Interaction among Saccharomyces cerevisiae pheromone receptors during endocytosis. - Wikidata - wikimedia - TriplyDB

Interaction among Saccharomyces cerevisiae pheromone receptors during endocytosis.

Interaction among Saccharomyces cerevisiae pheromone receptors during endocytosis.

http://www.wikidata.org/entity/Q37706178

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The C-terminal region of the yeast monocarboxylate transporter Jen1 acts as a glucose signal-responding degron recognized by the α-arrestin Rod1

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Interaction among Saccharomyces cerevisiae pheromone receptors during endocytosis.

http://www.wikidata.org/entity/Q37706178

description

article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 15 April 2014

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Interaction among Saccharomyces cerevisiae pheromone receptors during endocytosis.

@en

Interaction among Saccharomyces cerevisiae pheromone receptors during endocytosis.

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type

label

Interaction among Saccharomyces cerevisiae pheromone receptors during endocytosis.

@en

Interaction among Saccharomyces cerevisiae pheromone receptors during endocytosis.

@nl

prefLabel

Interaction among Saccharomyces cerevisiae pheromone receptors during endocytosis.

@en

Interaction among Saccharomyces cerevisiae pheromone receptors during endocytosis.

@nl

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Interaction among Saccharomyces cerevisiae pheromone receptors during endocytosis.

@en

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Chien-I Chang

http://www.w3.org/2001/XMLSchema#string

Duane D Jenness

http://www.w3.org/2001/XMLSchema#string

Kimberly A Schandel

http://www.w3.org/2001/XMLSchema#string

P2860

Dominant-negative mutations in the G-protein-coupled alpha-factor receptor map to the extracellular ends of the transmembrane segments.

Regulation of GPCR activity, trafficking and localization by GPCR-interacting proteins.

Dominant negative mutations in the alpha-factor receptor, a G protein-coupled receptor encoded by the STE2 gene of the yeast Saccharomyces cerevisiae.

G-protein-coupled receptors function as oligomers in vivo.

Yeast mutants affecting possible quality control of plasma membrane proteins.

Identification of a novel sequence mediating regulated endocytosis of the G protein-coupled alpha-pheromone receptor in yeast.

Homo-oligomeric complexes of the yeast alpha-factor pheromone receptor are functional units of endocytosis.

Changes in conformation at the cytoplasmic ends of the fifth and sixth transmembrane helices of a yeast G protein-coupled receptor in response to ligand binding.

The significance of G protein-coupled receptor crystallography for drug discovery.

Cytoplasmic tail phosphorylation of the alpha-factor receptor is required for its ubiquitination and internalization

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297-306

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scholarly article

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10.1242/BIO.20146866

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4

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3

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2014-04-15T00:00:00Z

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261220853

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24682008

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Saccharomyces cerevisiae

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3988799

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