A single amino acid in the second Ig-like domain of the human Fcγ receptor II is critical for human IgC2 binding
- Author
- WARMERDAM, P. A. M1 ; VAN DE WINKEL, J. G. J; VLUG, A; WESTERDAAL, N. A. C; CAPEL, P. J. A
[1] Univ. hosp. Utrecht, dep. exp. immunology, Utrecht 3508 GA, United States - Source
The Journal of immunology (1950). 1991, Vol 147, Num 4, pp 1338-1343 ; ref : 33 ref
- CODEN
- JOIMA3
- ISSN
- 0022-1767
- Scientific domain
- Biochemistry, molecular biology, biophysics; Immunology, immunopathology, allergology
- Publisher
- American Association of Immunologists, Bethesda, MD
- Publication country
- United States
- Document type
- Article
- Language
- English
- Keyword (fr)
- Chaîne peptidique γ Fragment peptidique Fc Homme Hybride moléculaire IgG2 Interaction moléculaire Polymorphisme Récepteur biologique Site fixation Transfection Domaine moléculaire Récepteur FcγII Immunoglobuline
- Keyword (en)
- Gamma-Peptide chain Fc-Fragment Human Molecular hybrid IgG2 Molecular interaction Polymorphism Biological receptor Binding site Transfection Immunoglobulins
- Keyword (es)
- Cadena peptídica γ Fragmento peptídico Fc Hombre Híbrido molecular IgG2 Interacción molecular Polimorfismo Receptor biológico Sitio fijación Transfección Inmunoglobulina
- Classification
- Pascal
- 002 Biological and medical sciences / 002A Fundamental and applied biological sciences. Psychology / 002A04 Molecular and cellular biology / 002A04F Cell structures and functions / 002A04F03 Cell receptors / 002A04F03F Miscellaneous
- Discipline
- Molecular and cell biology
- Origin
- Inist-CNRS
- Database
- PASCAL
- INIST identifier
- 5041438
Sauf mention contraire ci-dessus, le contenu de cette notice bibliographique peut être utilisé dans le cadre d’une licence CC BY 4.0 Inist-CNRS / Unless otherwise stated above, the content of this bibliographic record may be used under a CC BY 4.0 licence by Inist-CNRS / A menos que se haya señalado antes, el contenido de este registro bibliográfico puede ser utilizado al amparo de una licencia CC BY 4.0 Inist-CNRS
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DOI
10.4049/jimmunol.147.4.1338 
https://dx.doi.org/10.4049/jimmunol.147.4.1338
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