:
1806:
1742:
1705:
1697:
1653:
1643:
1509:
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1289:
1240:
1232:
1191:
1183:
1134:
1126:
1079:
1032:
1024:
960:
908:
892:
Zhurauski P, Arya SK, Jolly P, Tiede C, Tomlinson DC, Ko Ferrigno P, Estrela P (June 2018).
861:
811:
766:
725:
684:
676:
632:
594:
586:
544:
502:
494:
453:
445:
371:
363:
319:
309:
44:
35:
1891:
Heidelberger JB, Voigt A, Borisova ME, Petrosino G, Ruf S, Wagner SA, Beli P (April 2018).
1113:
Bedford R, Tiede C, Hughes R, Curd A, McPherson MJ, Peckham M, Tomlinson DC (August 2017).
1994:"Avacta and Memorial Sloan Kettering Cancer Center in cell therapy research collaboration"
1368:
Koutsoumpeli E, Tiede C, Murray J, Tang A, Bon RS, Tomlinson DC, Johnson S (March 2017).
802:
Turk V, Bode W (July 1991). "The cystatins: protein inhibitors of cysteine proteinases".
296:
Tiede C, Bedford R, Heseltine SJ, Smith G, Wijetunga I, Ross R, et al. (June 2017).
1686:"Ubiquitin Linkage-Specific Affimers Reveal Insights into K6-Linked Ubiquitin Signaling"
1338:
1285:
1179:
1020:
1005:"Development of an Affimer-antibody combined immunological diagnosis kit for glypican-3"
1917:
1892:
1710:
1685:
1658:
1631:
1302:
1269:
1245:
1220:
1196:
1163:
1139:
1114:
1037:
1004:
689:
664:
599:
574:
507:
482:
458:
433:
376:
351:
324:
297:
249:
164:
2056:
2388:
2363:
2289:
1836:
815:
771:
754:
116:
100:
2072:
1099:
980:
831:
788:
111:
screening techniques allows the identification of specific, high affinity Affimers.
928:
964:
367:
1811:
1701:
1385:
1536:"Affimer binders improve diagnostic assay performance for C.difficile detection"
232:
Affimers as therapeutics are in discovery and preclinical development to tackle
135:
78:
2018:
1636:
Proceedings of the National Academy of Sciences of the United States of America
1187:
1028:
912:
449:
350:
Klont F, Hadderingh M, Horvatovich P, Ten Hacken NH, Bischoff R (August 2018).
2122:
1130:
548:
82:
1820:
972:
680:
636:
590:
2373:
2348:
2343:
1908:
1648:
223:
167:. The large interaction surface results allows binding to target proteins.
160:
70:
2064:
1926:
1877:
1828:
1754:
1719:
1667:
1599:"Avacta Scientist Dr Geoff Platt presents Affimer data in webinar | Avacta"
1521:
1486:
1393:
1354:
1311:
1254:
1236:
1205:
1148:
1091:
1083:
1046:
920:
873:
739:
698:
644:
608:
556:
516:
467:
385:
333:
19:
823:
780:
2368:
2241:
1369:
714:"Cystatins: biochemical and structural properties, and medical relevance"
212:
208:
120:
31:
314:
73:, which function in nature as cysteine protease inhibitors, these 12–14
2338:
2328:
1868:
1851:
1346:
1293:
865:
498:
219:
183:
Affimer binders have been used across a number of platforms, including
128:
1746:
1513:
1478:
2358:
2353:
233:
1769:"Affimer® reagents facilitate affinity chromatography purification"
184:
139:
18:
730:
713:
1684:
Michel MA, Swatek KN, Hospenthal MK, Komander D (October 2017).
298:"Affimer proteins are versatile and renewable affinity reagents"
2131:
74:
1795:"Affinity purification of fibrinogen using an Affimer column"
1065:"Site-Specific Labeling of Affimers for DNA-PAINT Microscopy"
2087:"Affimer Technology: Results of PBMC Immunogenicity Testing"
1115:"Alternative reagents to antibodies in imaging applications"
845:
Arrata I, Barnard A, Tomlinson DC, Wilson AJ (March 2017).
1270:"Trivalent Gd-DOTA reagents for modification of proteins"
2117:
1799:
Biochimica et Biophysica Acta (BBA) - General Subjects
1946:"Interview with Amrik Basran at Avacta Life Sciences"
211:
in terms of tissue penetration, for example in solid
2314:
2298:
2282:
2250:
Single-chain variable fragment / di-scFv / tri-scFv
2240:
2204:
2170:
77:proteins share the common tertiary structure of an
623:Development and applications of the SQT variant".
