Quality control: Putting protein aggregates in a bind

Jay R. Unruh; Brian D. Slaughter; Rong Li

doi:10.1016/j.cub.2012.12.005

Quality control: Putting protein aggregates in a bind

Jay R. Unruh
, Brian D. Slaughter
, Rong Li

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

5 Scopus citations

Abstract

Asymmetric inheritance of protein aggregates in budding yeast is a fascinating yet controversial area of aging research. A recent study demonstrates that unfolded protein aggregates are confined to the mother by tethering to organelles rather than retrograde transport.

Original language	English (US)
Pages (from-to)	R74-R76
Journal	Current Biology
Volume	23
Issue number	2
DOIs	https://doi.org/10.1016/j.cub.2012.12.005
State	Published - Jan 21 2013
Externally published	Yes

ASJC Scopus subject areas

General Biochemistry, Genetics and Molecular Biology
General Agricultural and Biological Sciences

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10.1016/j.cub.2012.12.005

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title = "Quality control: Putting protein aggregates in a bind",

abstract = "Asymmetric inheritance of protein aggregates in budding yeast is a fascinating yet controversial area of aging research. A recent study demonstrates that unfolded protein aggregates are confined to the mother by tethering to organelles rather than retrograde transport.",

author = "Unruh, \{Jay R.\} and Slaughter, \{Brian D.\} and Rong Li",

year = "2013",

month = jan,

day = "21",

doi = "10.1016/j.cub.2012.12.005",

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T1 - Quality control

T2 - Putting protein aggregates in a bind

AU - Unruh, Jay R.

AU - Slaughter, Brian D.

AU - Li, Rong

PY - 2013/1/21

Y1 - 2013/1/21

N2 - Asymmetric inheritance of protein aggregates in budding yeast is a fascinating yet controversial area of aging research. A recent study demonstrates that unfolded protein aggregates are confined to the mother by tethering to organelles rather than retrograde transport.

AB - Asymmetric inheritance of protein aggregates in budding yeast is a fascinating yet controversial area of aging research. A recent study demonstrates that unfolded protein aggregates are confined to the mother by tethering to organelles rather than retrograde transport.

UR - https://www.scopus.com/pages/publications/84872732941

UR - https://www.scopus.com/pages/publications/84872732941#tab=citedBy

U2 - 10.1016/j.cub.2012.12.005

DO - 10.1016/j.cub.2012.12.005

M3 - Short survey

C2 - 23347944

AN - SCOPUS:84872732941

SN - 0960-9822

VL - 23

SP - R74-R76

JO - Current Biology

JF - Current Biology

IS - 2

ER -

Quality control: Putting protein aggregates in a bind

Abstract

ASJC Scopus subject areas

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