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1 Fab 5F10 fixes the B domain rigidly to the surface of th
2 Fab fragment of TRC105, a mAb that specifically binds to
3 Fab fragments of PG102, while retaining CD40 binding, di
4 Fab-7 boundary activity is known to depend on factors th
6 MET crystal structure shows that the 107_A07 Fab comes into close proximity with the HGF/SF-binding S
9 dence time of the anti-IL-17A and anti-IL-13 Fab' fragments in the lungs but PEGylation was able to p
10 f delivery of the anti-IL-17A and anti-IL-13 Fab' fragments within the lungs had a major impact on th
11 s residence time as well and the anti-IL-17A Fab' benefited more from PEGylation than the anti-IL-13
13 Finally, using I(125)-labeled anti-IL-17A Fab', we showed that the protein fragment hardly penetra
14 we determined the crystal structure of 2424 Fab in complex with a JRFL V3 peptide and showed that th
16 esolution structure of the DBLbeta3_D4::24E9 Fab complex derived from small-angle x-ray scattering.
17 n X-ray crystal structure of an FcRn-DX-2507 Fab complex, revealing a nearly complete overlap of the
20 , we determined the crystal structure of 5G6 Fab fragment in complex with its epitope peptide KL10 (G
23 inding to BMS-986010 (which contains the 7B7 Fab, where Fab is fragment antigen-binding region of an
24 al structure of the complex between C5 and a Fab fragment with the same sequence as eculizumab at a r
25 ostatin, proteins, and antibodies, such as a Fab arm of the antibody Herceptin and a designed antibod
29 cosahedral 3-fold axes prevents binding of a Fab to the third domain III of each E protein spike.
30 rowth factor) and two monovalent proteins (a Fab fragment and the transcription factor TBP) with low
31 EGF/angiopoietin 2 antibody with dual action Fab (DAF) as a potential therapeutic for neovascular age
32 Zr- and (124)I-labeled versions of alphaHER2 Fab-PAS200 allowed PET tumor imaging with high contrast.
34 nd the antigen binding fragments F(ab')2 and Fab) targeting epidermal growth factor receptor were lab
36 o immobilize whole anti-PTHrP antibodies and Fab' fragments to surfaces as biorecognition elements.
37 ation fork with streptavidin (dsDNA end) and Fab (5' ssDNA) we located the positions of these labels
38 t bound to the CD4 peptide mimetic M48U1 and Fab of anti-cluster A antibody N60-i3 revealed no pertur
39 ighly dependent on local tumor perfusion and Fab permeation in the SUDHL-4 and Granta-519 tumors.
42 holo-PDE6 in complex with the ROS-1 antibody Fab fragment was determined by cryo-electron microscopy.
43 ptamine 2B (5-HT2B) receptor and an antibody Fab fragment bound to the extracellular side of the rece
44 interested in the codon usage of an antibody Fab fragment gene exhibiting extreme toxicity in the E.
47 as to use (64)Cu-labeled anti-CD105 antibody Fab fragment for noninvasive assessment of angiogenesis
48 are functionalized with anti MC-LR antibody Fab' fragments for the selective capture of MC-LR from a
49 e-specific labeling of Env-specific antibody Fab with a fluorophore at high efficiency, and 3) optica
54 nning antibody 8ANC195, that can be added as Fabs to a soluble native-like Env trimer to stabilize it
58 cking experiments with an excess of either B-Fab or huDS6 were used to determine the extent of the an
59 pe controls with antilysozyme and anti-DM4 B-Fabs and blocking experiments with an excess of either B
60 x, incorporation of a miniPEG spacer between Fab' and MORF1 and between polymer backbone and pendant
63 f the PG9_N100(F)Y fragment antigen binding (Fab) confirmed that the mutated residue retains the para
64 n complex with fragments of antigen binding (Fabs) from two human monoclonal antibodies, IgG-94 and I
65 iple epitopes for fragments antigen-binding (Fabs) of both antibodies, demonstrating that 3B5H10 does
66 n issue in the development of the biosensor, Fab' fragments should be chosen as they are relatively c
71 functioning of the Bithorax complex boundary Fab-7, interacts specifically with a special class of CE
73 rived autoantibodies against complement C1q (Fab anti-C1q) and von Willebrand factor (VWF) led us to
76 onucleotide (MORF1) attached to an anti-CD20 Fab' fragment (Fab'-MORF1); (2) multiple copies of compl
77 Fab site-specifically conjugated to anti-CD3 Fab using the genetically encoded noncanonical amino aci
79 crystal structure of NA in complex with CD6 Fab reveals a unique epitope, where the heavy-chain comp
83 any platforms for creating bsAbs, controlled Fab-arm exchange (cFAE) has proven useful based on minim
89 ar measurements in the presence of anti-CS20 Fab fragments did not show any effect, indicating that b
90 light-sheet fluorescence microscopy with Cy5-Fab-PAS200 confirmed better tracer extravasation in the
91 of the complex between an omalizumab-derived Fab and IgE-Fc, with one Fab bound to each C3 domain.
