Disulfide Bond Formation and N-Glycosylation Modulate Protein-Protein Interactions in GPI-Transamidase (GPIT).

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Disulfide Bond Formation and N-Glycosylation Modulate Protein-Protein Interactions in GPI-Transamidase (GPIT).

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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 04 April 2017

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vedecký článok

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vetenskaplig artikel

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vědecký článek

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Disulfide Bond Formation and N ...... ns in GPI-Transamidase (GPIT).

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Disulfide Bond Formation and N ...... teractions in GPI-Transamidase

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Disulfide Bond Formation and N ...... ns in GPI-Transamidase (GPIT).

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Disulfide Bond Formation and N ...... teractions in GPI-Transamidase

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Disulfide Bond Formation and N ...... ns in GPI-Transamidase (GPIT).

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Disulfide Bond Formation and N ...... teractions in GPI-Transamidase

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P1476

Disulfide Bond Formation and N ...... ons in GPI-Transamidase (GPIT)

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Hao Wu

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

Lina Yi

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Qiubai Li

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

Stanley Lo

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Gaa1p and gpi8p are components of a glycosylphosphatidylinositol (GPI) transamidase that mediates attachment of GPI to proteins

PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8

Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and PIG-T, form a functionally important intermolecular disulfide bridge

Structural requirements for the recruitment of Gaa1 into a functional glycosylphosphatidylinositol transamidase complex

A conserved proline in the last transmembrane segment of Gaa1 is required for glycosylphosphatidylinositol (GPI) recognition by GPI transamidase

Human PIG-U and yeast Cdc91p are the fifth subunit of GPI transamidase that attaches GPI-anchors to proteins

Yeast Gpi8p is essential for GPI anchor attachment onto proteins

The structures of caspases-1, -3, -7 and -8 reveal the basis for substrate and inhibitor selectivity

Gpi17p does not stably interact with other subunits of glycosylphosphatidylinositol transamidase in Saccharomyces cerevisiae.

Deficiencies in the endoplasmic reticulum (ER)-membrane protein Gab1p perturb transfer of glycosylphosphatidylinositol to proteins and cause perinuclear ER-associated actin bar formation

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srep45912

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45912

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scholarly article

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10.1038/SREP45912

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English

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

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Gunes Bozkurt

Anant K Menon

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2017-04-04T00:00:00Z

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28374821

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glycosylation

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5379210

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