134:Many different tags and fusion proteins, such as
61:in Cambridge then across two laboratories at the
57:Affimer proteins were developed initially at the
753:Kondo H, Abe K, Emori Y, Arai S (January 1991).
2143:
2123:An Introduction to Affimer Technology - video
38:the molecular recognition characteristics of
8:
669:Protein Engineering, Design & Selection
625:Protein Engineering, Design & Selection
579:Protein Engineering, Design & Selection
2150:
2136:
2128:
568:
566:
1916:
1867:
1810:
1709:
1657:
1647:
1301:
1244:
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1138:
1036:
770:
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688:
598:
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506:
457:
375:
323:
313:
658:
656:
654:
427:
425:
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264:
1679:
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1625:
1623:
1593:
1591:
1589:
1225:ACS Applied Materials & Interfaces
1940:
1938:
1936:
1058:
1056:
998:
996:
994:
992:
990:
942:
940:
938:
887:
885:
883:
7:
712:Turk V, Stoka V, Turk D (May 2008).
345:
343:
291:
289:
287:
285:
283:
281:
279:
277:
2260:Small modular immunopharmaceutical
947:Basran A, Stanley E (2018-07-01).
14:
271:Proprietary name, owned by Avacta
81:lying on top of an anti-parallel
2195:
138:, single-stranded DNA, His, and
901:Biosensors & Bioelectronics
438:Biosensors & Bioelectronics
1964:"TMAC Affimer Drug Conjugates"
1:
2057:10.1016/s0140-6736(15)60372-5
965:10.1158/1538-7445.AM2018-3776
368:10.1021/acs.jproteome.8b00414
107:range. The ability to direct
1812:10.1016/j.bbagen.2022.130115
1702:10.1016/j.molcel.2017.08.020
1386:10.1021/acs.analchem.6b04790
816:10.1016/0014-5793(91)80804-C
772:10.1016/0014-5793(91)80090-p
537:Journal of Molecular Biology
356:Journal of Proteome Research
242:immune checkpoint inhibitors
197:protein-protein interactions
131:effects in target binding.
2411:
1188:10.1038/s41598-018-24953-4
1029:10.1038/s41598-017-10083-w
913:10.1016/j.bios.2018.02.041
450:10.1016/j.bios.2016.02.028
222:binders to increase their
2193:
1131:10.1007/s12551-017-0278-2
549:10.1016/j.jmb.2005.08.001
248:human samples showed low
195:. Affimers that inhibit
189:surface plasmon resonance
2218:fragment / Fab' fragment
1773:www.drugtargetreview.com
179:Reagents and Diagnostics
1909:10.15252/embr.201744754
1649:10.1073/pnas.1707856115
959:(13 Supplement): 3776.
854:Chemical Communications
718:Frontiers in Bioscience
404:The Scientist Magazine®
400:"Antibody Alternatives"
2255:Single-domain antibody
2185:Trifunctional antibody
1237:10.1021/acsami.6b13807
1084:10.1002/anie.201804020
681:10.1093/protein/gzu007
637:10.1093/protein/gzr019
591:10.1093/protein/gzq012
244:. Early studies using
24:
2364:Kunitz domain peptide
2230:Chemically linked Fab
2160:monoclonal antibodies
193:affinity purification
90:monoclonal antibodies
49:and mammalian cells.
40:monoclonal antibodies
22:
1856:Molecular BioSystems
1735:Analytical Chemistry
1502:Analytical Chemistry
1467:Analytical Chemistry
1374:Analytical Chemistry
1280:(116): 96194–96200.
240:cell therapy and as
157:synthetic antibodies
69:inhibitor family of
59:MRC Cancer Cell Unit
2019:"Pipeline | Avacta"
1339:2016Ana...141.6278W
1286:2015RSCAd...596194F
1231:(18): 15232–15244.
1180:2018NatSR...8.6572L
1119:Biophysical Reviews
1078:(34): 11060–11063.
