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Cited by 113 publications
(80 citation statements)
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References 26 publications
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“…Mutations in the Fc domain of hCD16a-Ig are L267F, L268E, G270A, and A363T (numbered as in accession number AAH69020.1). These mutations were shown to abolish the binding of Fc␥Rs (18,19). The anti-CD16 nonblocking monoclonal antibody (mAb) 214.1 (murine IgG1) was a generous gift from Dr. Howard Fleit (State University of New York, Long Island).…”
Section: Methodsmentioning
confidence: 99%
“…Mutations in the Fc domain of hCD16a-Ig are L267F, L268E, G270A, and A363T (numbered as in accession number AAH69020.1). These mutations were shown to abolish the binding of Fc␥Rs (18,19). The anti-CD16 nonblocking monoclonal antibody (mAb) 214.1 (murine IgG1) was a generous gift from Dr. Howard Fleit (State University of New York, Long Island).…”
Section: Methodsmentioning
confidence: 99%
“…The key amino acid residues in the Fc region that interact with Fcγ receptors (CD64 for FcγRI, CD32 FcγRII and CD16 FcγRIII), complement C1q and neonatal FcRn receptors have been determined. Earlier work using a domain swapping approach has defined regions that are required for Fcγ receptor (~230-238 amino acids 11 according to the EU numbering system) and complement binding (292-340 amino acids 12 ). Further studies have identified individual amino acid residues that interact with Fcγ receptors and complement C1q protein.…”
Section: Introductionmentioning
confidence: 99%
“…Several results pointed out the importance of residues 233-239 in the human system [8,9,11,12,24,25] [8]. Based on the threedimensional (3D) structure of the human Fc + RIIb, the interdomain cleft between the CH2 and CH3 domain of IgG was suggested as the Fc + RIIb binding site [28].…”
Section: Discussionmentioning
confidence: 99%
“…Hence, monomeric IgG present in the circulation does not trigger responses mediated by Fc + RI, Fc + RII or Fc + RIII [4]. Tryptophan residues in the first domain of all Fc + R play an important role in forming a hydrogen bridge with the ligand [6], and both the lower hinge and several residues in the CH2 domain of IgG were shown to participate in the interaction [6][7][8][9][10][11][12][13][14]. Glycosylation of IgG may also influence binding to certain Fc + R isoforms [15,16].…”
Section: Introductionmentioning
confidence: 99%