Binding of cytochrome b5 to membranes of isolated subcellular organelles from rat liver.
about
The carboxy-terminal 10 amino acid residues of cytochrome b5 are necessary for its targeting to the endoplasmic reticulumTransmembrane topogenesis of a tail-anchored protein is modulated by membrane lipid composition.Membrane-bound redox proteins of the murine Friend virus-induced erythroleukemia cellSynthesis of rat liver microsomal cytochrome b5 by free ribosomesAbsence of sugars in electrophoretically purified cytochrome b5 demonstrated by combined gas chromatography-mass spectrometry.Novel targeting signals mediate the sorting of different isoforms of the tail-anchored membrane protein cytochrome b5 to either endoplasmic reticulum or mitochondria.
P2860
Binding of cytochrome b5 to membranes of isolated subcellular organelles from rat liver.
description
1978 nî lūn-bûn
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1978年の論文
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1978年学术文章
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name
Binding of cytochrome b5 to membranes of isolated subcellular organelles from rat liver.
@en
type
label
Binding of cytochrome b5 to membranes of isolated subcellular organelles from rat liver.
@en
prefLabel
Binding of cytochrome b5 to membranes of isolated subcellular organelles from rat liver.
@en
P2860
P356
P1476
Binding of cytochrome b5 to membranes of isolated subcellular organelles from rat liver.
@en
P2093
P2860
P304
P356
10.1083/JCB.79.2.291
P407
P433
P577
1978-11-01T00:00:00Z