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1 agonist BU72 and a G protein mimetic camelid antibody fragment.
2 ation rates of T cells independent of the Fc antibody fragment.
3 y a nonionic detergent and complexed with an antibody fragment.
4  compared with mGluR1 IgG fused to a control antibody fragment.
5 ceptor site has been shown to be accessed by antibody fragments.
6 fragments, CD4 mimetic proteins, and various antibody fragments.
7 e for the observed dual specificity of these antibody fragments.
8 echanisms, in general, and for single-domain antibody fragments.
9 r the innate (un-accelerated) aggregation of antibody fragments.
10 ify putative allosteric sites in a series of antibody fragments.
11 and full-length antibody, as well as smaller antibody fragments.
12                                 The anti-DNA antibody fragment 3E10 Fv has received attention as a no
13 DS6 were used to determine the extent of the antibody fragment (64)Cu-DOTA-B-Fab binding specificity.
14                                          The antibody fragment (64)Cu-DOTA-B-Fab was more than 95% st
15 ine residues with photocaged tyrosine, in an antibody fragment, 7D12.
16  monoclonal Fv fragments (3.9 A) and without antibody fragments (8 A).
17 he tumor targeting of an internalizing human antibody fragment, a small-size platform, to provide hig
18 ES domain V (dV) in complex with a synthetic antibody fragment-a crystallization chaperone.
19 noparticles to 'shuttle' a model therapeutic antibody fragment across the epithelial cell layers.
20  contrast to directly labeled antibodies and antibody fragments, administration of the negatively cha
21 pproach can find utility when an antibody or antibody fragment against a known cell line needs to be
22 ive-cell microscopic imaging of single-chain antibody fragments against carcinoembryonic antigen in L
23                             Using monoclonal antibody fragments against nonstructural protein dengue
24    We further demonstrated that single-chain antibody fragments against tumor-specific antigens can b
25                               We show how an antibody fragment-aided single-particle cryo-EM can be a
26                                     Selected antibody fragments allowed specific detection of endogen
27                  Whereas directly conjugated antibodies, fragments and subfragments have shown promis
28 l, we developed a modular system in which an antibody fragment and a cytokine are conjugated via a DN
29 ted by the inhibitory anti-RAS intracellular antibody fragment and did not show any RAS-effector inhi
30  In this study, we developed a CD44-specific antibody fragment and evaluated it for imaging CD44-posi
31  electrode array was functionalised with the antibody fragment and integrated with microfluidics and
32 notoxin B3(dsFv)-PE38 (B3-PE38) in which the antibody fragment and the protein toxin are polyionic li
33  columns, it has become possible to separate antibody fragments and antibody-drug conjugate species i
34 ed for efficient production of BsAb, both as antibody fragments and as full-length IgG-like molecules
35 ular antibody (optobody) consisting of split antibody fragments and blue-light inducible heterodimeri
36 neering the variable and constant regions of antibody fragments and full-length antibodies to resist
37 antibodies, are the smallest antigen-binding antibody fragments and have ideal characteristics for PE
38 ntial reassembly of fusion proteins based on antibody fragments and interleukin-12 subunit mutants.
39 ics include peptides, monoclonal antibodies, antibody fragments and nontraditional binding scaffolds,
40 pproach to PEGylation of cytokines, enzymes, antibody fragments and peptides, without destroying thei
41 eview is provided for monoclonal antibodies, antibody fragments, and variants directed at CXCR4 and A
42 t of FR104 (n=5), a selective pegylated Fab' antibody fragment antagonist of CD28 that does not block
43                               A single-chain antibody fragment (anti-1F12 scFv) was isolated that rec
44 e antibody single-chain Fv fragments (scFv), antibody fragment-antigen binding (Fab') units, and apta
45 of the 5F7 anti-HER2 Nanobody (single-domain antibody fragment; approximately 13 kDa) after (18)F lab
46                    Bispecific antibodies and antibody fragments are a new class of therapeutics incre
47                                        Here, antibody fragments are constructed to target murine CD8
48                                              Antibody fragments are emerging as promising biopharmace
49                                              Antibody fragments are recognized as promising vehicles
50  molecules, in which anti-CD19 and anti-CD22 antibody fragments are site-specifically modified with F
51 unique IDE conformation by using a synthetic antibody fragment as a crystallization chaperone.
