The Sec61p complex mediates the integration of a membrane protein by allowing lipid partitioning of the transmembrane domain (Q74175787)

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9 November 2019

title

The Sec61p complex mediates the integration of a membrane protein by allowing lipid partitioning of the transmembrane domain (English)

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9 November 2019

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4

T A Rapoport

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9 November 2019

author name string

S U Heinrich

series ordinal

1

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9 November 2019

W Mothes

series ordinal

2

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9 November 2019

J Brunner

series ordinal

3

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9 November 2019

language of work or name

English

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publication date

1 July 2000

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9 November 2019

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9 November 2019

volume

102

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9 November 2019

issue

2

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9 November 2019

page(s)

233-244

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Biogenesis of Polytopic Membrane Proteins: Membrane Segments Assemble within Translocation Channels prior to Membrane Integration

9 November 2019

cites work

1 reference

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Transmembrane orientation of signal-anchor proteins is affected by the folding state but not the size of the N-terminal domain.

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The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process

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Protein translocation into proteoliposomes reconstituted from purified components of the endoplasmic reticulum membrane

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A protein of the endoplasmic reticulum involved early in polypeptide translocation

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Predicting the orientation of eukaryotic membrane-spanning proteins

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7 January 2021

Membrane protein biogenesis: regulated complexity at the endoplasmic reticulum

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7 January 2021

Sec61p is adjacent to nascent type I and type II signal-anchor proteins during their membrane insertion.

1 reference

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7 January 2021

A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane

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7 January 2021

ER quality control: the cytoplasmic connection

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The protein-conducting channel in the membrane of the endoplasmic reticulum is open laterally toward the lipid bilayer.

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Protein translocation: tunnel vision

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7 January 2021

Molecular mechanism of membrane protein integration into the endoplasmic reticulum

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7 January 2021

Signal sequence recognition in cotranslational translocation by protein components of the endoplasmic reticulum membrane

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7 January 2021

Topology of eukaryotic type II membrane proteins: importance of N-terminal positively charged residues flanking the hydrophobic domain

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Signal sequence recognition in posttranslational protein transport across the yeast ER membrane.

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7 January 2021

Extensions of the signal hypothesis--sequential insertion model versus amphipathic tunnel hypothesis

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7 January 2021

A short amino-terminal segment of microsomal cytochrome P-450 functions both as an insertion signal and as a stop-transfer sequence.

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7 January 2021

A protein-conducting channel in the endoplasmic reticulum.

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7 January 2021

On the transfer of integral proteins into membranes

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7 January 2021

Signal sequence-dependent function of the TRAM protein during early phases of protein transport across the endoplasmic reticulum membrane

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7 January 2021

Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues

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7 January 2021

Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane

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7 January 2021

10.1016/S0092-8674(00)00028-3

Identifiers

DOI

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10943843%20AND%20SRC:MED&resulttype=core&format=json

9 November 2019

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