Investigations of the Structure, Topology, and Interactions of the Transmembrane Domain of the Lipid-Sorting Protein p24 Being Highly Selective for Sphingomyelin-C18-Reference-Cited by-同舟云学术

Investigations of the Structure, Topology, and Interactions of the Transmembrane Domain of the Lipid-Sorting Protein p24 Being Highly Selective for Sphingomyelin-C18

Published:2019-05-23 Issue:24 Volume:58 Page:2782-2795
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Aisenbrey Christopher¹,Kemayo-Koumkoua Patricia¹,Salnikov Evgeniy S.¹,Glattard Elise¹,Bechinger Burkhard¹^ORCID

Affiliation:

1. Université de Strasbourg/CNRS, UMR7177, Institut de Chimie, 4, rue Blaise Pascal, 67070 Strasbourg, France

Funder

Agence Nationale de la Recherche

Universit? de Strasbourg

Centre National de la Recherche Scientifique

R?gion Grand-Est

RTRA International Center of Frontier Research in Chemistry

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.9b00375

Reference68 articles.

1. The p24 family and selective transport processes at the ER-Golgi interface

2. COPI Budding within the Golgi Stack

3. Evidence for Segregation of Sphingomyelin and Cholesterol during Formation of Copi-Coated Vesicles

4. A structure of the COPI coat and the role of coat proteins in membrane vesicle assembly

5. p24 family proteins: key players in the regulation of trafficking along the secretory pathway

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