52 on and site-specifically labeled recombinant antibody fragments as binders to improve the assay perfo
53 e unique properties of camelid single-domain antibody fragments as structural probes for studying the
54 icase domain in complex with DNA and with an antibody fragment, as well as SAXS and domain associatio
55  hybrid sensor consists of anti-TNT specific antibody fragments attached to a hydrophilic QD via meta
56 ET-MALDI-MS detection, a proof of concept of antibody fragment background reduction in the ISET-MALDI
57                  To generate a dual-modality antibody fragment-based imaging agent, the DML was label
58 uctured nature, specific recognition with an antibody fragment becomes feasible and may help define t
59 thod required additional purification of the antibody fragments before immobilization.
60 ith the TNB recognition element bound in the antibody fragment binding site, bringing the two dyes in
61 We examined the efficacy of idarucizumab, an antibody fragment binding to dabigatran, in a mouse mode
62  a panel of chimeric rabbit/human monoclonal antibody fragments (both Fab and scFv) against rHBeAg.
63 g peptide and another using a fusion with an antibody fragment, both targeting the erythrocyte-specif
64 o offer a new generation of in vitro-derived antibody fragments, both for further engineering as dire
65 n of model analyte cardiac troponin I by two antibody fragments brought the label moieties together a
66 ful detection of antigen with a spin labeled antibody fragment by continuous-wave electron paramagnet
67 protein, which were selectively cleaved into antibody fragments by 2-mercaptoethylamine.
68          Here, we have developed photoactive antibody fragments by genetic site-specific replacement
69 ow, in addition, that the binding of a camel antibody fragment, cAb-HuL6, which was raised against wi
70 the efficacy of a llama-derived, heavy-chain antibody fragment called anti-rotavirus protein (ARP1),
71 yeast-displayed library of synthetic camelid antibody fragments called "nanobodies." Using this platf
72 n inhibitors selected using an intracellular antibody fragment (called Abd compounds).
73 s that contain disulfide bonds, such as scFv antibody fragments, can be translocated via Tat only whe
74               Infusion of these radiolabeled antibody fragments, combined with SPECT, produces clear
75 tide antigen fused to an erythrocyte-binding antibody fragment completely prevented diabetes onset in
76 report the structures of four AAV-monoclonal antibody fragment complexes, AAV1-ADK1a, AAV1-ADK1b, AAV
77 Therefore, pre-conditioning cells to express antibody fragments confers effective intracellular immun
78 ring cost of bacterially expressed PEGylated antibody fragments could provide decisive advantages for
79 T platform that uses a chemically programmed antibody fragment (cp-Fab) as on/off switch.
80              Next, EETI 2.5F was fused to an antibody fragment crystallizable (Fc) domain (EETI 2.5F-
81 d trajectories of two proteins (lysozyme and antibody fragment D1.3) in 4 M glycerol to rigorous stat
82           The results show the importance of antibody fragment density on nanoparticle uptake, and su
83 r a monoclonal antibody and its single-chain antibody fragments derivatives.
84                                        Three antibody fragments derived from huDS6 were produced, pur
85 d by the development of robust high affinity antibody fragments derived from the breast cancer therap
86 San Francisco, CA) is a humanized monoclonal antibody fragment designed to bind all forms of VEGF, th
87 ynamically binding, low-affinity fluorescent antibody fragment differentiates between specific and no
88          (99m)Tc-cAbVCAM1-5, a single-domain antibody fragment directed against mouse or human vascul
89 as also tested using a single-chain variable antibody fragment directed against the FVIII light chain
90 ic agent linked covalently to an antibody or antibody fragment directed toward a specific cell surfac
91 utralizing Nanobodies (single domain camelid antibodies fragment) directed against several chemokines
92           Additionally, the highest-affinity antibody fragment displayed 10-fold-increased broad neut
93 ace plasmon resonance-based immunoassay, the antibody fragment displayed cross-reactivity with seven
94 stems include the selection and evolution of antibody fragments, DNA binding domains, enzymes, intera
95 sized that the smallest independently folded antibody fragments (domains) could exhibit exceptionally
96  show, there is tremendous potential for all antibody fragments either as robust diagnostic reagents
