(Q40700330)

English

Palmitoylation-defective asialoglycoprotein receptors are normal in their cellular distribution and ability to bind ligand, but are defective in ligand uptake and degradation.

scientific article published on October 2002

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scholarly article

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12359251%20AND%20SRC:MED&resulttype=core&format=json

13 December 2019

Palmitoylation-defective asialoglycoprotein receptors are normal in their cellular distribution and ability to bind ligand, but are defective in ligand uptake and degradation (English)

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12359251%20AND%20SRC:MED&resulttype=core&format=json

13 December 2019

1

1 reference

Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12359251%20AND%20SRC:MED&resulttype=core&format=json

13 December 2019

author name string

Amit Saxena

2

1 reference

Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12359251%20AND%20SRC:MED&resulttype=core&format=json

13 December 2019

Janet A Weigel

3

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12359251%20AND%20SRC:MED&resulttype=core&format=json

13 December 2019

Paul H Weigel

4

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12359251%20AND%20SRC:MED&resulttype=core&format=json

13 December 2019

publication date

1 October 2002

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12359251%20AND%20SRC:MED&resulttype=core&format=json

13 December 2019

Biochemical and Biophysical Research Communications

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12359251%20AND%20SRC:MED&resulttype=core&format=json

13 December 2019

297

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12359251%20AND%20SRC:MED&resulttype=core&format=json

13 December 2019

4

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12359251%20AND%20SRC:MED&resulttype=core&format=json

13 December 2019

980-986

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:12359251%20AND%20SRC:MED&resulttype=core&format=json

13 December 2019

Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins

1 reference

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7 January 2021

Palmitoylation: a post-translational modification that regulates signalling from G-protein coupled receptors

1 reference

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7 January 2021

Fatty acylated proteins as components of intracellular signaling pathways

1 reference

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7 January 2021

Fatty acylation of proteins

1 reference

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7 January 2021

The asialoglycoprotein receptor: a model for endocytic transport receptors

1 reference

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7 January 2021

The asialoglycoprotein receptor: relationships between structure, function, and expression

1 reference

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7 January 2021

Glycans as endocytosis signals: the cases of the asialoglycoprotein and hyaluronan/chondroitin sulfate receptors

1 reference

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7 January 2021

Sequence of a second human asialoglycoprotein receptor: conservation of two receptor genes during evolution

1 reference

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7 January 2021

Asialoglycoprotein receptor deficiency in mice lacking the major receptor subunit. Its obligate requirement for the stable expression of oligomeric receptor.

1 reference

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7 January 2021

A novel cycle involving fatty acyl-coenzyme A regulates asialoglycoprotein receptor activity in permeable hepatocytes

1 reference

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7 January 2021

Fatty acylation of the rat and human asialoglycoprotein receptors. A conserved cytoplasmic cysteine residue is acylated in all receptor subunits

1 reference

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7 January 2021

The human asialoglycoprotein receptor is palmitoylated and fatty deacylation causes inactivation of state 2 receptors

1 reference

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7 January 2021

Fatty acylation of the rat asialoglycoprotein receptor. The three subunits from active receptors contain covalently bound palmitate and stearate

1 reference

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7 January 2021

The minor subunit splice variants, H2b and H2c, of the human asialoglycoprotein receptor are present with the major subunit H1 in different hetero-oligomeric receptor complexes

1 reference

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7 January 2021

Nonpalmitoylated human asialoglycoprotein receptors recycle constitutively but are defective in coated pit-mediated endocytosis, dissociation, and delivery of ligand to lysosomes

1 reference

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7 January 2021

THE ATTRACTIONS OF PROTEINS FOR SMALL MOLECULES AND IONS

1 reference

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7 January 2021

A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

1 reference

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7 January 2021

“Western Blotting”: Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A

1 reference

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7 January 2021

Hydroxylamine treatment differentially inactivates purified rat hepatic asialoglycoprotein receptors and distinguishes two receptor populations

1 reference

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7 January 2021

H2, the minor subunit of the human asialoglycoprotein receptor, trafficks intracellularly and forms homo-oligomers, but does not bind asialo-orosomucoid

1 reference

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7 January 2021

Surface and internal galactosyl receptors are heterooligomers and retain this structure after ligand internalization or receptor modulation

1 reference

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7 January 2021

Hypertonic media inhibit receptor-mediated endocytosis by blocking clathrin-coated pit formation

1 reference

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7 January 2021

SK HEP-1: a human cell line of endothelial origin

1 reference

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7 January 2021

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