4.6 Article

The Novel S527F Mutation in the Integrin β3 Chain Induces a High Affinity αIIbβ3 Receptor by Hindering Adoption of the Bent Conformation

Related references

Note: Only part of the references are listed.
Article Biochemistry & Molecular Biology

Specific cysteines in β3 are involved in disulfide bond exchange-dependent and -independent activation of αIIbβ3

Ronit Mor-Cohen et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2008)

Article Biochemistry & Molecular Biology

A structural hypothesis for the transition between bent and extended conformations of the leukocyte β2 integrins

MinLong Shi et al.

JOURNAL OF BIOLOGICAL CHEMISTRY (2007)

Review Hematology

Platelet integrin αIIbβ3:: activation mechanisms

Y.-Q. Ma et al.

JOURNAL OF THROMBOSIS AND HAEMOSTASIS (2007)

Article Biochemistry & Molecular Biology

Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation

N Beglova et al.

NATURE STRUCTURAL BIOLOGY (2002)

Article Multidisciplinary Sciences

Crystal structure of the extracellular segment of integrin αVβ3

JP Xiong et al.

SCIENCE (2001)