97          Rapid renal clearance of the 50-kDa antibody fragment enables same-day imaging.
98                            Here we show that antibody fragments engineered to recognize the protectiv
99 rate that the topically applied single-chain antibody fragment ESBA105 penetrated into the anterior c
100                       Single-chain Fv (scFv) antibody fragments exhibit improved pharmacokinetics and
101 ion was used for the selection of mutant Fab antibody fragments exhibiting improved expression in the
102 ibility using two domain-specific monoclonal antibody fragments (F(ab)s) isolated from a very large n
103      The SPR partition data obtained for the antibody fragment F63, the HIV fusion inhibitor enfuvirt
104                                           An antibody fragment (Fab) of MAb E was found to neutralize
105 d the energetics of binding of a therapeutic antibody fragment (Fab) to the native and non-native for
106 termined a crystal structure of the COVA1-16 antibody fragment (Fab) with the SARS-CoV-2 receptor-bin
107 opy to correlate the number of antibodies or antibody fragments (Fab) bound to an individual virion w
108   In this work, we adopt a methodology using antibody fragments (Fab) conjugated to gold nanoparticle
109 kungunya virus-like particles complexed with antibody fragments (Fab) of two highly protective human
110  a broad spectrum of neutralizing monoclonal antibody fragments (Fab).
111 y fragments (for example, classic monovalent antibody fragments (Fab, scFv)) and engineered variants
112                   We constructed a synthetic antibody-fragment (Fab) library in the phage-display for
113 pe variants (IgG1, IgG2, IgG3, and IgG4) and antibody fragments [Fab, F(ab')(2)] were expressed in Ch
114  used a conformationally selective synthetic antibody fragment (Fab30) that recognizes the phosphopep
115  structure of natural BfAChE in complex with antibody fragment Fab410.
116                        Crystal structures of antibody fragments (Fabs) 311 and 317 with an (NPNA)3 pe
117     Here we identified a series of synthetic antibody fragments (Fabs) against different conformation
118                Antibody derivatives, such as antibody fragments (Fabs) and single-chain variable frag
119                   Here we describe synthetic antibody fragments (Fabs) as structural and biochemical
120 -diversity phage display library to engineer antibody fragments (Fabs) that can modulate the activity
121                    By using rational design, antibody fragments (Fabs) that mimic thrombopoietin (TPO
122                 We have previously described antibody fragments (FABs) that recognize activated betaa
123              Radiolabeling of antibodies and antibody fragments facilitates the development of new ta
124 ispecific antibodies in which a BBB-crossing antibody fragment FC5 was used as a BBB carrier.
125                           Examining the half antibody fragments for detection of the pathogen in the
126 uction of other disease-targeting bispecific antibody fragments for early detection and diagnosis of
127 versatile platform for generating bispecific antibody fragments for redirected killing and, with the
128 acle is to tether cytokines to antibodies or antibody fragments for targeted cell delivery.
129                          Smaller recombinant antibody fragments (for example, classic monovalent anti
130 ) and feline parvovirus (FPV) complexed with antibody fragments from eight different neutralizing mon
131 xpression of an anti-digoxin single-chain Fv antibody fragment fused to the C terminus of ClyA result
132 levels of recombinant VHH or single-chain Fv antibody fragments fused to the human immunoglobulin G1-
133 -galactosidase intracellular single chain Fv antibody fragment, fused to inactive procaspase-3, induc
134      The crystal structure of LMO2 with this antibody fragment has been solved revealing a conformati
135 Pseudomonas aeruginosa and a cancer-specific antibody fragment, has been developed to manage cancer,
136             Monoclonal antibodies (mAbs) and antibody fragments have become an emerging class of ther
137                                   Engineered antibody fragments have been developed with the appropri
138                                              Antibody fragments have been forged into multivalent and
139                                        These antibody fragments have great potential for diagnosis an
140               Antigranulocyte antibodies and antibody fragments have limitations and are not widely a
141 ts include the approved humanized monoclonal antibody fragment idarucizumab for reversing the effects
142 lysine epitopes or the human single-chain Fv antibody fragment IK17 targeted to MDA-like epitopes ("t
143 mphipathic helix that makes contact with the antibody fragment in such a way that the hydrophobic fac
144 old more sensitive detection of human Vkappa antibody fragments in ELISA.
145       The current trend of using recombinant antibody fragments in research to develop novel antidote
146 published methods, we assembled two parental antibody fragments in the hinge region by the protein tr
147  of anti-interleukin (IL)-17A and anti-IL-13 antibody fragments in the lungs and to improve their the
148  that affect the residence time of PEGylated antibody fragments in the lungs following pulmonary deli
149 ants in complexes with conformation-specific antibody fragments in the outward-open and inward-open s
150            In this study, small and bivalent antibody fragments, including anti-prostate-specific mem
151  By assembling and testing several anti-CD20 antibody fragment-interferon ?
152 ic conjugation to a cysteine residue-bearing antibody fragment, introduction of a commercially availa
153                                          The antibody fragment is a tool for dissecting LMO2 function
154 in we describe a novel approach in which the antibody fragment is tagged with two handles: one for th
155 or stabilized by a G-protein mimetic camelid antibody fragment isolated by conformational selection u
156 etection of a chemical flame retardant using antibody fragments isolated from an alpaca has been deve
157 cal characterization of an oligomer-specific antibody fragment, KW1.
