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December 1, 1984The Journal of Experimental MedicineOpen Access

C3b covalently bound to IgG demonstrates a reduced rate of inactivation by factors H and I.

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Authors

LFL F FriesNational Institutes of HealthTGT A GaitherNational Institutes of HealthCHC H HammerUniversity of Maryland, Baltimore

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Cite This Study

Fries et al. (1984) studied this question.

synapsesocial.com/papers/6a6f2e38febe604dd7083112https://doi.org/10.1084/jem.160.6.1640
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Also Consider

Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Natural release of covalently bound C3b from cell surfaces and the study of this phenomenon in the fluid-phase system.1984 · 39 citations
  2. 2Identification of the membrane glycoprotein that is the C3b receptor of the human erythrocyte, polymorphonuclear leukocyte, B lymphocyte, and monocyte1980 · 645 citations
  3. 3Human complement C3b inactivator: isolation, characterization, and demonstration of an absolute requirement for the serum protein beta1H for cleavage of C3b and C4b in solution.1977 · 686 citations
  4. 4Classical complement pathway activation by antipneumococcal antibodies leads to covalent binding of C3b to antibody molecules1983 · 43 citations