Lumenal proteins of the mammalian endoplasmic reticulum are required to complete protein translocation. (Q49486465)

20 February 2018

title

Lumenal proteins of the mammalian endoplasmic reticulum are required to complete protein translocation. (English)

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20 February 2018

main subject

endoplasmic reticulum

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2

Blobel G

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20 February 2018

Nicchitta CV

1

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20 February 2018

language of work or name

English

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publication date

1 June 1993

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20 February 2018

published in

Cell

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20 February 2018

volume

73

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20 February 2018

issue

5

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20 February 2018

page(s)

989-998

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20 February 2018

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

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A yeast gene important for protein assembly into the endoplasmic reticulum and the nucleus has homology to DnaJ, an Escherichia coli heat shock protein

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Requirement for hsp70 in the mitochondrial matrix for translocation and folding of precursor proteins

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Sec61p and BiP directly facilitate polypeptide translocation into the ER.

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Bidirectional movement of a nascent polypeptide across microsomal membranes reveals requirements for vectorial translocation of proteins

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Secretory protein translocation in a yeast cell-free system can occur posttranslationally and requires ATP hydrolysis

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Formation of a functional ribosome-membrane junction during translocation requires the participation of a GTP-binding protein

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Regulating the retention of T-cell receptor alpha chain variants within the endoplasmic reticulum: Ca(2+)-dependent association with BiP

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SSC1, an essential member of the yeast HSP70 multigene family, encodes a mitochondrial protein

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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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In vitro protein translocation across the yeast endoplasmic reticulum: ATP-dependent posttranslational translocation of the prepro-alpha-factor

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Structure of a yeast pheromone gene (MF alpha): a putative alpha-factor precursor contains four tandem copies of mature alpha-factor.

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A protein-conducting channel in the endoplasmic reticulum.

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8 October 2022

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Isolation and characterization of cDNA clones for rat ribophorin I: complete coding sequence and in vitro synthesis and insertion of the encoded product into endoplasmic reticulum membranes

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8 October 2022

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Preparation and characterization of dog pancreas microsomal membranes specifically depleted of protein disulphide-isomerase

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8 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/0092-8674(93)90276-V

Oxidized redox state of glutathione in the endoplasmic reticulum

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8 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/0092-8674(93)90276-V

How do polypeptides cross the mitochondrial membranes?

1 reference

8 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/0092-8674(93)90276-V

Targeting of the hepatitis B virus precore protein to the endoplasmic reticulum membrane: after signal peptide cleavage translocation can be aborted and the product released into the cytoplasm

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8 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/0092-8674(93)90276-V

Import of honeybee prepromelittin into the endoplasmic reticulum: structural basis for independence of SRP and docking protein.

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8 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/0092-8674(93)90276-V

Uncoupling translocation from translation: implications for transport of proteins across membranes

1 reference

8 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/0092-8674(93)90276-V

A protein of the endoplasmic reticulum involved early in polypeptide translocation

1 reference

8 October 2022

https://opencitations.net/index/coci/api/v1/references/10.1016/0092-8674(93)90276-V

Identifiers

DOI

10.1016/0092-8674(93)90276-V

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20 February 2018

PubMed ID

8500184

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20 February 2018