158                   Antibodies, and engineered antibody fragments, labeled with radioisotopes are being
159 r, compared with full-size antibodies, these antibody fragments lack the ability to bind the neonatal
160  of allergen-specific IgE with combinatorial antibody fragment library technology to analyze immunogl
161 ibodies into Fab, scFv or even single-domain antibody fragments like VHHs will be reviewed.
162 used to treat cancer that are composed of an antibody fragment linked to a toxin.
163 ortantly, our results suggest that PEGylated antibody fragments may represent a unique approach for m
164               These results demonstrate that antibody fragment mediated proteolytic degradation of Ab
165 ies of an iodinated anti-p185HER2 engineered antibody fragment [minibody (scFv-C(H)3)2; 80 kDa], made
166 using (89)Zr-labeled PEGylated single-domain antibody fragments (nanobodies or VHHs), to explore the
167                 Here we develop single-chain antibody fragments (nanobodies) against tubulin to achie
168                       We generated a camelid antibody fragment (nanobody) to the human beta(2) adrene
169 tabilizing the receptor with a single-domain antibody fragment ("nanobody") discovered using a synthe
170         We show for the first time that half antibody fragments obtained by reduction via tris(2-carb
171 ent regions of the antibody from analysis of antibody fragments obtained from FabRICATOR digestion.
172 es to half-life extenders such as monoclonal antibodies, fragments of antibodies, and albumin.
173 usly been reported that several single-chain antibody fragments of human origin (scFv) neutralize the
174  timing of maximum binding of each anti-PSMA antibody fragment on the cell surface in vivo in mice be
175 led sequential assembly of biotin-engineered antibody fragments on a streptavidin scaffold with a def
176 ne (CRH) based on the immobilization of half-antibody fragments on gold nanoparticles (AuNp).
177                The expression of recombinant antibody fragments on the surface of mammalian cells has
178 at the structural differences of immobilized antibodies (fragmented or intact) significantly influenc
179  an azide-modified fluorescent single-domain antibody fragment or an intact immunoglobulin produced i
180 alysis of LRP6(1-4) bound to a noninhibitory antibody fragment or to full-length Dkk1 shows that in b
181 ular, and site-specific methods for coupling antibody fragments or bioactive proteins to nucleic acid
182 ithout the binding of conformation-selective antibody fragments or inhibitors, the resting ABCG2 adop
183 PET/SPECT) of cancer with radiometal-labeled antibody fragments or peptides is hampered by low tumor-
184 e applied to accurately predict antibody and antibody fragment penetration distance in tumor tissue.
185 he smallest fully functional antigen-binding antibody fragments possessing ideal properties as probes
186 argeting vectors for TRT include antibodies, antibody fragments, proteins, peptides, and small molecu
187 V gp120 and its complexes with receptors and antibody fragments provide high-resolution pictures of s
188 s used to deliver a recombinant single-chain antibody fragment rabbit intrabody (pAd-2S03) capable of
189 n which scTRAIL was additionally fused to an antibody fragment recognizing epidermal growth factor re
190 en-specific monoclonal antibodies (mAbs) and antibody fragments relies on high-throughput screening o
191 re into the binding site of an EGFR-specific antibody fragment, resulting in quantifiable EGFR-depend
192 he nonpathogenic wild strain showed that the antibody fragments retained their specific antigen bindi
