A Gly → Ser Change Causes Defective Folding in Vitro of Calcium-binding Epidermal Growth Factor-like Domains from Factor IX and Fibrillin-1
Open Access
- 1 April 1998
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 273 (14) , 7807-7813
- https://doi.org/10.1074/jbc.273.14.7807
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- Marfan Database (second edition): software and database for the analysis of mutations in the human FBN1 geneNucleic Acids Research, 1997
- Notch3 mutations in CADASIL, a hereditary adult-onset condition causing stroke and dementiaNature, 1996
- Solution Structure of a Pair of Calcium-Binding Epidermal Growth Factor-like Domains: Implications for the Marfan Syndrome and Other Genetic DisordersCell, 1996
- Haemophilia B (sixth edition): a database of point mutations and short additions and deletionsNucleic Acids Research, 1996
- The structure of a Ca2+-binding epidermal growth factor-like domain: Its role in protein-protein interactionsCell, 1995
- Epidermal growth factor-like modulesCurrent Opinion in Structural Biology, 1993
- Ligand requirements for Ca2+ binding to EGF-like domainsProtein Engineering, Design and Selection, 1992
- Molecular genetics of the LDL receptor gene in familial hypercholesterolemiaHuman Mutation, 1992
- Key residues involved in calcium-binding motifs in EGF-like domainsNature, 1991
- Hemophilia B Durham: a mutation in the first EGF-like domain of factor IX that is characterized by polymerase chain reactionBlood, 1988