Endoplasmic reticulum stress caused by aggregate-prone proteins containing homopolymeric amino acids.
about
Functional characterization of the protein C A267T mutation: evidence for impaired secretion due to defective intracellular transport.Protein C mutation (A267T) results in ER retention and unfolded protein response activation.Regulation of endoplasmic reticulum stress in rat cortex by p62/ZIP through the Keap1-Nrf2-ARE signalling pathway after transient focal cerebral ischaemia.
P2860
Endoplasmic reticulum stress caused by aggregate-prone proteins containing homopolymeric amino acids.
description
2007 nî lūn-bûn
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2007年の論文
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2007年学术文章
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2007年学术文章
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2007年学术文章
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2007年学术文章
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2007年学术文章
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2007年学术文章
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2007年學術文章
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2007年學術文章
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name
Endoplasmic reticulum stress c ...... ing homopolymeric amino acids.
@en
Endoplasmic reticulum stress c ...... ing homopolymeric amino acids.
@nl
type
label
Endoplasmic reticulum stress c ...... ing homopolymeric amino acids.
@en
Endoplasmic reticulum stress c ...... ing homopolymeric amino acids.
@nl
prefLabel
Endoplasmic reticulum stress c ...... ing homopolymeric amino acids.
@en
Endoplasmic reticulum stress c ...... ing homopolymeric amino acids.
@nl
P2093
P2860
P1433
P1476
Endoplasmic reticulum stress c ...... ing homopolymeric amino acids.
@en
P2093
Eriko Fujita
Isei Tanida
Kazuya Toriumi
Naohiro Uchio
Noboru Sasagawa
Reiko Kuroda
Shoichi Ishiura
Takashi Momoi
Yoriko Kouroku
P2860
P304
P356
10.1111/J.1742-4658.2007.06085.X
P407
P577
2007-10-08T00:00:00Z