193         Idarucizumab, a humanized monoclonal antibody fragment, reverses dabigatran anticoagulation.
194            The resulting chemically modified antibody fragment, RGD-Man(5)-IgG1 Fc (5), retained biol
195              Cargos in the form of synthetic antibody fragments (sABs) were conjugated to the enginee
196      The 4M5.3 anti-fluorescein single chain antibody fragment (scFv) contains 14 mutations from the
197                 Here, we used a single-chain antibody fragment (scFv) derived from the anti-nucleosom
198 s-driven mathematical model for single-chain antibody fragment (scFv) folding in Saccharomyces cerevi
199  of a novel internalizing human single chain antibody fragment (scFv) labeled with ((9)(9)m)Tc (((9)(
200 n consisting of an idiotypic single chain Fv antibody fragment (scFv) linked to a cytokine (GM-CSF) o
201  molecular design of a single chain variable antibody fragment (scFv) that binds with high affinity t
202 ifferentiation 3 (CD3)-specific single-chain antibody fragment (scFv), effectively redirected T cells
203 ed gold cluster (MPC) with a single chain Fv antibody fragment (scFv), mutated to present an exposed
204      A prostate tumor-targeting single-chain antibody fragment (scFv), UA20, along with a nonbinding
205 n particular, smaller, single-chain-variable antibody fragments (scFv's) are attractive for detecting
206 inimal functional unit (i.e., a single-chain antibody fragment [scFv]) is an effective strategy for r
207 sed to a high-affinity anti-fluorescein scFv antibody fragment (scFvFITC).
208                                 Single-chain antibody fragments (scFvs) are first isolated from an ex
209  of human-based single chain variable domain antibody fragments (scFvs) directed against the Abeta 25
210         We were able to isolate single chain antibody fragments (scFvs) from a phage displayed antibo
211 11 unique human single-chain variable region antibody fragments (scFvs) that bind the envelope protei
212  composed of a few neutralizing single chain antibody fragments (scFvs) that bind to two different ep
213 arge phage display libraries of single-chain antibody fragments (scFvs), the three-stage approach tha
214 esigning (18)F-labeled camelid single-domain antibody fragments (sdAbs) specifically targeting the ma
215 ovided an insight into understanding how the antibody fragments self-assemble on the QD.
216 nteraction provides a way of controlling the antibody fragment serum half-life without compromising e
217  crystal structure in complex with a camelid antibody fragment show that the doublecortin C-terminal
218  assignments for two distinct, high affinity antibody fragments (single chain variable and antigen-bi
219                                  This yields antibody fragments so small as to be considered peptides
220 nding domain (ABD) and a llama single-domain antibody fragment specific for mouse and human serum alb
221                       A single chain camelid antibody fragment specific for the C-terminal doublecort
222              We evaluated a small engineered antibody fragment specific for the HER2 receptor tyrosin
223 recently found that a CAR composed of a scFv antibody fragment specific for the Tn-glycoform of MUC1
224                  We developed alpaca-derived antibody fragments specific for mouse class II MHC and C
225 ty trade-offs, we have selected single-chain antibody fragments specific for the negatively charged a
226    These findings for diverse antibodies and antibody fragments specific for unrelated antigens sugge
227 mass spectrometry reveal that binding of the antibody fragment strongly inhibits the locally cooperat
228                    Site-selectively modified antibody fragments such as the one described here may be
229                                Single domain antibody fragments, such as camelid-derived VHHs, can se
230                                   Engineered antibody fragments, such as diabodies, minibodies, and s
231             Here we show that a single chain antibody fragment (syn-10H scFv) isolated from a phage d
232    In August 2012, ranibizumab, a monoclonal antibody fragment targeting VEGF designed for ocular use
233 of mAbs, single-domain antibodies, and other antibody fragments targeting CXCR4 and ACKR3, formerly r
234 ollowing engagement by a bivalent engineered antibody fragment that binds CD37 and activates both SHP
235                 Idarucizumab is a monoclonal antibody fragment that binds dabigatran with high affini
236 e evaluated intravenous PB2452, a monoclonal antibody fragment that binds ticagrelor with high affini
237 blockading RAS-effector interactions with an antibody fragment that binds to activated RAS, and show
238 mation of this complex using a single domain antibody fragment that inhibits LMO2 by sequestering it
239 he sensor consists of a dye-labeled anti-TNT antibody fragment that interacts with a cofunctional sur
240 ch the tumor cell specificity of a humanized antibody fragment that recognizes CD3 on T cells is chem
241 C precursors was rescued via tethering to an antibody fragment that specifically binds the human RBC
242 ution, we engineered a high-affinity camelid antibody fragment that stabilizes the active state of th
243                                     By using antibody fragments that are specific to the target biomo
244  evolutionary strategy to isolate monovalent antibody fragments that bridge together two different re
245  use of chemically or genetically engineered antibody fragments that can be attached to the sensor su
246       Nanobodies are 12-15 kDa single-domain antibody fragments that can be delivered by inhalation a
