The Crystal Structure of the Major Cat Allergen Fel d 1, a Member of the Secretoglobin Family
Open Access
- 1 September 2003
- journal article
- Published by Elsevier BV
- Vol. 278 (39), 37730-37735
- https://doi.org/10.1074/jbc.m304740200
Abstract
No abstract availableThis publication has 54 references indexed in Scilit:
- Refinement of Macromolecular Structures by the Maximum-Likelihood MethodActa Crystallographica Section D-Biological Crystallography, 1997
- SWISS‐MODEL and the Swiss‐Pdb Viewer: An environment for comparative protein modelingElectrophoresis, 1997
- IgE antibodies to recombinant forms of Fel d I: Dichotomy between fluid-phase and solid-phase binding studiesJournal of Allergy and Clinical Immunology, 1995
- Enhanced immunoreactivity and preferential heterodimer formation of reassociated Fel d I recombinant chainsMolecular Immunology, 1995
- Effects of castration and testosterone onFel dI production by sebaceous glands of male cats: II-morphometric assessmentClinical and Experimental Allergy, 1994
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- Main-chain Bond Lengths and Bond Angles in Protein StructuresJournal of Molecular Biology, 1993
- Role of the Major Allergen (Fel d I) in Patients Sensitized to Cat AllergensInternational Archives of Allergy and Immunology, 1993
- Refined structure of rat Clara cell 17 kDa protein at 3·0 Å resolutionJournal of Molecular Biology, 1992
- Structure and refinement of the oxidized P21 form of uteroglobin at 1.64 Å resolutionJournal of Molecular Biology, 1989