The identification of proteins in the proximity of signal-anchor sequences during their targeting to and insertion into the membrane of the ER. (Q43107796)

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scientific article published in April 1991

Language	Label	Description	Also known as
English	The identification of proteins in the proximity of signal-anchor sequences during their targeting to and insertion into the membrane of the ER.	scientific article published in April 1991

Statements

scholarly article

1 reference

Europe PubMed Central

PMC publication ID

14 November 2017

The identification of proteins in the proximity of signal-anchor sequences during their targeting to and insertion into the membrane of the ER. (English)

1 reference

Europe PubMed Central

PMC publication ID

14 November 2017

1

1 reference

Europe PubMed Central

PMC publication ID

14 November 2017

4

object named as

Rapoport TA

1 reference

Europe PubMed Central

PMC publication ID

14 November 2017

author name string

Görlich D

2

1 reference

Europe PubMed Central

PMC publication ID

14 November 2017

Wiedmann M

3

1 reference

Europe PubMed Central

PMC publication ID

14 November 2017

Dobberstein B

5

1 reference

Europe PubMed Central

PMC publication ID

14 November 2017

language of work or name

0 references

publication date

1 April 1991

1 reference

Europe PubMed Central

PMC publication ID

14 November 2017

number of pages

10

1 reference

based on heuristic

inferred from page(s)

Journal of Cell Biology

1 reference

Europe PubMed Central

PMC publication ID

14 November 2017

113

1 reference

Europe PubMed Central

PMC publication ID

14 November 2017

1

1 reference

Europe PubMed Central

PMC publication ID

14 November 2017

35-44

1 reference

Europe PubMed Central

PMC publication ID

14 November 2017

Isolation of intracellular membranes by means of sodium carbonate treatment: application to endoplasmic reticulum

1 reference

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Secretion and membrane localization of proteins in Escherichia coli.

1 reference

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A novel in vitro transcription-translation system: accurate and efficient synthesis of single proteins from cloned DNA sequences.

1 reference

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Primary structure of human transferrin receptor deduced from the mRNA sequence

1 reference

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Multiple mechanisms of protein insertion into and across membranes.

1 reference

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Direct probing of the interaction between the signal sequence of nascent preprolactin and the signal recognition particle by specific cross-linking

1 reference

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Translation arrest by oligodeoxynucleotides complementary to mRNA coding sequences yields polypeptides of predetermined length

1 reference

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Signal recognition particle-dependent membrane insertion of mouse invariant chain: a membrane-spanning protein with a cytoplasmically exposed amino terminus

1 reference

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Signal and membrane anchor functions overlap in the type II membrane protein I gamma CAT.

1 reference

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Transcending the impenetrable: how proteins come to terms with membranes

1 reference

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Photocrosslinking of the signal sequence of nascent preprolactin to the 54-kilodalton polypeptide of the signal recognition particle

1 reference

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A signal sequence receptor in the endoplasmic reticulum membrane

1 reference

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Identification of signal sequence binding proteins integrated into the rough endoplasmic reticulum membrane

1 reference

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Mechanism of protein translocation across the endoplasmic reticulum membrane

1 reference

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The transmembrane segment of the human transferrin receptor functions as a signal peptide.

1 reference

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

1 reference

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25 May 2018

Evidence for the loop model of signal-sequence insertion into the endoplasmic reticulum

1 reference

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Integration of a small integral membrane protein, M2, of influenza virus into the endoplasmic reticulum: analysis of the internal signal-anchor domain of a protein with an ectoplasmic NH2 terminus

1 reference

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Each of the activities of signal recognition particle (SRP) is contained within a distinct domain: analysis of biochemical mutants of SRP.

1 reference

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Protein translocation across the endoplasmic reticulum membrane: identification by photocross-linking of a 39-kD integral membrane glycoprotein as part of a putative translocation tunnel

1 reference

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A tripartite structure of the signals that determine protein insertion into the endoplasmic reticulum membrane

1 reference

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Predicting the orientation of eukaryotic membrane-spanning proteins

1 reference

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25 May 2018

Photocrosslinking demonstrates proximity of a 34 kDa membrane protein to different portions of preprolactin during translocation through the endoplasmic reticulum

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2288910

25 May 2018

A membrane component of the endoplasmic reticulum that may be essential for protein translocation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2288910

25 May 2018

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

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2288910

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Access of proteinase K to partially translocated nascent polypeptides in intact and detergent-solubilized membranes

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2288910

25 May 2018

The signal sequence receptor has a second subunit and is part of a translocation complex in the endoplasmic reticulum as probed by bifunctional reagents

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2288910

25 May 2018

Structure and biosynthesis of the signal-sequence receptor

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2288910

25 May 2018

A nascent membrane protein is located adjacent to ER membrane proteins throughout its integration and translation

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2288910

25 May 2018

Requirements for the membrane insertion of signal-anchor type proteins

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2288910

25 May 2018

The 54-kD protein of signal recognition particle contains a methionine-rich RNA binding domain

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=2288910

25 May 2018

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/1848866

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Signal recognition particle mediates the insertion of a transmembrane protein which has a cytoplasmic NH2 terminus

1 reference

https://pubmed.ncbi.nlm.nih.gov/1848866

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1083/JCB.113.1.35

1 reference

Europe PubMed Central

PMC publication ID

14 November 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

14 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

14 November 2017

ResearchGate publication ID

0 references

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