92 tope-labeled, protease-cleaved, mAb domains (Fab and Fc) has been demonstrated from both E. coli and
95 t TrR1 tumors were treated with (177)Lu-DOTA-Fab-PEG24-EGF or (111)In-DTPA-Fab-PEG24-EGF at the NOAEL
96 was measured after exposure to (177)Lu-DOTA-Fab-PEG24-EGF or (111)In-DTPA-Fab-PEG24-EGF or to monosp
98 The maximum injected amount of (177)Lu-DOTA-Fab-PEG24-EGF that caused no observable adverse effects
103 ormal tissue biodistribution of (177)Lu-DOTA-Fab-PEG24-EGF was studied at 48 h after injection in ath
104 h (177)Lu-DOTA-Fab-PEG24-EGF or (111)In-DTPA-Fab-PEG24-EGF at the NOAEL, or with unlabeled immunoconj
105 or growth more effectively than (111)In-DTPA-Fab-PEG24-EGF because of a 9.3-fold-higher radiation-abs
106 o (177)Lu-DOTA-Fab-PEG24-EGF or (111)In-DTPA-Fab-PEG24-EGF or to monospecific (177)Lu- or (111)In-lab
109 bodies requires the engineering of effective Fab libraries guided by the knowledge of the principles
110 We show in a crystal structure that ESK1 Fab binds to RMF/HLA-A*02:01 in a mode different from th
111 function appropriately when substituted for Fab-7: it blocks crosstalk but does not support bypass.
114 te residing in the antigen-binding fragment (Fab or Fv) is an autonomous and complete unit for antige
115 SOSIP.664 with the antigen-binding fragment (Fab) of PGT145, a broadly neutralizing quaternary-struct
116 e influence of the antigen-binding fragment (Fab) on FcRn interactions has been reported, the underly
118 RF1) attached to an anti-CD20 Fab' fragment (Fab'-MORF1); (2) multiple copies of complementary oligon
119 dopt a methodology using antibody fragments (Fab) conjugated to gold nanoparticles (immunogold) to ma
120 odified alphaCD20 antigen-binding fragments (Fab), prepared by PASylation with a 200-residue polypept
121 ombinant antibody antigen-binding fragments (Fab), that is specific for HT-2 toxin and has a positive
122 matted as soluble antigen-binding fragments (Fab), these clones expressed well, were predominantly mo
123 Crystal structures of antibody fragments (Fabs) 311 and 317 with an (NPNA)3 peptide illustrate the
124 ed a series of synthetic antibody fragments (Fabs) against different conformations of betaarrs from p
125 ody derivatives, such as antibody fragments (Fabs) and single-chain variable fragments (scFvs), are n
126 re we describe synthetic antibody fragments (Fabs) as structural and biochemical probes to investigat
127 play library to engineer antibody fragments (Fabs) that can modulate the activity of the enzyme isoci
128 bes have been largely thought to result from Fab-antigen interactions, recent studies suggest that re
134 ependent antibodies in chimeric rabbit/human Fab format and validated it by next-generation sequencin
139 d when the CD20-specific radiotracers (125)I-Fab-ABD and (125)I-Fab-PAS200 were applied (respective p
140 cific radiotracers (125)I-Fab-ABD and (125)I-Fab-PAS200 were applied (respective percentages injected
141 monovalent hapten and recombinant SPE-7 IgE Fab inhibit its cytokinergic activity as measured by mas
143 given to show the versatility of immobilized Fab' fragments in different applications and future dire
144 binds to several BX-C boundaries, including Fab-7 and Mcp To study Pita functions, we have used a bo
145 s and antibody-derived constructs (including Fab, Fc-fusions and bispecifics) in mammalian cells.
