CFTR: New Members Join the Fold

William R. Skach

doi:10.1016/j.cell.2006.11.002

CFTR: New Members Join the Fold

William R. Skach

Biochemistry & Molecular Biology

Research output: Contribution to journal › Short survey › peer-review

23 Scopus citations

Abstract

The folding, misfolding, and degradation of membrane proteins is controlled by multiple processes within the cell. In this issue of Cell, Wang et al. (2006) present an interactome for CFTR, the chloride channel that is misfolded and prematurely degraded in cystic fibrosis. Among the proteins interacting with CFTR is a new member of the Hsp90 chaperone system, Aha1, that plays a central role in CFTR folding.

Original language	English (US)
Pages (from-to)	673-675
Number of pages	3
Journal	Cell
Volume	127
Issue number	4
DOIs	https://doi.org/10.1016/j.cell.2006.11.002
State	Published - Nov 17 2006

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology

Access to Document

10.1016/j.cell.2006.11.002

Cite this

@article{022c99a8655142b39ce1e9de42965f89,

title = "CFTR: New Members Join the Fold",

abstract = "The folding, misfolding, and degradation of membrane proteins is controlled by multiple processes within the cell. In this issue of Cell, Wang et al. (2006) present an interactome for CFTR, the chloride channel that is misfolded and prematurely degraded in cystic fibrosis. Among the proteins interacting with CFTR is a new member of the Hsp90 chaperone system, Aha1, that plays a central role in CFTR folding.",

author = "Skach, {William R.}",

year = "2006",

month = nov,

day = "17",

doi = "10.1016/j.cell.2006.11.002",

language = "English (US)",

volume = "127",

pages = "673--675",

journal = "Cell",

issn = "0092-8674",

publisher = "Cell Press",

number = "4",

}

TY - JOUR

T1 - CFTR

T2 - New Members Join the Fold

AU - Skach, William R.

PY - 2006/11/17

Y1 - 2006/11/17

N2 - The folding, misfolding, and degradation of membrane proteins is controlled by multiple processes within the cell. In this issue of Cell, Wang et al. (2006) present an interactome for CFTR, the chloride channel that is misfolded and prematurely degraded in cystic fibrosis. Among the proteins interacting with CFTR is a new member of the Hsp90 chaperone system, Aha1, that plays a central role in CFTR folding.

AB - The folding, misfolding, and degradation of membrane proteins is controlled by multiple processes within the cell. In this issue of Cell, Wang et al. (2006) present an interactome for CFTR, the chloride channel that is misfolded and prematurely degraded in cystic fibrosis. Among the proteins interacting with CFTR is a new member of the Hsp90 chaperone system, Aha1, that plays a central role in CFTR folding.

UR - http://www.scopus.com/inward/record.url?scp=33750817664&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33750817664&partnerID=8YFLogxK

U2 - 10.1016/j.cell.2006.11.002

DO - 10.1016/j.cell.2006.11.002

M3 - Short survey

C2 - 17110327

AN - SCOPUS:33750817664

SN - 0092-8674

VL - 127

SP - 673

EP - 675

JO - Cell

JF - Cell

IS - 4

ER -

CFTR: New Members Join the Fold

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this