Signal peptides open protein-conducting channels in E. coli (Q42602564)

3 November 2017

title

Signal peptides open protein-conducting channels in E. coli (English)

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3 November 2017

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2

Blobel G

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3 November 2017

Simon SM

1

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3 November 2017

language of work or name

English

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publication date

1 May 1992

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3 November 2017

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3 November 2017

volume

69

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3 November 2017

issue

4

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3 November 2017

page(s)

677-684

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Protein translocation across the endoplasmic reticulum. I. Detection in the microsomal membrane of a receptor for the signal recognition particle

3 November 2017

cites work

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8 October 2022

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Translocation of secretory proteins across the microsomal membrane occurs through an environment accessible to aqueous perturbants

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SecB functions as a cytosolic signal recognition factor for protein export in E. coli

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Fusion of phospholipid vesicles with a planar membrane depends on the membrane permeability of the solute used to create the osmotic pressure

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Endogenously synthesized peptide with an endoplasmic reticulum signal sequence sensitizes antigen processing mutant cells to class I-restricted cell-mediated lysis

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[13] Bacterial Membranes

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Translocation of proteins across the endoplasmic reticulum. II. Signal recognition protein (SRP) mediates the selective binding to microsomal membranes of in-vitro-assembled polysomes synthesizing secretory protein

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Conformations of signal peptides induced by lipids suggest initial steps in protein export

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Modulation of folding pathways of exported proteins by the leader sequence

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Unity in function in the absence of consensus in sequence: role of leader peptides in export

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Reconstitution of Cell Membrane Structure in vitro and its Transformation into an Excitable System

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A membrane component essential for vectorial translocation of nascent proteins across the endoplasmic reticulum: requirements for its extraction and reassociation with the membrane

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Stop-transfer regions do not halt translocation of proteins into chloroplasts

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8 October 2022

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Translocation of proteins across the endoplasmic reticulum. I. Signal recognition protein (SRP) binds to in-vitro-assembled polysomes synthesizing secretory protein

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8 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/0092-8674(92)90231-Z

A protein-conducting channel in the endoplasmic reticulum

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8 October 2022

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Ribonucleoparticle-independent import of proteins into mammalian microsomes involves a membrane protein which is sensitive to chemical alkylation.

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The signal recognition particle receptor mediates the GTP-dependent displacement of SRP from the signal sequence of the nascent polypeptide

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8 October 2022

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Assembly of the Semliki Forest virus membrane glycoproteins in the membrane of the endoplasmic reticulum in vitro

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The signal recognition particle in S. cerevisiae

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https://opencitations.net/index/coci/api/v1/references/10.1016/0092-8674(92)90231-Z

Assembly of proteins into membranes

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8 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/0092-8674(92)90231-Z

Production and ultrastructure of lysozyme and ethylenediaminetetraacetate-lysozyme spheroplasts of Escherichia coli

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8 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/0092-8674(92)90231-Z

The signal sequence of nascent preprolactin interacts with the 54K polypeptide of the signal recognition particle

1 reference

8 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/0092-8674(92)90231-Z

Identifiers

DOI

10.1016/0092-8674(92)90231-Z

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3 November 2017

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