146 engineered hinge domain of IgG3 to increase Fab domain flexibility necessary for hetero-bivalent bin
147 ion considerably reduced toxicity, increased Fab expression from negligible levels to 10 mg/l, and re
148 e demonstrate that the antibody NT4X and its Fab fragment reacting with both the free N-terminus of A
151 In the case of the AD-2S1 peptide, the KE5 Fab fragment complex identified nine germline-encoded co
153 ation was found to be associated with its M1 Fab that activates the alternative pathway in an Fc-inde
154 IT consisting of a humanized anti-mesothelin Fab fused to domain III of Pseudomonas exotoxin A, in wh
157 plexes display a compact rsCSP with multiple Fabs bound, with the rsCSP-Fab311 complex forming a high
158 ographic and competition binding analyses of Fab fragments and scFvs defined three spatially distinct
164 tremendous progress in the immobilization of Fab' fragments onto gold, Si-based, polysaccharide-based
166 nd 3D electron microscopy reconstructions of Fab-trimer complexes revealed a horizontal binding angle
167 This review will show the current scope of Fab' immobilization techniques available and illustrate
173 an unusually extensive aromatic cage in one Fab and the histone N terminus to a pocket in the other,
175 e antibodies/ethanolamine) and one optimized Fab' fragment-based surface (TUBTS/Fab' fragments) were
177 atic, exposure of V. cholerae to 2D6 IgA (or Fab fragments) resulted in a 5-fold increase in surface-
178 e generated that consist of anti-Her2 IgG or Fab site-specifically conjugated to anti-CD3 Fab using t
179 e was directly blocked by either PA50 mAb or Fab and suggested that receptor blockade is the mechanis
185 We prepared the antibody mimetic Fab-PEG-Fab (FpFinfliximab) for direct intravitreal injection to
187 olved in the prolonged presence of PEGylated Fab' in the airway lumen might include binding to the mu
188 ssment of FR104 (n=5), a selective pegylated Fab' antibody fragment antagonist of CD28 that does not
189 mpared to the ligand-free trimer, the PGT145 Fab-BG505 SOSIP.664 complex displayed increased melting
192 was validated using previously recalcitrant Fab-antigen complexes where introduction of an engineere
194 ent on the heavy chain (HC) variable region (Fab) and the other present on the conserved HC constant
199 fied by PG9, bind asymmetrically as a single Fab to the apex of the symmetric Env trimer using a prot
201 hes that consist of a tumor antigen-specific Fab molecule engrafted with a peptide neo-epitope, which
204 conformation-, epitope- and domain-specific Fabs, we feel that the CBP tag embodies all the attribut
206 y engineering strategy to generate synthetic Fab variants that significantly reduces elbow flexibilit
209 The near-atomic structure also revealed that Fab binding had caused capsid destabilization in regions
210 the cryo-electron density maps, we show that Fab fragments of antibody 8B10 extend radially from the
219 ing an oriented immobilization approach, the Fab' fragments are covalently attached to gold surface t
220 resolution of 2.5 A of a complex between the Fab fragments of E1 and HM14c10 and provide the first de
221 resolution of 2.5 A of a complex between the Fab fragments of E1 and HM14c10 provides the first detai
222 ll molecules is demonstrated, as binding the Fab to the capsid allowed us to determine the 50-kDa Fab
223 n of individual glycan species from both the Fab and Fc N-Linked glycosylation sites is consistent wi
224 ure of the nAChR alpha1 subunit bound by the Fab fragment of mAb35, a reference monoclonal antibody t
225 s(-1) over preformed fibrin-rich clots, the Fab 9O12 decreased the recruitment of platelets by up to
226 rategy by substituting modified DNAs for the Fab-7 boundary, which is located between the iab-6 and i
228 dy with single residue pair mutations in the Fab region to promote efficient and stable cognate light
236 " by E1 by increasing its recognition of the Fab HM14c10 light chain CDRs.IMPORTANCE A chimeric yello
237 and determined the crystal structure of the Fab in complex with its target, which identifies the bin
238 d-Fab complex map showed that binding of the Fab induced significant conformational changes that were
239 urine IgE, we reveal that interaction of the Fab region of 'free' SPE-7 IgE with the Fab of Fcepsilon
240 onal antibodies to be the CDR H3 loop of the Fab region, and show that they all have nano to micromol
243 t increase in thermodynamic stability of the Fab, a feature predicted by the computational model.
