The physiological structure of human C-reactive protein and its complex with phosphocholine
- 15 February 1999
- journal article
- Published by Elsevier BV in Structure
- Vol. 7 (2), 169-177
- https://doi.org/10.1016/s0969-2126(99)80023-9
Abstract
No abstract availableKeywords
This publication has 36 references indexed in Scilit:
- Pentameric and decameric structures in solution of serum amyloid P component by X-ray and neutron scattering and molecular modelling analysesJournal of Molecular Biology, 1997
- Crystal structure of a decameric complex of human serum amyloid P component with bound dAMPJournal of Molecular Biology, 1997
- A role for secretory phospholipase A2 and C-reactive protein in the removal of injured cellsImmunology Today, 1997
- Comparative analyses of pentraxins: implications for protomer assembly and ligand bindingStructure, 1994
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Binding of pentraxins to different nuclear structures: C-reactive protein binds to small nuclear ribonucleoprotein particles, serum amyloid P component binds to chromatin and nucleoliClinical and Experimental Immunology, 1994
- Formation of Two-dimensional Arrays of Annexin V on Phosphatidylserine-containing LiposomesJournal of Molecular Biology, 1994
- Elucidation of a protease-sensitive site involved in the binding of calcium to C-reactive proteinBiochemistry, 1989
- Serum amyloid P component is the major calcium-dependent specific DNA binding protein of the serumBiochemical and Biophysical Research Communications, 1987
- Preliminary X-ray study of crystals of human C-reactive proteinJournal of Molecular Biology, 1987