1021:2017NatSR...7.9608X
315:10.7554/elife.24903
65:. Derived from the
63:University of Leeds
1950:Drug Target Review
1869:10.1039/c5mb00284b
1347:10.1039/c6an01602b
1294:10.1039/c5ra20359g
1168:Scientific Reports
1009:Scientific Reports
866:10.1039/c6cc09395g
499:10.1039/C5SC01472G
25:
2395:Antibody mimetics
2382:
2381:
2324:Affibody molecule
2316:Antibody mimetics
2242:Variable fragment
2164:antibody mimetics
1747:10.1021/ac300835b
1696:(1): 233–246.e5.
1514:10.1021/ac802513n
1479:10.1021/ac061863z
1333:(22): 6278–6286.
1072:Angewandte Chemie
860:(19): 2834–2837.
493:(10): 5586–5594.
161:disulfide bridges
67:cysteine protease
28:Affimer molecules
2402:
2199:
2152:
2145:
2138:
2129:
2106:
2105:
2103:
2102:
2093:. Archived from
2083:
2077:
2076:
2051:(Suppl 1): S57.
2039:
2033:
2032:
2030:
2029:
2015:
2009:
2008:
2006:
2005:
1996:. Archived from
1989:
1983:
1982:
1980:
1979:
1970:. Archived from
1960:
1954:
1953:
1942:
1931:
1930:
1920:
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1713:
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1605:. Archived from
1595:
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1581:
1580:
1571:. Archived from
1561:
1555:
1554:
1552:
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1542:. Archived from
1532:
1526:
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1497:
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1490:
1462:
1456:
1455:
1453:
1452:
1443:. Archived from
1433:
1427:
1426:
1424:
1423:
1414:. Archived from
1404:
1398:
1397:
1380:(5): 3051–3058.
1365:
1359:
1358:
1322:
1316:
1315:
1305:
1265:
1259:
1258:
1248:
1216:
1210:
1209:
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1142:
1110:
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1103:
1069:
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660:
649:
648:
619:
613:
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570:
561:
560:
532:
521:
520:
510:
487:Chemical Science
478:
472:
471:
461:
429:
414:
413:
411:
410:
396:
390:
389:
379:
362:(8): 2892–2899.
347:
338:
337:
327:
317:
293:
272:
269:
2410:
2409:
2405:
2404:
2403:
2401:
2400:
2399:
2385:
2384:
2383:
2378:
2310:
2294:
2278:
2236:
2217:
2200:
2191:
2166:
2156:
2114:
2109:
2100:
2098:
2085:
2084:
2080:
2041:
2040:
2036:
2027:
2025:
2017:
2016:
2012:
2003:
2001:
1992:Mulligan, Tom.
1991:
1990:
1986:
1977:
1975:
1962:
1961:
1957:
1944:
1943:
1934:
1890:
1889:
1885:
1862:(10): 2738–49.
1849:
1848:
1844:
1791:
1790:
1786:
1777:
1775:
1767:
1766:
1762:
1741:(15): 6553–60.
1732:
1731:
1727:
1683:
1682:
1675:
1629:
1628:
1621:
1612:
1610:
1597:
1596:
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1529:
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1111:
1107:
1067:
1062:
1061:
1054:
1002:
1001:
988:
953:Cancer Research
946:
945:
936:
896:
891:
890:
881:
849:
844:
843:
839:
801:
800:
796:
752:
751:
747:
724:(13): 5406–20.
711:
710:
706:
662:
661:
652:
621:
620:
616:
572:
571:
564:
534:
533:
524:
480:
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2023:www.avacta.com
2010:
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1690:Molecular Cell
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1642:(1): E72–E81.
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1603:www.avacta.com
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1569:www.avacta.com
1556:
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1508:(9): 3314–20.
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1473:(3): 1089–96.
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1441:www.avacta.com
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631:(9): 751–63.
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2333:
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2206:Fab fragment
2177:
2099:. Retrieved
2095:the original
2090:
2081:
2048:
2044:
2037:
2026:. Retrieved
2022:
2013:
2002:. Retrieved
1998:the original
1987:
1976:. Retrieved
1972:the original
1967:
1958:
1949:
1900:
1897:EMBO Reports
1896:
1886:
1859:
1855:
1845:
1802:
1798:
1787:
1776:. Retrieved
1772:
1763:
1738:
1734:
1728:
1693:
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1639:
1635:
1611:. Retrieved
1607:the original
1602:
1577:. Retrieved
1573:the original
1568:
1559:
1548:. Retrieved
1544:the original
1539:
1530:
1505:
1501:
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1470:
1466:
1460:
1449:. Retrieved
1445:the original
1440:
1431:
1420:. Retrieved
1416:the original
1411:
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1377:
1373:
1363:
1330:
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1320:
1277:
1274:RSC Advances
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1214:
1171:
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1008:
956:
952:
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900:
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840:
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807:
804:FEBS Letters
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762:
759:FEBS Letters
758:
748:
731:10.2741/3089
721:
717:
707:
672:
668:
628:
624:
617:
582:
578:
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407:. Retrieved
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267:
245:
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217:
206:
203:Therapeutics
182:
174:
171:Applications
154:
150:
136:fluorophores
133:
125:
112:
108:
99:
87:
56:
45:
27:
26:
2158:Engineered
1327:The Analyst
1174:(1): 6572.
