Reversibly locking a protein fold in an active conformation with a disulfide bond: Integrin L I domains with high affinity and antagonist activity in vivo-Reference-Cited by-同舟云学术

Reversibly locking a protein fold in an active conformation with a disulfide bond: Integrin L I domains with high affinity and antagonist activity in vivo

Published:2001-05-15 Issue:11 Volume:98 Page:6009-6014
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

Shimaoka M.,Lu C.,Palframan R. T.,von Andrian U. H.,McCormack A.,Takagi J.,Springer T. A.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference45 articles.

1. Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm

2. Direct evidence for two affinity states for lymphocyte function-associated antigen 1 on activated T cells.

3. Chemokines Trigger Immediate β2 Integrin Affinity and Mobility Changes

4. The I Domain of Integrin Leukocyte Function-associated Antigen-1 Is Involved in a Conformational Change Leading to High Affinity Binding to Ligand Intercellular Adhesion Molecule 1 (ICAM-1)

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