Signal recognition particle-dependent membrane insertion of mouse invariant chain: a membrane-spanning protein with a cytoplasmically exposed amino terminus (Q41507439)

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scientific article published on June 1986

Language	Label	Description	Also known as
English	Signal recognition particle-dependent membrane insertion of mouse invariant chain: a membrane-spanning protein with a cytoplasmically exposed amino terminus	scientific article published on June 1986

Statements

scholarly article

1 reference

Europe PubMed Central

1 October 2017

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

1 reference

Europe PubMed Central

1 October 2017

author name string

Lipp J

1

1 reference

Europe PubMed Central

1 October 2017

Dobberstein B

2

1 reference

Europe PubMed Central

1 October 2017

language of work or name

0 references

publication date

1 June 1986

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Europe PubMed Central

1 October 2017

number of pages

7

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based on heuristic

inferred from page(s)

Journal of Cell Biology

1 reference

Europe PubMed Central

1 October 2017

102

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Europe PubMed Central

1 October 2017

6

1 reference

Europe PubMed Central

1 October 2017

2169-2175

1 reference

Europe PubMed Central

1 October 2017

The spontaneous insertion of proteins into and across membranes: the helical hairpin hypothesis

1 reference

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10 June 2018

Identification and characterization of a membrane component essential for the translocation of nascent proteins across the membrane of the endoplasmic reticulum

1 reference

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10 June 2018

Translocation of proteins across the endoplasmic reticulum III. Signal recognition protein (SRP) causes signal sequence-dependent and site-specific arrest of chain elongation that is released by microsomal membranes

1 reference

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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

1 reference

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Signal recognition protein is required for the integration of acetylcholine receptor delta subunit, a transmembrane glycoprotein, into the endoplasmic reticulum membrane

1 reference

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Structure of the neuraminidase gene in human influenza virus A/PR/8/34

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Membrane insertion and oligomeric assembly of HLA-DR histocompatibility antigens

1 reference

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Purification of a membrane-associated protein complex required for protein translocation across the endoplasmic reticulum

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Intracellular protein topogenesis

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The complete sequence of the mRNA for the HLA-DR-associated invariant chain reveals a polypeptide with an unusual transmembrane polarity

1 reference

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Structure of the murine Ia-associated invariant (Ii) chain as deduced from a cDNA clone.

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NH2-terminal hydrophobic region of influenza virus neuraminidase provides the signal function in translocation

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Protein translocation across the endoplasmic reticulum. II. Isolation and characterization of the signal recognition particle receptor

1 reference

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

1 reference

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Mechanisms of integration of de novo-synthesized polypeptides into membranes: signal-recognition particle is required for integration into microsomal membranes of calcium ATPase and of lens MP26 but not of cytochrome b5

1 reference

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Signal recognition particle contains a 7S RNA essential for protein translocation across the endoplasmic reticulum

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Pushing the signal hypothesis: what are the limits?

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Rat liver asialoglycoprotein receptor lacks a cleavable NH2-terminal signal sequence

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Primary structure of human transferrin receptor deduced from the mRNA sequence

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Multiple mechanisms of protein insertion into and across membranes.

1 reference

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A signal sequence for the insertion of a transmembrane glycoprotein. Similarities to the signals of secretory proteins in primary structure and function

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1 reference

https://pubmed.ncbi.nlm.nih.gov/3458708

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1 reference

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1 reference

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1 reference

https://pubmed.ncbi.nlm.nih.gov/3458708

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Direct evidence for the transmembrane orientation of the hepatic glycoprotein receptors

1 reference

https://pubmed.ncbi.nlm.nih.gov/3458708

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One gene encodes two distinct Ia-associated invariant chains

1 reference

https://pubmed.ncbi.nlm.nih.gov/3458708

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Signal recognition particle-dependent insertion of coronavirus E1, an intracellular membrane glycoprotein

1 reference

https://pubmed.ncbi.nlm.nih.gov/3458708

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Biochemical characterization of Ia antigens. I. Characterization of the 31K polypeptide associated with I-A subregion Ia antigens

1 reference

https://pubmed.ncbi.nlm.nih.gov/3458708

12 December 2020

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Identifiers

10.1083/JCB.102.6.2169

1 reference

Europe PubMed Central

1 October 2017

1 reference

Europe PubMed Central

1 October 2017

1 reference

Europe PubMed Central

1 October 2017

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