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Literature DB >> 27905422

Cell biology: Sort of unexpected.

Martin R Pool¹.

Abstract

Mesh：
Humans
Protein Transport

Year: 2016 PMID： 27905422 DOI： 10.1038/540045a

Source DB: PubMed Journal: Nature ISSN： 0028-0836 Impact factor: 49.962

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16 in total

1. Different effects of Sec61α, Sec62 and Sec63 depletion on transport of polypeptides into the endoplasmic reticulum of mammalian cells.

Authors: Sven Lang; Julia Benedix; Sorin V Fedeles; Stefan Schorr; Claudia Schirra; Nico Schäuble; Carolin Jalal; Markus Greiner; Sarah Hassdenteufel; Jörg Tatzelt; Birgit Kreutzer; Ludwig Edelmann; Elmar Krause; Jens Rettig; Stefan Somlo; Richard Zimmermann; Johanna Dudek
Journal: J Cell Sci Date: 2012-02-28 Impact factor: 5.285

2. Signal sequences. The limits of variation.

Authors: G von Heijne
Journal: J Mol Biol Date: 1985-07-05 Impact factor: 5.469

Review 3. Fidelity of cotranslational protein targeting by the signal recognition particle.

Authors: Xin Zhang; Shu-ou Shan
Journal: Annu Rev Biophys Date: 2014 Impact factor: 12.981

4. The SND proteins constitute an alternative targeting route to the endoplasmic reticulum.

Authors: Naama Aviram; Tslil Ast; Elizabeth A Costa; Eric C Arakel; Silvia G Chuartzman; Calvin H Jan; Sarah Haßdenteufel; Johanna Dudek; Martin Jung; Stefan Schorr; Richard Zimmermann; Blanche Schwappach; Jonathan S Weissman; Maya Schuldiner
Journal: Nature Date: 2016-11-30 Impact factor: 49.962

5. Principles of ER cotranslational translocation revealed by proximity-specific ribosome profiling.

Authors: Calvin H Jan; Christopher C Williams; Jonathan S Weissman
Journal: Science Date: 2014-11-06 Impact factor: 47.728

6. Efficient secretion of small proteins in mammalian cells relies on Sec62-dependent posttranslational translocation.

Authors: Asvin K K Lakkaraju; Ratheeshkumar Thankappan; Camille Mary; Jennifer L Garrison; Jack Taunton; Katharina Strub
Journal: Mol Biol Cell Date: 2012-05-30 Impact factor: 4.138

7. Signal sequences specify the targeting route to the endoplasmic reticulum membrane.

Authors: D T Ng; J D Brown; P Walter
Journal: J Cell Biol Date: 1996-07 Impact factor: 10.539

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

Authors: G Blobel; B Dobberstein
Journal: J Cell Biol Date: 1975-12 Impact factor: 10.539

Cell biology: Sort of unexpected.

1. Different effects of Sec61α, Sec62 and Sec63 depletion on transport of polypeptides into the endoplasmic reticulum of mammalian cells.

2. Signal sequences. The limits of variation.

Review 3. Fidelity of cotranslational protein targeting by the signal recognition particle.

4. The SND proteins constitute an alternative targeting route to the endoplasmic reticulum.

5. Principles of ER cotranslational translocation revealed by proximity-specific ribosome profiling.

6. Efficient secretion of small proteins in mammalian cells relies on Sec62-dependent posttranslational translocation.

7. Signal sequences specify the targeting route to the endoplasmic reticulum membrane.

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

9. Cotranslational signal-independent SRP preloading during membrane targeting.

10. SEC62 encodes a putative membrane protein required for protein translocation into the yeast endoplasmic reticulum.

1. An alternative pathway for membrane protein biogenesis at the endoplasmic reticulum.

2. Multiple pathways facilitate the biogenesis of mammalian tail-anchored proteins.