Protein translocation at the ER membrane: A complex process becomes more so. (Q47895935)

6 February 2018

title

Protein translocation at the ER membrane: A complex process becomes more so. (English)

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6 February 2018

author name string

Johnson AE

series ordinal

1

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6 February 2018

publication date

1 March 1997

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6 February 2018

published in

Trends in Cell Biology

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6 February 2018

volume

7

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6 February 2018

issue

3

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6 February 2018

page(s)

90-95

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6 February 2018

Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane

cites work

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https://api.crossref.org/works/10.1016%2FS0962-8924%2897%2901029-5

7 January 2021

Protein transport across the eukaryotic endoplasmic reticulum and bacterial inner membranes

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7 January 2021

Regulation by the ribosome of the GTPase of the signal-recognition particle during protein targeting

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7 January 2021

Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases

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7 January 2021

Signal sequences specify the targeting route to the endoplasmic reticulum membrane

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7 January 2021

Signal sequences: the same yet different

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7 January 2021

A two-step recognition of signal sequences determines the translocation efficiency of proteins.

1 reference

https://api.crossref.org/works/10.1016%2FS0962-8924%2897%2901029-5

7 January 2021

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

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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

Signal sequence processing in rough microsomes

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7 January 2021

A protein-conducting channel in the endoplasmic reticulum.

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7 January 2021

Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore.

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https://api.crossref.org/works/10.1016%2FS0962-8924%2897%2901029-5

7 January 2021

The signal sequence moves through a ribosomal tunnel into a noncytoplasmic aqueous environment at the ER membrane early in translocation

1 reference

https://api.crossref.org/works/10.1016%2FS0962-8924%2897%2901029-5

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

Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p

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Novel role for Sp1 in phorbol ester enhancement of human platelet thromboxane receptor gene expression

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7 January 2021

Sequence-specific alteration of the ribosome-membrane junction exposes nascent secretory proteins to the cytosol

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7 January 2021

A nascent secretory protein may traverse the ribosome/endoplasmic reticulum translocase complex as an extended chain

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7 January 2021

Oligomeric Rings of the Sec61p Complex Induced by Ligands Required for Protein Translocation

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7 January 2021

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

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7 January 2021

Determination of the transmembrane topology of yeast Sec61p, an essential component of the endoplasmic reticulum translocation complex

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7 January 2021

Synthesis and secretion of apolipoprotein B from cultured liver cells

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Ubiquitin-proteasome pathway mediates intracellular degradation of apolipoprotein B

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7 January 2021

Directionality in protein translocation across membranes: the N-tail phenomenon.

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7 January 2021

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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7 January 2021

Discrete cross-linking products identified during membrane protein biosynthesis

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7 January 2021

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

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7 January 2021

Reinitiation of protein translocation across the endoplasmic reticulum membrane for the topogenesis of multispanning membrane proteins

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7 January 2021

10.1016/S0962-8924(97)01029-5

Identifiers

DOI

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6 February 2018

PubMed ID

17708914

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6 February 2018