1015:(1): 9608.
444:: 607–613.
236:, both via
79:alpha-helix
53:Development
2266:bispecific
2224:bispecific
2179:bispecific
2101:2018-10-22
2028:2018-10-22
2004:2018-10-22
1978:2018-10-22
1778:2018-10-22
1613:2018-10-22
1579:2018-10-19
1550:2018-10-19
1451:2018-10-19
1422:2018-10-19
409:2018-10-18
260:References
209:antibodies
147:Properties
121:antibodies
96:Production
83:beta-sheet
30:are small
2374:nanoCLAMP
2349:Anticalin
2344:Alphabody
2306:Intrabody
1837:247199635
1821:0304-4165
973:0008-5472
224:half-life
143:formats.
71:cystatins
2389:Category
2369:Monobody
2073:35622552
2065:26312879
1927:29467282
1878:26135796
1829:35240235
1755:22789061
1720:28943312
1668:29247053
1522:19320493
1487:17263340
1394:28192970
1355:27704086
1312:27019702
1255:28421739
1206:29700342
1149:28752365
1100:46950252
1092:29873161
1047:28852111
981:81376936
921:29482002
874:28217789
832:40444629
789:40605067
740:18508595
699:24668773
645:21616931
609:20179045
557:16139842
517:29861896
468:26897263
386:30005571
334:28654419
113:In vitro
109:in vitro
32:proteins
2339:Affitin
2334:Affimer
2329:Affilin
1918:5891417
1711:5640506
1659:5776790
1335:Bibcode
1303:4786947
1282:Bibcode
1246:5432960
1197:5920084
1176:Bibcode
1140:5578921
1038:5575301
1017:Bibcode
929:3549374
907:: 1–8.
824:1855589
781:1993479
690:4000234
600:2851446
508:5949846
459:4785862
377:6079930
325:5487212
246:ex vivo
227:in vivo
220:albumin
213:tumours
129:avidity
2359:DARPin
2354:Avimer
2214:F(ab')
2118:Avacta
2091:Avacta
2071:
2063:
2045:Lancet
1968:Avacta
1925:
1915:
1876:
1835:
1827:
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1540:Avacta
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1412:Avacta
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332:
322:
234:cancer
155:These
46:E.coli
2069:S2CID
1833:S2CID
1096:S2CID
1068:(PDF)
977:S2CID
925:S2CID
897:(PDF)
850:(PDF)
828:S2CID
785:S2CID
302:eLife
238:CAR-T
185:ELISA
140:c-Myc
36:mimic
2162:and
2061:PMID
1923:PMID
1874:PMID
1825:PMID
1817:ISSN
1803:1866
1751:PMID
1716:PMID
1664:PMID
1518:PMID
1483:PMID
1390:PMID
1351:PMID
1308:PMID
1251:PMID
1202:PMID
1145:PMID
1088:PMID
1043:PMID
969:ISSN
917:PMID
870:PMID
820:PMID
777:PMID
736:PMID
695:PMID
641:PMID
605:PMID
553:PMID
513:PMID
464:PMID
382:PMID
330:PMID
254:PDL1
2053:doi
2049:385
1913:PMC
1905:doi
1864:doi
1807:doi
1743:doi
1706:PMC
1698:doi
1654:PMC
1644:doi
1640:115
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1475:doi
1382:doi
1343:doi
1331:141
1298:PMC
1290:doi
1241:PMC
1233:doi
1192:PMC
1184:doi
1135:PMC
1127:doi
1080:doi
1033:PMC
1025:doi
961:doi
909:doi
905:108
862:doi
812:doi
808:285
767:doi
763:278
726:doi
685:PMC
677:doi
633:doi
595:PMC
587:doi
545:doi
541:352
503:PMC
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454:PMC
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372:PMC
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320:PMC
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