Juxtamembrane contribution to transmembrane signaling-Reference-Cited by-同舟云学术

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Juxtamembrane contribution to transmembrane signaling

Published:2015-07 Issue:4 Volume:104 Page:317-322
ISSN:0006-3525
Container-title:Biopolymers
language:en
Short-container-title:Biopolymers

Author:

Deng Wei¹,Li Renhao¹

Affiliation:

1. Department of Pediatrics; Aflac Cancer and Blood Disorders Center, Emory University School of Medicine; Atlanta GA 30322

Funder

National Institutes of Health

American Society of Hematology

Publisher

Wiley

Subject

Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1002/bip.22651/fullpdf

Reference75 articles.

1. The HAMP Domain Structure Implies Helix Rotation in Transmembrane Signaling

2. Dynamic Helix Interactions in Transmembrane Signaling

3. Structural Insights into Calmodulin-regulated L-selectin Ectodomain Shedding

4. Calmodulin Adopts an Extended Conformation when Interacting with L-Selectin in Membranes

5. A Piston Model for Transmembrane Signaling of the Aspartate Receptor

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