247 ew generation of radiolabeled antibodies and antibody fragments that can be used as cancer-specific i
248  imaging based on cell surface expression of antibody fragments that can irreversibly bind to radiome
249                                Intracellular antibody fragments that interfere with molecular interac
250                   Here, we have screened for antibody fragments that recognize the tumor-specific gly
251 odies are noncovalent dimers of single-chain antibody fragments that retain the avidity of intact IgG
252 selection strategy for conformation specific antibody fragments that stimulate procaspase activity, s
253 ory assays require the use of antibodies and antibody fragments that strongly bind to their cell surf
254 ary in the phage-display format and isolated antibody-fragments that bind pMHC with high affinity and
255 ctural changes in a native humanized Fab A33 antibody fragment, that correlated with the experimental
256              Anti-fibers as well as anti-PAO antibodies fragment the amyloid fibers, however the frag
257 bitors were sequestered with an anti-digoxin antibody fragment, the sodium excretion rates in the oua
258 ating the size and format of anti-p185(HER2) antibody fragments, the kidney activity was reduced and
259  to the coreceptor-binding region by smaller antibody fragments, the single-domain (VHH) version of J
260     Rabbit anti-RANKL IgG antibody or F(ab') antibody fragments thereof were injected into the palata
261 e have isolated an anti-LMO2 single chain Fv antibody fragment to determine if intracellular interfer
262 demonstrate that using a unique GTP-specific antibody fragment to monitor GTPase cycling in the prese
263               The binding of this engineered antibody fragment to the amyloidogenic variants of lysoz
264 f the fragment with a PEG moiety or a second antibody fragment to tune its circulatory half-life or i
265  relative binding capabilities of antibodies/antibody fragments to cell surface targets on the bencht
266 ate the use of luminescent QDs conjugated to antibody fragments to develop solution-phase nanoscale s
267 roperties of synthetic receptor ligands with antibody fragments to develop useful biochemical tools a
268 adiolabeled small molecules, antibodies, and antibody fragments to image the tumor microenvironment,
269 These results support the use of recombinant antibody fragments to inhibit NS3 enzyme as a novel, fea
270 GF-beta, as well as two different inhibitory antibody fragments to understand the structural underpin
271 ter, with and without the cocrystallized Fab antibody fragment, to investigate the properties of this
272 erized a caffeine-specific, heavy-chain-only antibody fragment (V(HH)) from llama that is capable of
273 ody, AB1, using just a homology model of the antibody fragment variable region and a protein-protein
274 display technology to identify single-domain antibody fragments (VHH) that bind the LRP6 P3E3P4E4 reg
275                Camelid-derived single-domain antibody fragments (VHHs or nanobodies) offer a possible
276 , have been truncated to yield single-domain antibody fragments (VHHs or nanobodies) that overcome ma
277 ted a panel of camelid-derived single-domain antibody fragments (VHHs) against influenza virus nucleo
278  used (89)Zr-labeled PEGylated single-domain antibody fragments (VHHs) specific for CD8 to track the
279           From a library of heavy chain-only antibody fragments (VHHs), we isolated an antibody (1B7)
280 michannels that were liganded by Fab-epitope antibody fragments via atomic force microscopy.
281 M can be robustly applied across a series of antibody fragments (VL to Fab), and subsequently, the DC
282 rental clone the resultant affinity-enhanced antibody fragment was applied in an optimized fluorescen
283                                          The antibody fragment was, however, not stable enough under
284                             Idarucizumab, an antibody fragment, was developed to reverse the anticoag
285                   Idarucizumab, a monoclonal antibody fragment, was developed to reverse the anticoag
286 gen-binding activity of a human single-chain antibody fragment were simultaneously improved.
287                                              Antibody fragments were predominately located within the
288                                        Three antibody fragments were produced and examined as potenti
289 iple, nanorobots loaded with combinations of antibody fragments were used in two different types of c
290                      These carbohydrate-free antibody fragments were used to bind the glycoprotein ho
291   Our study provided a novel monoclonal scFv antibody fragment which specifically bound to HSP60 of S
292 rian cancer using a yeast-display library of antibody fragments, while subtracting those that bind to
293  to study a model system consisting of a Fab antibody fragment with specificity toward the peptide ab
294                  Radioiodinated antibody and antibody fragments with (125)I were used to determine th
295 ingle domains represent a promising class of antibody fragments with applications as therapeutic moda
296 positive cancer cells, as well as multimeric antibody fragments with enhanced activity.
297 ovide guidelines for designing other grafted antibody fragments with hydrophobic binding loops.
298 logies is expected to include antibodies and antibody fragments with novel mechanisms of action and e
299                                              Antibody fragments with optimized pharmacokinetic profil
300 gation away from the antigen-binding site of antibody fragments, with a controlled linker-to-protein

 
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