Direct observation of proteolytic cleavage at the S2 site upon forced unfolding of the Notch negative regulatory region
Published 2012 View Full Article
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Title
Direct observation of proteolytic cleavage at the S2 site upon forced unfolding of the Notch negative regulatory region
Authors
Keywords
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Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 109, Issue 41, Pages E2757-E2765
Publisher
Proceedings of the National Academy of Sciences
Online
2012-09-25
DOI
10.1073/pnas.1205788109
References
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- (2011) Jianhan Chen et al. PLoS One
- Evidence for Increased Exposure of the Notch1 Metalloprotease Cleavage Site upon Conversion to an Activated Conformation
- (2011) Kittichoat Tiyanont et al. STRUCTURE
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- (2010) Emily B. Pratt et al. ACTA HISTOCHEMICA
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- Metalloprotease ADAM10 Is Required for Notch1 Site 2 Cleavage
- (2009) Geert van Tetering et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- A Notch updated
- (2009) An-Chi Tien et al. JOURNAL OF CELL BIOLOGY
- Selective Use of ADAM10 and ADAM17 in Activation of Notch1 Signaling
- (2009) E. C. Bozkulak et al. MOLECULAR AND CELLULAR BIOLOGY
- Effects of S1 Cleavage on the Structure, Surface Export, and Signaling Activity of Human Notch1 and Notch2
- (2009) Wendy R. Gordon et al. PLoS One
- Mechanically Activated Integrin Switch Controls 5 1 Function
- (2009) J. C. Friedland et al. SCIENCE
- Structure of the Notch1-negative regulatory region: implications for normal activation and pathogenic signaling in T-ALL
- (2008) W. R. Gordon et al. BLOOD
- GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation
- (2008) Berk Hess et al. Journal of Chemical Theory and Computation
- Mechanotransduction gone awry
- (2008) Diana E. Jaalouk et al. NATURE REVIEWS MOLECULAR CELL BIOLOGY
- A conserved face of the Jagged/Serrate DSL domain is involved in Notch trans-activation and cis-inhibition
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- Versatile cloning system for construction of multimeric proteins for use in atomic force microscopy
- (2002) Annette Steward et al. PROTEIN SCIENCE
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