244 ink the constant and variable domains of the Fab, can introduce disorder and thus diminish their effe
247 alactose-alpha-1,3-galactose, located on the Fab region of cetuximab, was identified as the target re
251 coupling of antigen specificity through the Fab domain to signal transduction via Fc-Fc receptor int
252 ity capture of human IgGs via binding to the Fab region, followed by on-bead IdeS digestion to remove
253 l means of antigen recognition, in which the Fab fragment of an antibody acts as an adaptor, linking
255 /2013, French Polynesia) in complex with the Fab fragment of a highly therapeutic and neutralizing hu
256 ies of the GI.1 P domain in complex with the Fab fragment of a human IgA monoclonal antibody (IgA 5I2
258 the Fab region of 'free' SPE-7 IgE with the Fab of FcepsilonRI-bound SPE-7 IgE is the basis of its c
260 Yersinia pestis were characterised for their Fab affinity against the purified protein and their Fc a
261 lographically determined structures of these Fab fragments into the cryo-electron density maps, we sh
262 form sampling techniques, we show that these Fab and Fc fingerprint spectra can be rapidly acquired i
263 models suggest two mechanisms for how these Fabs may prevent the conversion of PrP(C) into PrP(Sc).
266 nces between rHBeAg and HBeAg, we used these Fabs in microscale immunoaffinity chromatography to puri
268 been shown to be antigenic when attached to Fab oligosaccharides of monoclonal antibodies (mAbs) , w
269 e late boundary complex (LBC), that binds to Fab-7 sequences that have insulator functions in late em
270 across a series of antibody fragments (VL to Fab), and subsequently, the DCM was combined with molecu
273 fic (177)Lu- and (111)In-labeled trastuzumab Fab or EGF killed tumor cells that predominantly express
275 and EGFR on BC cells by linking trastuzumab Fab fragments through a polyethylene glycol (PEG24) spac
281 as well as their complexes with each of two Fab fragments (HuM-P and HuM-R1), which recognize N- and
282 one and pendant MORF2, and comparison of two Fab' fragments, one from 1F5 antibody (Fab'1F5), the oth
283 recognition by the new bNAb BG1 in which two Fabs bind asymmetrically per Env trimer using a compact
284 structures of the complexes of IL-6 with two Fabs derived from conventional camelid antibodies that a
285 l properties, such as the ability to undergo Fab-arm exchange and limit immune complex formation.
287 ), followed by dual enzymatic labeling using Fab fragments of anti-Dig and anti-FITC conjugated to pe
288 effects of these changes on cell viability, Fab yield and display on filamentous phage using differe
290 whereas the IgG4 isotype can undergo in vivo Fab arm exchange leading to bispecific antibody and off-
291 ZM197M SOSIP.664 trimer complexed with VRC01 Fab against the CD4 binding site at subnanometer resolut
292 MS-986010 (which contains the 7B7 Fab, where Fab is fragment antigen-binding region of an antibody),
293 ermined the structure of CPV in complex with Fab E to 4.1 A resolution, which allowed de novo buildin
294 structures of the allergens in complex with Fab fragments of three murine mAbs that interfere with I
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