Symbiosis: A cycle made for two
- R. Smallridge
- BiologyNature reviews. Molecular cell biology
- 1 June 2003
The first epidermal growth factor-like domain of the low-density lipoprotein receptor contains a noncanonical calcium binding site.
- S. Malby, R. Pickering, S. Saha, R. Smallridge, S. Linse, A. Downing
- Biology, ChemistryBiochemistry
- 27 January 2001
Comparison of the K(d) for the C-terminal site with the calcium concentration in late vesicles indicates that the binding properties of this module may be tuned to titrate upon endocytosis of the LDL receptor-ligand complex, and thus calcium binding may play a role in the ligand dissociation process.
A Gly → Ser Change Causes Defective Folding in Vitro of Calcium-binding Epidermal Growth Factor-like Domains from Factor IX and Fibrillin-1*
- P. Whiteman, A. Downing, R. Smallridge, P. Winship, P. Handford
- BiologyJournal of Biological Chemistry
- 3 April 1998
NMR analysis of a covalently linked pair of fibrillin cbEGF domains demonstrates that the C-terminal domain adopts the native epidermal growth factor fold, despite the fact that the adjacent mutant domain is misfolded.
EGF-like domain calcium affinity modulated by N-terminal domain linkage in human fibrillin-1.
- R. Smallridge, P. Whiteman, K. Doering, P. Handford, A. Downing
- BiologyJournal of Molecular Biology
- 26 February 1999
Results indicate that fibrillin-1 cbEGF Ca2+ affinity can be significantly modulated by the type of domain which is linked to its N terminus, and may contribute to the biomechanical properties of the microfibrillar network.
Solution Structure and Dynamics of a Calcium Binding Epidermal Growth Factor-like Domain Pair from the Neonatal Region of Human Fibrillin-1* 210
- R. Smallridge, P. Whiteman, J. Werner, I. Campbell, P. Handford, A. Downing
- BiologyJournal of Biological Chemistry
- 4 April 2003
Backbone dynamics data confirm the extended structure of cb EGF12–13 and lend support to the hypothesis that a correlation exists between backbone flexibility and cbEGF domain calcium affinity, and provide important insight into the potential consequences of MFS-associated mutations for the assembly and biomechanical properties of connective tissue microfibrils.
Proteolysis: A new family
- R. Smallridge
- BiologyNature reviews. Molecular cell biology
- 1 August 2002
The identification of SPP as a presenilin-like aspartic protease by Martoglio and co-workers supports the view that Presenilins are proteases.
A G1127S Change in Calcium-binding Epidermal Growth Factor-like Domain 13 of Human Fibrillin-1 Causes Short Range Conformational Effects*
- P. Whiteman, R. Smallridge, V. Knott, J. Cordle, A. Downing, P. Handford
- BiologyJournal of Biological Chemistry
- 18 May 2001
It is demonstrated that missense mutations in fibrillin-1 cbEGF domains can cause short range structural effects in addition to long range effects previously observed with a E1073K mutation in cb EGF12.
Cell adhesion: Making new contacts
- R. Smallridge
- MedicineNature reviews. Molecular cell biology
- 2003
DNA repair: Family resemblance
- R. Smallridge
- BiologyNature reviews. Molecular cell biology
- 1 February 2006
Glycoprotein degradation: Time for a trim
- R. Smallridge
- BiologyNature reviews. Molecular cell biology
- 1 April 2003
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