Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling.

By J. Takagi, B. Petre, Thomas Walz, T. Springer. Cell, 2002

1,212 citations recorded by the source corpus.

Subfields: Immunology and Allergy, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/fc64049d17bd7d4759f6ad531f7027a15ce4a6c7

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Immunology and Allergy

1. M. Humphries
2. Iain D. Campbell
3. M. Schwartz
4. T. Springer
5. C. Carman
6. B. Luo
7. T. Kinashi
8. Werner Müller

In Molecular Biology

1. M. Humphries
2. M. Schwartz
3. Iain D. Campbell
4. T. Springer
5. C. Carman
6. B. Luo
7. T. Kinashi
8. Thomas Walz

Citations in the corpus

• Structural basis of integrin regulation and signaling. (2007, methodology): “The influence on equilibration between these states has been studied of a flexible, C-terminal clasp fused to the C termini of the α and β subunit ectodomains, which mimics association between the α and β subunit transmembrane domains (33, 43).”
• Rolling Adhesion through an Extended Conformation of Integrin αLβ2 and Relation to α I and β I-like Domain Interaction (2004, methodology): “Residue L-Glu-310 in the linker demonstrated at least three distinct conformationalfollowing the I domain is critical for communication states (Takagi et al., 2002, 2003).”
• The critical cytoplasmic regions of the αL/β2 integrin in Rap1-induced adhesion and migration (2003, background): “Alternatively, it could lead to further conformational changes of LFA-1 that result in a fully open, highaffinity conformation, as is proposed for LFA-1 (Cabanas and Hogg, 1993) and IIb 3 (Takagi et al., 2002).”
• Adhesion of membranes via receptor-ligand complexes: Domain formation, binding cooperativity, and active processes (2009, background): “In one of their conformations, the integrin molecules are extended and can bind to apposing ligands [102, 103, 104].”
• An Essential Role for Talin during αMβ2-mediated Phagocytosis (2007, background): “Mn2 treatment activates integrins from the outside by opening up the folded, inactive extracellular domain, and it converts integrins to their extended, high-affinity conformation (Takagi et al., 2002).”
• Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics (2004, background): “jpg" NDATA ITEM> ]> Integrins are adhesion receptors that transmit signals bidirectionally across the plasma membran”
• Integrins and extracellular matrix in mechanotransduction. (2010, background): “During integrin activation a “knee-jerk” extension occurs to give the high-affinity/active conformation with the ligand-binding head repositioned away from the membrane in a more favorable position for ligand binding.(24,25) The affinity of the receptor is dependent on the conformation of the recept”
• Integrin structure, activation, and interactions. (2011, background): “By EM, an acute angle between the hybrid domain and b-I was observed in the bent state, and an obtuse angle in the extended, ligand-occupied state (Takagi et al. 2002).”