Crystals of the human heavy chain disease protein riv and human Fc fragment are isomorphous: Further evidence for conformational flexibility in the hinge region of immunoglobulins-Reference-Cited by-同舟云学术

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Crystals of the human heavy chain disease protein riv and human Fc fragment are isomorphous: Further evidence for conformational flexibility in the hinge region of immunoglobulins

Published:1983-04 Issue:3 Volume:165 Page:559-561
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Mariuzza R.A.,Poljak R.J.,Mihaesco C.,Mihaesco E.

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference9 articles.

1. A fragment corresponding to the CH2 region of immunoglobulin G (IgG) with complement fixing activity

2. Crystallographic structure studies of an IgG molecule and an Fc fragment

3. Crystallographic study of human myeloma Fc-fragment

4. Sequences of Immunoglobulin Chains;Kabat,1979

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1. A historical perspective on protein crystallization from 1840 to the present day;FEBS Journal;2013-11-25

2. Fusion Proteins: Applications and Challenges;Fusion Protein Technologies for Biopharmaceuticals;2013-02-12

3. Effect of zinc on human IgG1 and its FcγR interactions;Immunology Letters;2012-03

4. The structure of immunoglobulins and their interaction with complement;Activators and Inhibitors of Complement;1993

5. Structure of antibodies and their complexes with antigens;Molecular Immunology;1991-12

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