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

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2 September 2017

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

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Europe PubMed Central

2 September 2017

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Blobel G

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Europe PubMed Central

2 September 2017

Gilmore R

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Europe PubMed Central

PubMed ID

2992801

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2 September 2017

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English

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1 September 1985

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Europe PubMed Central

2 September 2017

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Europe PubMed Central

2 September 2017

42

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Europe PubMed Central

2 September 2017

497-505

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Europe PubMed Central

2 September 2017

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Europe PubMed Central

2 September 2017

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

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

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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

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Selective solubilization of proteins from red blood cell membranes by protein perturbants.

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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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Studies on polysome-membrane interactions in mouse myeloma cells.

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Transient involvement of signal recognition particle and its receptor in the microsomal membrane prior to protein translocation.

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Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma

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A receptor for single segments of secretory proteins in rough endoplasmic reticulum 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

1 reference

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Partial resistance of nascent polypeptide chains to proteolytic digestion due to ribosomal shielding.

1 reference

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Ribosome-membrane interaction. Nondestructive disassembly of rat liver rough microsomes into ribosomal and membranous components

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10.1016/0092-8674(85)90107-2

1 reference

stated in

Europe PubMed Central

2 September 2017

1 reference

Europe PubMed Central

PubMed ID

2992801

retrieved

2 September 2017

(Q38352117)

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

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