p24 and p23, the major transmembrane proteins of COPI-coated transport vesicles, form hetero-oligomeric complexes and cycle between the organelles of the early secretory pathway (Q28142237)

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scientific article (publication date: 26 March 1999)

Language	Label	Description	Also known as
English	p24 and p23, the major transmembrane proteins of COPI-coated transport vesicles, form hetero-oligomeric complexes and cycle between the organelles of the early secretory pathway	scientific article (publication date: 26 March 1999)

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scholarly article

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p24 and p23, the major transmembrane proteins of COPI-coated transport vesicles, form hetero-oligomeric complexes and cycle between the organelles of the early secretory pathway (English)

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transmembrane transport

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transmembrane protein

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author name string

D Gommel

1

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L Orci

2

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E M Emig

3

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M J Hannah

4

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M Ravazzola

5

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W Nickel

6

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J B Helms

7

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F T Wieland

8

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K Sohn

9

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language of work or name

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publication date

26 March 1999

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447

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2-3

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179-85

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'Coatomer': a cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles

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https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2900246-X

21 January 2018

ADP-Ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: A novel role for a GTP-binding protein

1 reference

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21 January 2018

ADP-ribosylation factor, a small GTP-binding protein, is required for binding of the coatomer protein beta-COP to Golgi membranes

1 reference

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21 January 2018

Coatomer interaction with di-lysine endoplasmic reticulum retention motifs

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21 January 2018

Retrieval of transmembrane proteins to the endoplasmic reticulum

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Coatomer is essential for retrieval of dilysine-tagged proteins to the endoplasmic reticulum

1 reference

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An integral membrane component of coatomer-coated transport vesicles defines a family of proteins involved in budding

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Bimodal interaction of coatomer with the p24 family of putative cargo receptors

1 reference

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A major transmembrane protein of Golgi-derived COPI-coated vesicles involved in coatomer binding

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gp25L/emp24/p24 protein family members of the cis-Golgi network bind both COP I and II coatomer

1 reference

https://api.crossref.org/works/10.1016%2FS0014-5793%2899%2900246-X

21 January 2018

Erv25p, a component of COPII-coated vesicles, forms a complex with Emp24p that is required for efficient endoplasmic reticulum to Golgi transport

1 reference

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21 January 2018

Involvement of the transmembrane protein p23 in biosynthetic protein transport

1 reference

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21 January 2018

p23, a major COPI-vesicle membrane protein, constitutively cycles through the early secretory pathway

1 reference

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Pre- and post-Golgi vacuoles operate in the transport of Semliki Forest virus membrane glycoproteins to the cell surface

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A new type of coated vesicular carrier that appears not to contain clathrin: its possible role in protein transport within the Golgi stack

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Tight control of gene expression in mammalian cells by tetracycline-responsive promoters

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A coat subunit of Golgi-derived non-clathrin-coated vesicles with homology to the clathrin-coated vesicle coat protein beta-adaptin.

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A RAPID METHOD OF TOTAL LIPID EXTRACTION AND PURIFICATION

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Two dimensional then layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots

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Identification, by a monoclonal antibody, of a 53-kD protein associated with a tubulo-vesicular compartment at the cis-side of the Golgi apparatus

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Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product

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Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa

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The absence of Emp24p, a component of ER-derived COPII-coated vesicles, causes a defect in transport of selected proteins to the Golgi.

1 reference

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7 January 2021

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10.1016/S0014-5793(99)00246-X

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