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  • VRC01
  • Of the three amino acids in the VH1-2*02 gene segment that define a motif for VRC01-like antibodies (W50, N58, flanking the HCDR2 region, and R71), the two identified macaque VH1.23 alleles described here encode two. (iavi.org)
  • Also unlike VRC01, GE356 was minimally modified by somatic hypermutation, its light (L) chain CDRs were of average lengths and it displayed a binding footprint proximal to the trimer axis. (iavi.org)
  • molecule
  • The antibodies bind to a variety of sites on the myosin-II molecule, including the heads, the proximal end of the tail near the junction of the heads and tail, and the tip of the tail. (duke.edu)
  • This demonstrates that antibodies can inhibit polymerization of myosin-II, but only when they bind to key sites on the tail of the molecule. (duke.edu)
  • bulky
  • One of the antibodies, 4A1, has a relatively high activity for the substrate having a bulky group. (ovid.com)
  • To determine the amino acid residues related to the binding of the bulky group, we determined the amino acid sequences of VL and VH regions of 4A1 by the cycle sequencing method, built the three-dimensional structure of the V regions, labeled 4A1 with [14C]phenyl glyoxal in the presence and absence of I-1 or I-13, and analyzed the labeled incubation mixture with SDS-PAGE. (ovid.com)
  • From these results, the possibility that Arg-H28 of the heavy chain is involved in binding the bulky group of the substrate is discussed. (ovid.com)
  • reactive
  • This antibody was more reactive with the extracts of mucosa adjacent to carcinoma tissues than with the carcinoma extracts. (duke.edu)
  • cells
  • MAb2 94-7 competed with an anti-HAV cellular receptor antibody for binding to HAV-susceptible cells and partially blocked virus infection. (deepdyve.com)
  • The present invention provides antibodies useful as therapeutics for treating and/or preventing diseases associated with cells expressing GT468, including tumor-related diseases such as breast cancer, lung cancer, gastric cancer, ovarian cancer, and hepatocellular cancer. (freepatentsonline.com)
  • Thus, the inability of rid1 and ANG to infect HVEM-expressing cells may be due to the failure of these virion gDs to bind to HVEM on the cell. (asm.org)
  • variant
  • A variant gD protein, gD-1(Δ290-299t), showed enhanced binding to HVEMt relative to the binding of wild-type gDt ( 55 , 57 ). (asm.org)
  • motif
  • Cholesterol binds the C-terminal transmembrane (TM) residues, near an amphipathic helix, without requiring a cholesterol recognition sequence motif. (antibody-antibodies.com)
  • dependent
  • This binding is dependent on the native conformation of gD but is independent of its asparagine-linked oligosaccharides. (asm.org)
  • vitro
  • Subsequently, we demonstrated that soluble, truncated gD (gDt) from the KOS strain binds directly to a soluble, truncated form of HVEM (HVEMt) in vitro ( 55 ). (asm.org)
  • tail
  • Some of the antibodies that bind to the tip of the myosin-II tail decorate the bare zone of the myosin-II thin filament with 14-nm periodicity. (duke.edu)
  • Both antibodies bind near one another at the tip of the myosin-II tail and are those that decorate the bare zone of preformed bipolar filaments with 14-nm periodicity. (duke.edu)
  • None of the other antibodies affect myosin filament formation, including one that binds to another site near the tip of the myosin-II tail. (duke.edu)
  • Analyzing X-ray crystal structures of such adducts, two binding modes were observed: some inhibitors bind with their tail within the hydrophobic half of the active site, defined by residues Phe131, Val135, Leu198, Pro202, Leu204. (antibody-antibodies.com)
  • Other derivatives bind with their tail in a different region, pointing toward the hydrophilic half and making strong parallel stacking with Phe131. (antibody-antibodies.com)
  • thus
  • This route offers slower absorption from the site of administration, thus causing a sustained release effect. (google.com)
  • Thus, virion gD is the principal mediator of HSV binding to HVEM. (asm.org)